Cytokines

Interleukin 16 (IL-16), also known as lymphocyte chemoattractant factor (LCF), refers to the C-terminal peptide of  pro-IL-16 isoform 1, which is a nuclear and cytoplasmic PDZ-containing protein. The C-terminus of pro-IL-16 is cleaved by Caspase-3, resulting in the release of secreted IL-16. Mature IL-16 has been shown to bind the cell surface receptor CD4 and functions as an immunomodulatory cytokine.   Product Properties Synonyms Lymphocyte chemoattractant factor , LCF Accession O54824 GeneID 16170 Source E.coli-derived Mouse IL-16, Ser1205-Ser1322. Molecular Weight Approximately 12.2 kDa. AA Sequence SAASASAASD ISVESKEATV CTVTLEKTSA GLGFSLEGGK GSLHGDKPLT INRIFKGTEQ GEMVQPGDEI LQLAGTAVQG LTRFEAWNVI KALPDGPVTI VIRRTSLQCK QTTASADS Tag None Physical Appearance Sterile Filtered White lyophilized (freeze-dried) powder. Purity > 98% by SDS-PAGE and HPLC analyses. Biological Activity The biological activity determined by a chemotaxis bioassay using human peripheral T lymphocytes is in a concentration range of 1.0-100 ng/ml. Fully biologically active when compared to standard. Endotoxin < 1.0 EU per 1μg of the protein by the LAL method. Formulation Lyophilized from a 0.2 μm filtered concentrated solution in 1 × PBS, pH 7.4. Reconstitution We recommend that this vial be briefly centrifuged prior to opening to bring the contents to the bottom. Reconstitute in sterile distilled water or aqueous buffer containing 0.1% BSA to a concentration of 0.1-1.0mg/mL. Stock solutions should be apportioned into working aliquots and stored at ≤ -20℃. Further dilutions should be made in appropriate buffered solutions.   Shipping and Storage The products are shipped with ice pack and can be stored at -20℃ to -80℃ for 1 year. Recommend to aliquot the protein into smaller quantities when first used and avoid repeated freeze-thaw cycles.   Cautions 1. Avoid repeated freeze-thaw cycles. 2. For your safety and health, please wear lab coats and disposable gloves for operation. 3. For research use only!

Read more less

Interleukin 19 (IL-19) is a member of the IL-10 family of cytokines. The IL-10 family is a class II alpha -helical collection of cytokines that contains two groups, a viral homolog and a cellular homolog group. Within the cellular homolog group, there are two additional groupings, one which uses IL-10 R2 as a signal transducing receptor (IL-10, IL-22 and IL-26), and one which uses IL-20 R2 as a signal transducing receptor (IL-19, IL-20 and IL-24). Mouse IL-19 is synthesized as a 176 amino acid (aa) precursor that contains a 24 aa signal sequence and a 152 aa mature region. Based on human studies, it is expected to be secreted as a glycosylated monomer, 35 - 45 kDa in size. IL-19 is unusual in that it contains seven amphipathic helices. Mature mouse IL-19 shares 69% aa sequence identity with the mature human IL-19, and 85% and 68% aa identity to unpublished Genbank sequences for rat and canine IL-19, respectively. Although mouse IL-19 is active on human cells, human IL-19 is not active on mouse cells. IL-19 expression is limited to activated keratinocytes and monocytes, with a possible contribution from B cells. IL-19 binds a receptor  complex consisting of the IL-20 receptor alpha (also known as IL-20 R1) and the IL-20 receptor beta (IL-20 R2). This receptor complex is  also shared by IL-20 and IL-24. Notably, IL-19 is reported to actually bind to IL-20 R2, which is generally considered to be only the signal transducing receptor subunit. Functionally, it has been reported that IL-19 both will and will not induce IL-6 and TNF production by monocytes. It does, however, seem to drive T-helper cell differentiation towards a Th2 response, inducing both IL-10 and production of itself .   Product Properties Synonyms IL-10C; IL19; MDA1 Accession Q8CJ70 GeneID 329244 Source E.coli-derived Mouse IL-19, Leu25-Ala176. Molecular Weight Approximately 17.6 kDa. AA Sequence LRRCLISVDM RLIEKSFHEI KRAMQTKDTF KNVTILSLEN LRSIKPGDVC CMTNNLLTFY RDRVFQDHQE RSLEVLRRIS SIANSFLCVQ KSLERCQVHR QCNCSQEATN ATRIIHDNYN QLEVSSAALK SLGELNILLA WIDRNHLETP AA Tag None Physical Appearance Sterile Filtered White lyophilized (freeze-dried) powder. Purity > 97% by SDS-PAGE and HPLC analyses. Biological Activity The ED50 as determined by a cell proliferation assay using human IL-20Rα and human IL-20Rβ co-transfected murine BaF3 pro-B cells is less than 0.8 ng/mL, corresponding to a specific activity of >1.25 × 106 IU/mg. Fully biologically active when compared to standard. Endotoxin < 1.0 EU per 1μg of the protein by the LAL method. Formulation Lyophilized from a 0.2 μm filtered concentrated solution in 1 × PBS, pH 7.4 , with 3 % Trehalose. Reconstitution We recommend that this vial be briefly centrifuged prior to opening to bring the contents to the bottom. Reconstitute in sterile distilled water or aqueous buffer containing 0.1% BSA to a concentration of 0.1-1.0 mg/mL. Stock solutions should be apportioned into working aliquots and stored at ≤ -20°C. Further dilutions should be made in appropriate buffered solutions.   Shipping and Storage The products are shipped with ice pack and can be stored at -20℃ to -80℃ for 1 year. Recommend to aliquot the protein into smaller quantities when first used and avoid repeated freeze-thaw cycles.   Cautions 1. Avoid repeated freeze-thaw cycles. 2. For your safety and health, please wear lab coats and disposable gloves for operation. 3. For research use only!

Read more less

Interleukin-2(IL-2) is a powerful immunoregulatory lymphokine produced by T-cells in response to antigenic or mitogenic stimulation. It is expressed by CD4+ and CD8+ T cells, γδ T cells, B cells, dendritic cells, and eosinophils. IL-2/IL-2R signaling is required for T- cell proliferation and other fundamental functions which are essential for the immune response. The receptor for IL-2 consists of three subunits (55 kDa IL-2Rα, 75 kDa IL-2Rβ, and 64 kDa common gamma chain γc/IL-2Rγ) that are present on the cell surface in varying preformed complexes. Mature human IL-2 shares 56% and 66% amino acid sequence identity with mouse and rat IL-2, respectively. Human and mouse IL-2 exhibit cross-species activity.   Product Properties Synonyms Interleukin-2,IL-2,T-cell Growth Factor, TCGF, Aldesleukin Accession P04351 GeneID 16183 Source E.coli-derived mouse IL-2 protein, Ala21-Gln169 Molecular Weight Approximately 17.2 kDa. AA Sequence APTSSSTSSS TAEAQQQQQQ QQQQQQHLEQ LLMDLQELLS RMENYRNLKL PRMLTFKFYL PKQATELKDL QCLEDELGPL RHVLDLTQSK SFQLEDAENF ISNIRVTVVK LKGSDNTFEC QFDDESATVV DFLRRWIAFC QSIISTSPQ Tag None Physical Appearance Sterile Filtered White lyophilized (freeze-dried) powder. Purity > 95% by SDS-PAGE and HPLC analyses. Biological Activity The ED50 as determined by a cell proliferation assay using murine CTLL-2 cells is less than 0.2 ng/mL, corresponding to a specific activity of > 5.0 × 106 IU/mg. Fully biologically active when compared to standard. Endotoxin < 1.0 EU per 1μg of the protein by the LAL method. Formulation Lyophilized from a 0.2 μm filtered concentrated solution in 1 × PBS, pH 7.4. Reconstitution We recommend that this vial be briefly centrifuged prior to opening to bring the contents to the bottom. Reconstitute in sterile distilled water or aqueous buffer containing 0.1% BSA to a concentration of 0.1-1.0 mg/mL. Stock solutions should be apportioned into working aliquots and stored at ≤ -20°C. Further dilutions should be made in appropriate buffered solutions.   Shipping and Storage The products are shipped with ice pack and can be stored at -20 ℃ for 1 year. 1 month, 2 to 8 °C under sterile conditions after reconstitution. 3 months, -20 °C under sterile conditions after reconstitution. Recommend to aliquot the protein into smaller quantities when first used and avoid repeated freeze-thaw cycles.   Cautions 1. Avoid repeated freeze-thaw cycles. 2. For your safety and health, please wear lab coats and disposable gloves for operation. 3. For research use only!

Read more less

Interleukin-21 (IL-21) is an approximately 14 kDa four-helix-bundle cytokine in the family of cytokines that utilize the common gamma chain (gamma c) as a receptor subunit. Mature mouse IL-21 shares 66%, 59%, 58%, and 88% aa sequence identity with mature canine, human, rabbit, and rat IL-21, respectively. It can induce target cells division or proliferation. IL-21 elicits its effect through binding to IL-21R. IL-21 is a type I cytokine whose receptor is expressed on T, B, and NK cells. Within the B cell lineage, IL-21 regulates IgG1 production and cooperates with IL-4 for the production of multiple Ab classes in vivo. IL-21 has a significant influence on the regulation of B cell function in vivo and cooperates with IL-4. Additionally, IL-21 promoted tumor-specific CTL activity and enhanced memory responses to tumor rechallenge.   Product Properties Synonyms CVID11, IL21, IL-21, interleukin 21, Za11 Accession Q9ES17 GeneID 60505 Source E.coli-derived mouse IL-21 protein, His18-Ser146 Molecular Weight Approximately 15.0 kDa. AA Sequence HKSSPQGPDR LLIRLRHLID IVEQLKIYEN DLDPELLSAP QDVKGHCEHA AFACFQKAKL KPSNPGNNKT FIIDLVAQLR RRLPARRGGK KQKHIAKCPS CDSYEKRTPK EFLERLKWLL QKMIHQHLS Tag None Physical Appearance Sterile Filtered White lyophilized (freeze-dried) powder. Purity > 98% by SDS-PAGE and HPLC analyses. Biological Activity The ED50 as determined by a cell proliferation assay using human N1186 T cells is less than 25 ng/mL, corresponding to a specific activity of > 4.0 × 104 IU/mg. Fully biologically active when compared to standard. Endotoxin < 1.0 EU per 1μg of the protein by the LAL method. Formulation Lyophilized from a 0.2 μm filtered concentrated solution in 2 × PBS, pH 7.4. Reconstitution We recommend that this vial be briefly centrifuged prior to opening to bring the contents to the bottom. Reconstitute in sterile distilled water or aqueous buffer containing 0.1% BSA to a concentration of 0.1-1.0 mg/mL. Stock solutions should be apportioned into working aliquots and stored at ≤ -20°C. Further dilutions should be made in appropriate buffered solutions.   Shipping and Storage The products are shipped with ice pack and can be stored at -20℃ to -80℃ for 1 year. Recommend to aliquot the protein into smaller quantities when first used and avoid repeated freeze-thaw cycles.   Cautions 1. Avoid repeated freeze-thaw cycles. 2. For your safety and health, please wear lab coats and disposable gloves for operation. 3. For research use only!

Read more less

Interleukin 3 is a pleiotropic factor produced primarily by activated T cells that can stimulate the proliferation. At the amino acid sequence level, mature human and mouse IL-3 share only 29% sequence identity. Consistent with this lack of homology, IL-3 activity is highly species-specific and human IL-3 does not show activity on murine cells. Cytokines are actively involved in the host-defense system to coordinate the functional activity and the generation of effector cells. Some of these molecules function as inflammatory mediators and hematopoietic growth factors at the same time such as IL-3. IL-3 is known as a pleiotropic cytokine with a broad spectrum of target cells and functions. IL-3 regulates the proliferation and differentiation of normal hematopoietic progenitor cells in the early stages of hematopoiesis. And IL-3 inhibits apoptosis and promotes the autonomous growth of blast cells.   Product Properties Synonyms Interleukin-3, IL-3, Hematopoietic growth factor, MCGF, Multipotential colony-stimulating factor, P-cell-stimulating factor Accession P01586 GeneID 16187 Source E.coli-derived mouse IL-1alpha protein, Asp33-Cys166. Molecular Weight Approximately 14.8 kDa. AA Sequence DTHRLTRTLN CSSIVKEIIG KLPEPELKTD DEGPSLRNKS FRRVNLSKFV ESQGEVDPED RYVIKSNLQK LNCCLPTSAN DSALPGVFIR DLDDFRKKLR FYMVHLNDLE TVLTSRPPQP ASGSVSPNRG TVEC Tag None Physical Appearance Sterile Filtered White lyophilized (freeze-dried) powder. Purity > 98% by SDS-PAGE and HPLC analyses. Biological Activity The ED50 as determined by the dose-dependent stimulation of the proliferation of murine M-NFS-60 cells is less than 0.05 ng/mL, corresponding to a specific activity of > 2 × 107  IU/mg. Fully biologically active when compared to standard. Endotoxin < 1.0 EU per 1μg of the protein by the LAL method. Formulation Lyophilized from a 0.2 μm filtered concentrated solution in PBS, pH 7.4. Reconstitution We recommend that this vial be briefly centrifuged prior to opening to bring the contents to the bottom. Reconstitute in sterile distilled water or aqueous buffer containing 0.1% BSA to a concentration of 0.1-1.0 mg/mL. Stock solutions should be apportioned into working aliquots and stored at ≤ -20°C. Further dilutions should be made in appropriate buffered solutions.   Shipping and Storage The products are shipped with ice pack and can be stored at -20 ℃ for 1 year. 1 month, 2 to 8 °C under sterile conditions after reconstitution. 3 months, -20 °C under sterile conditions after reconstitution. Recommend to aliquot the protein into smaller quantities when first used and avoid repeated freeze-thaw cycles.   Cautions 1. Avoid repeated freeze-thaw cycles. 2. For your safety and health, please wear lab coats and disposable gloves for operation. 3. For research use only!

Read more less

IL-33, also known as NF-HEV and DVS 27, is a 17.5 kDa proinflammatory protein that may also regulate gene transcription. DVS  27 was identifed as a gene that is up- regulated in vasospastic cerebral arteries. NF-HEV was described as a nuclear factor that is preferentially expressed in the endothelial cells of high endothelial venules relative to endothelial cells from other tissues. IL-33 was identified based on sequence and structural homology with IL-1 family cytokines. DVS 27, NF-HEV, and IL-33 share 100% amino acid sequence identity. IL-33 is constitutively expressed in smooth muscle and airway epithelia. It is up- regulated in arterial smooth muscle, dermal fibroblasts, and keratinocytes following IL-1 alpha or IL- 1 beta stimulation. Similar to IL-1, IL-33 can be cleaved in vitro by caspase- 1, generating an N- terminal fragment that is slightly shorter than the C- terminal fragment. The N- terminal portion of full length IL-33 contains a predicted bipartite nuclear localization sequence and a homeodomain-like helix-turn-helix DNA binding domain. By immunofluorescence, full length IL-33 localizes to the nucleus in HUVECs and transfectants. The C- terminal fragment, corresponding to mature IL-33, binds and triggers signaling through mast cell IL- 1 R4/ST2L, a longtime orphan receptor involved in the augmentation of Th2 cell responses. A ternary signaling complex is formed by the subsequent association of IL-33 and ST2L with IL- 1 RAcP. Stimulation of Th2 polarized lymphocytes with mature IL-33 in vitro  induces  IL-5  and  IL-13  secretion. In vivo administration of mature IL-33 promotes increased production of IL-5, IL-13, IgE, and IgA, as well as splenomegaly and inflammatory infiltration of mucosal tissues. Full length and mature mouse IL-33 share approximately 55% and 90% aa sequence identity with human and rat IL-33, respectively. Mouse IL-33 shares less than 25% aa sequence identity with other IL-1 family proteins.   Product Properties Synonyms IL-1F11, NF-HEV Accession Q8BVZ5 GeneID 77125 Source E.coli-derived Mouse IL-33, Ser109-Ile266. Molecular Weight Approximately 17.5 kDa. AA Sequence SIQGTSLLTQ SPASLSTYND QSVSFVLENG CYVINVDDSG KDQEQDQVLL RYYESPCPAS QSGDGVDGKK LMVNMSPIKD TDIWLHANDK DYSVELQRGD VSPPEQAFFV LHKKSSDFVS FECKNLPGTY IGVKDNQLAL VEEKDESCNN IMFKLSKI Tag None Physical Appearance Sterile Filtered White lyophilized (freeze-dried) powder. Purity > 98% by SDS-PAGE and HPLC analyses. Biological Activity The ED50 as determined by a cell proliferation assay using murine D10S cells is less than 0.5 ng/mL, corresponding to a specific activity of > 2.0 × 106 IU/mg. Fully biologically active when compared to standard. Endotoxin < 1.0 EU per 1μg of the protein by the LAL method. Formulation Lyophilized from a 0.2 µm filtered solution in PBS, and 1 mM EDTA. Reconstitution We recommend that this vial be briefly centrifuged prior to opening to bring the contents to the bottom. Reconstitute in sterile distilled water or aqueous buffer containing 0.1% BSA to a concentration of 0.1-1.0 mg/mL. Stock solutions should be apportioned into working aliquots and stored at ≤ -20°C. Further dilutions should be made in appropriate buffered solutions.   Shipping and Storage The products are shipped with ice pack and can be stored at -20℃ to -80℃ for 1 year. Recommend to aliquot the protein into smaller quantities when first used and avoid repeated freeze-thaw cycles.   Cautions 1. Avoid repeated freeze-thaw cycles. 2. For your safety and health, please wear lab coats and disposable gloves for operation. 3. For research use only!

Read more less

IL- 36 alpha, previously called IL- 1F6 and FIL1 epsilon (family of IL- 1 member epsilon), is a member of the IL- 1 family which includes IL- 1 beta, IL- 1 alpha, IL- 1ra, IL- 18, and novel family members IL- 36 Ra (IL- 1F5), IL- 36 beta (IL- 1F8), IL- 36 gamma (IL- 1F9), IL- 37 (IL- 1F7) and IL- 1F10. All family members show a 12 beta - strand, beta - trefoil configuration, and are believed to have arisen from a common ancestral gene. It can be externalized non- specifically in response to LPS and ATP- induced activation of the P2X7 receptor. Full- length recombinant IL- 36 alpha is less active than endogenous IL- 36 alpha, but trimming of the N- termini enhances its activity. Mouse IL- 36 alpha shares 83% aa sequence identity with rat IL- 36 alpha, 54- 60% with human, rabbit, equine and bovine IL- 36 alpha, and 27- 57% aa sequence identity with other novel IL- 1 family members. IL- 36 alpha is mainly found in skin and lymphoid tissues, but also in fetal brain, trachea, stomach and intestine. It is expressed by monocytes, B and T cells. The receptor for IL- 36 alpha is a combination of IL- 1 Rrp2 (also called IL- 1 RL2 or IL- 1 R6), mainly found in epithelia and keratinocytes, and the widely expressed IL- 1 RAcP. IL- 36 alpha, beta and gamma all activate NF- kappa B and MAPK pathways in an IL- 1 Rrp2 dependent manner, and induce production of inflammatory cytokines and chemokines such as CXCL8/IL- 8. IL- 36 alpha and other family members are overexpressed in psoriatic skin lesions, and transgenic overexpression of IL- 36 alpha in skin keratinocytes produces epidermal hyperplasia. IL- 36 alpha is present in kidney tubule epithelia; it is highly overexpressed in tubulointerstitial lesions in mouse models of chronic glomerulonephritis, lupus nephritis and diabetic nephritis. IL- 36 alpha is induced by inflammation in adipose tissue- resident alternately activated (M2) macrophages, and reduces adipocyte differentiation.   Product Properties Synonyms FIL1 epsilon, IL-1 epsilon, IL-1F6, IL-1H1 Accession Q9JLA2 GeneID 54448 Source E.coli-derived Mouse IL-36α,153aa, Arg8-His160. Molecular Weight Approximately 17.1 kDa. AA Sequence RAASPSLRHV QDLSSRVWIL QNNILTAVPR KEQTVPVTIT LLPCQYLDTL ETNRGDPTYM GVQRPMSCLF CTKDGEQPVL QLGEGNIMEM YNKKEPVKAS LFYHKKSGTT STFESAAFPG WFIAVCSKGS CPLILTQELG EIFITDFEMI VVH Tag None Physical Appearance Sterile Filtered White lyophilized (freeze-dried) powder. Purity > 95% by SDS-PAGE and HPLC analyses. Biological Activity The ED50 as determined by inducing IL-6 secretion in murine NIH/3T3 cells is less than 25 ng/mL, corresponding to a specific activity of > 4.0 × 104 IU/mg. Fully biologically active when compared to standard. Endotoxin < 1.0 EU per 1μg of the protein by the LAL method. Formulation Lyophilized from a 0.2 μm filtered concentrated solution in PBS, 1 mM DTT, 3 % trehalose. Reconstitution We recommend that this vial be briefly centrifuged prior to opening to bring the contents to the bottom. Reconstitute in sterile distilled water or aqueous buffer containing 0.1% BSA to a concentration of 0.1-1.0 mg/mL. Stock solutions should be apportioned into working aliquots and stored at ≤ -20°C. Further dilutions should be made in appropriate buffered solutions.   Shipping and Storage The products are shipped with ice pack and can be stored at -20℃ to -80℃ for 1 year. Recommend to aliquot the protein into smaller quantities when first used and avoid repeated freeze-thaw cycles.   Cautions 1. Avoid repeated freeze-thaw cycles. 2. For your safety and health, please wear lab coats and disposable gloves for operation. 3. For research use only!

Read more less

IL- 36 alpha, previously called IL- 1F6 and FIL1 epsilon (family of IL- 1 member epsilon), is a member of the IL- 1 family which includes IL- 1 beta, IL- 1 alpha, IL- 1ra, IL- 18, and novel family members IL- 36 Ra (IL- 1F5), IL- 36 beta (IL- 1F8), IL- 36 gamma (IL- 1F9), IL- 37 (IL- 1F7) and IL- 1F10. All family members show a 12 beta - strand, beta - trefoil configuration, and are believed to have arisen from a common ancestral gene. IL- 36 alpha is an 18 kDa, 160 amino acid (aa) intracellular and secreted protein that contains no signal sequence, no prosegment and no potential N- linked glycosylation sites. It can be externalized non- specifically in response to LPS and ATP- induced activation of the P2X7 receptor. Full- length recombinant IL- 36 alpha is less active than endogenous IL- 36 alpha, but trimming of the N- termini enhances its activity. Mouse IL- 36 alpha shares 83% aa sequence identity with rat IL- 36 alpha, 54- 60% with human, rabbit, equine and bovine IL- 36 alpha, and 27- 57% aa sequence identity with other novel IL- 1 family members. IL- 36 alpha is mainly found in skin and lymphoid tissues, but also in fetal brain, trachea, stomach and intestine. It is expressed by monocytes,  B and T cells. The receptor for IL- 36  alpha is a combination of IL- 1  Rrp2 (also called     IL- 1 RL2 or IL- 1 R6), mainly found in epithelia and keratinocytes, and the widely expressed IL- 1 RAcP. IL- 36 alpha, beta and gamma all activate NF- kappa B and MAPK pathways in an IL- 1 Rrp2 dependent manner, and induce production of inflammatory cytokines and chemokines such as CXCL8/IL- 8. IL- 36 alpha and other family members are overexpressed in psoriatic skin lesions, and transgenic overexpression of IL- 36 alpha in skin keratinocytes produces epidermal hyperplasia. IL- 36 alpha is present in kidney tubule epithelia; it is highly overexpressed in tubulointerstitial lesions in mouse models of chronic glomerulonephritis, lupus nephritis and diabetic nephritis. IL- 36 alpha is induced by inflammation in adipose tissue- resident alternately activated (M2) macrophages, and reduces adipocyte differentiation.   Product Properties Synonyms FIL1 epsilon, IL-1 epsilon, IL-1F6, IL-1H1 Accession Q9JLA2 GeneID 54448 Source E.coli-derived Mouse IL-36α,160aa, Met1-His160, with an N-terminal Met. Molecular Weight Approximately 18.0 kDa. AA Sequence MNKEKELRAA SPSLRHVQDL SSRVWILQNN ILTAVPRKEQ TVPVTITLLP CQYLDTLETN RGDPTYMGVQ RPMSCLFCTK DGEQPVLQLG EGNIMEMYNK KEPVKASLFY HKKSGTTSTF ESAAFPGWFI AVCSKGSCPL ILTQELGEIF ITDFEMIVVH Tag None Physical Appearance Sterile Filtered White lyophilized (freeze-dried) powder. Purity > 95% by SDS-PAGE and HPLC analyses. Biological Activity The specific activity determined by its ability in a functional ELISA. Immobilized rMuIL-36α at 1 µg/mL can bind recombinant murine IL-1 Rrp2 with a range of 0.15-5 µg/mL. Fully biologically active when compared to standard. Endotoxin < 1.0 EU per 1μg of the protein by the LAL method. Formulation Lyophilized from a 0.2 μm filtered concentrated solution in PBS, pH 7.4, 5 % trehalose. Reconstitution We recommend that this vial be briefly centrifuged prior to opening to bring the contents to the bottom. Reconstitute in sterile distilled water or aqueous buffer containing 0.1% BSA to a concentration of 0.1-1.0 mg/mL. Stock solutions should be apportioned into working aliquots and stored at ≤ -20°C. Further dilutions should be made in appropriate buffered solutions.   Shipping and Storage The products are shipped with ice pack and can be stored at -20℃ to -80℃ for 1 year. Recommend to aliquot the protein into smaller quantities when first used and avoid repeated freeze-thaw cycles.   Cautions 1. Avoid repeated freeze-thaw cycles. 2. For your safety and health, please wear lab coats and disposable gloves for operation. 3. For research use only!

Read more less

Mouse interleukin-36 beta [IL-36 beta ; previously IL-1F8, FIL-1 eta(eta) and IL-1H2] is a member of the IL-1 family  of proteins that includes IL-1 beta, IL-1 alpha, IL-1ra, IL-18, IL-36Ra/IL-1F5, IL-36 alpha /IL-1F6, IL-37/IL-1F7, IL-36 gamma /IL-1F9 and IL-1F10. All family members show a 12 beta-stranded beta-trefoil configuration, share up to 50% amino acid (aa) sequence identity, and are believed to have arisen from a common ancestral gene. Although two alternatively spliced transcript variants for human  IL-36 beta /IL-1F8 have been described, to date, only one mouse IL-36 beta /IL-1F8 isoform is known. Mouse IL-36 beta /IL-1F8 shares 61% and 74% aa identity with human IL-36 beta isoform 2 and rat IL-36 beta, respectively. IL-36 beta is agonistic, stimulating release of inflammatory mediators such as IL-6 and IL-8, and cytotoxic peptides such as beta-defensins 2 and 3 that aid in defense against microbial pathogens. The receptor for IL-36 proteins is IL-1 Rrp2, with IL-1 RAcP as a coreceptor. Antagonism of IL-36 proteins by IL-36Ra, which also binds IL-1 Rrp2, has been shown by some investigators. Skin keratinocytes express highest levels of IL-36 proteins and their receptors, followed by epithelia in the esophagus, trachea and bronchae. IL-36 beta expression is increased in psoriatic skin and may play a role in pathogenesis of psoriasis. IL-36 beta is also expressed in resting and activated monocytes and B cells, synovial fibroblasts, neurons and glia, and is detectable in plasma and body fluids. IL-36 beta, along with IL-36 alpha and  IL-36 gamma, is up-regulated by IL-1 alpha and TNF- alpha in keratinocytes, and has been shown to activate NF- kappa B and MAPK signaling pathways in an IL-1 Rrp2-dependent manner. Full-length recombinant IL-36 proteins appear less active than their endogenous counterparts, but trimming of the N-termini enhances their activity.   Product Properties Synonyms FIL1 eta, IL-1 eta, IL-1F8, IL-1H2 Accession Q9D6Z6 GeneID 69677 Source E.coli-derived Mouse IL-36β, 153aa, Ser31-Lys183. Molecular Weight Approximately 17.4 kDa. AA Sequence SSQSPRNYRV HDSQQMVWVL TGNTLTAVPA SNNVKPVILS LIACRDTEFQ DVKKGNLVFL GIKNRNLCFC CVEMEGKPTL QLKEVDIMNL YKERKAQKAF LFYHGIEGST SVFQSVLYPG WFIATSSIER QTIILTHQRG KLVNTNFYIE SEK Tag None Physical Appearance Sterile Filtered White lyophilized (freeze-dried) powder. Purity > 97% by SDS-PAGE and HPLC analyses. Biological Activity The ED50 as determined by inducing IL-6 secretion in murine NIH/3T3 cells is less than 10 ng/mL, corresponding to a specific activity of > 1.0 × 105 IU/mg. Fully biologically active when compared to standard. Endotoxin < 1.0 EU per 1μg of the protein by the LAL method. Formulation Lyophilized from a 0.2 μm filtered concentrated solution in PBS, pH 7.4, 5 % trehalose. Reconstitution We recommend that this vial be briefly centrifuged prior to opening to bring the contents to the bottom. Reconstitute in sterile distilled water or aqueous buffer containing 0.1% BSA to a concentration of 0.1-1.0 mg/mL. Stock solutions should be apportioned into working aliquots and stored at ≤ -20°C. Further dilutions should be made in appropriate buffered solutions.   Shipping and Storage The products are shipped with ice pack and can be stored at -20℃ to -80℃ for 1 year. Recommend to aliquot the protein into smaller quantities when first used and avoid repeated freeze-thaw cycles.   Cautions 1. Avoid repeated freeze-thaw cycles. 2. For your safety and health, please wear lab coats and disposable gloves for operation. 3. For research use only!

Read more less

CXCL17 also named dendritic cell and monocyte chemokine-like protein (DMC) and VEGF co-regulated chemokine 1 (VCC-1), is a small cytokine belonging to the CXC chemokine family. CXCL17 was the last chemokine ligand to be described and is the 17th member of the CXC chemokine family. Its strategic expression in mucosal tissues suggests that it is involved in innate immunity and/or sterility of the mucosa. Mature human DMC shares 73%, 71% and 64% amino acid sequence identity with bovine, mouse and rat DMC, respectively. It may be a housekeeping chemokine regulating recruitment of nonactivated blood monocytes and immature dendritic cells into tissues and may play a role in the innate defense against infections. CXCL17 also has a role in angiogenesis of importance for tumour develop   Product Properties Synonyms C-X-C Motif Chemokine 17, CXCL17, Dcip1, DMC, UNQ473, VCC-1, VEGF Coregulated Chemokine 1, VEGF Co-Regulated Chemokine 1 Accession Q6UXB2 GeneID 284340 Source E.coli-derived human VCC-1/CXCL17 protein, Ser22-Leu119. Molecular Weight Approximately 11.5 kDa. AA Sequence SSLNPGVARG HRDRGQASRR WLQEGGQECE CKDWFLRAPR RKFMTVSGLP KKQCPCDHFK GNVKKTRHQR HHRKPNKHSR ACQQFLKQCQ LRSFALPL Tag None Physical Appearance Sterile Filtered White lyophilized (freeze-dried) powder. Purity >96% by SDS-PAGE and HPLC analyses. Biological Activity than 5.0 μg/ml, corresponding to a specific activity of > 200 IU/mg. Fully biologically active when compared to standard. Endotoxin < 0.1 EU per 1μg of the protein by the LAL method. Formulation Lyophilized from a 0.2 μm filtered concentrated solution in PBS, pH 7.4, with 3 % Trehalose. Reconstitution We recommend that this vial be briefly centrifuged prior to opening to bring the contents to the bottom. Reconstitute in sterile distilled water or aqueous buffer containing 0.1% BSA to a concentration of 0.1-1.0 mg/mL. Stock solutions should be apportioned into working aliquots and stored at ≤ -20℃. Further dilutions should be made in appropriate buffered solutions.   Shipping and Storage The products are shipped with ice pack and can be stored at -20℃ to -80℃ for 1 year. Recommend to aliquot the protein into smaller quantities when first used and avoid repeated freeze-thaw cycles.   Cautions 1. Avoid repeated freeze-thaw cycles. 2. For your safety and health, please wear lab coats and disposable gloves for operation. 3. For research use only!

Read more less

Vimentins are class-III intermediate filaments found in various non-epithelial cells, especially mesenchymal cells.Human Vimentin shares 97-98% aa identity with mouse, rat, ovine, bovine and canine Vimentin. Vimentin is involved in positioning autophagosomes, lysosomes and the Golgi complex within the cell. Vimentin helps maintain the lipid composition of cellular membranes, and caspase cleavage of Vimentin is a key event in apoptosis.   Product Properties Synonyms FLJ36605, VIM Accession P08670 GeneID 7431 Source E.coli-derived Human Vimentin, Ser2-Glu466. Molecular Weight Approximately 53.5 kDa. AA Sequence STRSVSSSSY RRMFGGPGTA SRPSSSRSYV TTSTRTYSLG SALRPSTSRS LYASSPGGVY ATRSSAVRLR SSVPGVRLLQ DSVDFSLADA INTEFKNTRT NEKVELQELN DRFANYIDKV RFLEQQNKIL LAELEQLKGQ GKSRLGDLYE EEMRELRRQV DQLTNDKARV EVERDNLAED IMRLREKLQE EMLQREEAEN TLQSFRQDVD NASLARLDLE RKVESLQEEI AFLKKLHEEE IQELQAQIQE QHVQIDVDVS KPDLTAALRD VRQQYESVAA KNLQEAEEWY KSKFADLSEA ANRNNDALRQ AKQESTEYRR QVQSLTCEVD ALKGTNESLE RQMREMEENF AVEAANYQDT IGRLQDEIQN MKEEMARHLR EYQDLLNVKM ALDIEIATYR KLLEGEESRI SLPLPNFSSL NLRETNLDSL PLVDTHSKRT LLIKTVETRD GQVINETSQH HDDLE Tag None Physical Appearance Sterile Filtered White lyophilized (freeze-dried) powder. Purity > 95% by SDS-PAGE and HPLC analyses. Endotoxin < 0.1 EU per 1μg of the protein by the LAL method. Formulation Lyophilized from a 0.2 µm filtered solution in 30 % Acetonitrile and 0.1 % TFA. Reconstitution We recommend that this vial be briefly centrifuged prior to opening to bring the contents to the bottom. Reconstitute in 4 mM HCl to a concentration of 0.1-1.0 mg/mL. Stock solutions should be apportioned into working aliquots and stored at ≤ -20℃. Further dilutions should be made in appropriate buffered solutions.   Shipping and Storage The products are shipped with ice pack and can be stored at -20℃ for 1 year. 1 month, 2 to 8 °C under sterile conditions after reconstitution. 3 months, -20 °C under sterile conditions after reconstitution. Recommend to aliquot the protein into smaller quantities when first used and avoid repeated freeze-thaw cycles.   Cautions 1. Avoid repeated freeze-thaw cycles. 2. For your safety and health, please wear lab coats and disposable gloves for operation. 3. For research use only.

Read more less

Vitronectin (VTN) is a glycoprotein that is involved in cell adhesion, migration, and survival. It is a multifunctional protein that plays a role in processes such as blood coagulation, wound healing, and tissue regeneration. VTN also has potential therapeutic applications for diseases such as cancer and cardiovascular disease.   Product Properties Synonyms V75 ; Vitronectin ; VN Uniprot No. P04004 Source Recombinant Human VTN Protein is expressed from HEK293 Cells with His tag at the N-terminal. It contains Asp20-Leu478. Molecular Weight The protein has a predicted MW of 54.23 kDa. And it migrates as 72-100 kDa under reducing (R) condition (SDS-PAGE) due to glycosylation. Purity > 95% as determined by SDS-PAGE. Endotoxin <1 EU per 1μg of the protein by the LAL method. Formulation Lyophilized from 0.22 μm filtered solution in PBS (pH 7.4). Reconstitution Centrifuge tubes before opening. Dissolve lyophilized protein with sterile PBS to ensure the concentration is greater than 100 ug/mL.   Shipping and Storage The product should be stored at -25~-15℃ for 1 year from date of receipt. 2-7 days, 2 ~8 °C under sterile conditions after reconstitution. 3 months, -25~-15℃ under sterile conditions after reconstitution. Recommend to aliquot the protein into smaller quantities when first used and avoid repeated freeze-thaw cycles.   Cautions 1.Please operate with lab coats and disposable gloves,for your safety. 2.This product is for research use only.

Read more less

Activin A, a homodimer of activin βA subunits, is a member of the transforming growth factor (TGF)-β super-family. Activin A is produced by the placenta during human pregnancy, has been recognized as a multifunctional cytokine expressed in a wide range of tissues and cells with roles in regulation of wound repair, cell differentiation, apoptosis, embryogenesis, and inflammation. The 14 kDa mature human beta A chain shares 100% amino acid sequence identity with bovine, feline, mouse, porcine, and rat beta A. Activin A has been proposed in several pathological processes such as carcinogenesis and fibrosis, and this cytokine may also be involved in the pathogenesis of various inflammatory disorders such as inflammatory bowel disease and rheumatoid arthritis.   Product Properties Synonyms Activin A, activin AB alpha polypeptide, erythroid differentiation factor, Erythroid differentiation protein, FSH-releasing protein, inhibin beta A chain Accession P08476 GeneID 3624 Source Insect Cell-derived Human/Mouse/Rat Activin A/Inhibin beta A protein, Gly311 - Ser426. Molecular Weight Approximately 26 kDa. AA Sequence GLECDGKVNI CCKKQFFVSF KDIGWNDWII APSGYHANYC EGECPSHIAG TSGSS LSFHS TVINHYRMRG HSPFANLKSC CVPTKLRPMS MLYYDDGQNI IKKDIQNMIV EECGCS Tag None Physical Appearance Sterile Filtered White lyophilized (freeze-dried) powder. Purity > 95% by SDS-PAGE analyses. Biological Activity Test in processing. Endotoxin < 0.1 EU per 1μg of the protein by the LAL method. Formulation Lyophilized from a 0.2 μm filtered concentrated solution in 20 mM Tris-HCl, pH 8.0, 300 mM NaCl, with 5% Trehalose, 0.02% Tween-20. Reconstitution We recommend that this vial be briefly centrifuged prior to opening to bring the contents to the bottom. Reconstitute in sterile 10mM HCl to a concentration of 0.1-0.3 mg/mL. Stock solutions should be apportioned into working aliquots and stored at ≤ -20℃. Further dilutions should be made in appropriate buffered solutions.   Shipping and Storage The products are shipped with ice pack and can be stored at -20 ℃ for 1 year. 1 month, 2 to 8 °C under sterile conditions after reconstitution. 3 months, -20 °C under sterile conditions after reconstitution. Recommend to aliquot the protein into smaller quantities when first used and avoid repeated freeze-thaw cycles.   Cautions 1. Avoid repeated freeze-thaw cycles. 2. For your safety and health, please wear lab coats and disposable gloves for operation. 3. For research use only!

Read more less

Mouse aFGF, encoded by the FGF1 gene, is a member of the fibroblast growth factor (FGF) family. Fibroblast growth factor was found in pituitary extracts in 1973 and then tested in a bioassay that caused fibroblasts to proliferate. After further fractionating the extract using acidic and basic pH, two different forms have isolated that named "acidic fibroblast growth factor" (FGF-1) and "basic fibroblast growth factor" (FGF-2). Murine aFGF shares 52 % amino acid sequence identity with bFGF. Murine aFGF shares 96 % amino acid sequence identity with human aFGF, so it exhibits considerable species crossreactivity between murine and human aFGF. In mammalian FGF receptor family has 4 members, FGFR1, FGFR2, FGFR3, and FGFR4, and 1, 2, 3 have 2 sub-types “b”, “c” . aFGF can bind and activate all 7 different FGFRs. Affinity between aFGF and its receptors can be increased by heparin or heparan sulfate proteoglycan. aFGF plays an important role in the regulation of cell survival, cell division, angiogenesis, cell differentiation and cell migration.   Product Properties Synonyms Fibroblast growth factor 1；FGF-1；Acidic fibroblast growth factor；HBGF-1 Accession P61148 GeneID 14164 Source E.coli-derived mouse Acidic Fibroblast Growth Factor protein, Phe16-Asp155 Molecular Weight Approximately 15.8 kDa. AA Sequence FNLPLGNYKK PKLLYCSNGG HFLRILPDGT VDGTRDRSDQ HIQLQLSAES AGEVYIKGTE TGQYLAMDTE GLLYGSQTPN EECLFLERLE ENHYNTYTSK KHAEKNWFVG LKKNGSCKRG PRTHYGQKAI LFLPLPVSSD Tag None Physical Appearance Sterile Filtered White lyophilized (freeze-dried) powder. Purity > 96 % by SDS-PAGE and HPLC analyses. Biological Activity Fully biologically active when compared to standard. The ED50 as determined by a cell proliferation assay using murine balb/c 3T3 cells is less than 0.2 ng/ml, corresponding to a specific activity of > 5.0 × 106 IU/mg in the presence of 10 μg/ml of heparin. Endotoxin < 1.0 EU per 1μg of the protein by the LAL method. Formulation Lyophilized from a 0.2 µm filtered concentrated solution in PBS, pH 7.4. Reconstitution We recommend that this vial be briefly centrifuged prior to opening to bring the contents to the bottom. Reconstitute in sterile distilled water or aqueous buffer containing 0.1 % BSA to a concentration of 0.1-1.0 mg/mL. Stock solutions should be apportioned into working aliquots and stored at ≤ -20 °C. Further dilutions should be made in appropriate buffered solutions.   Shipping and Storage The products are shipped with ice pack and can be stored at -20℃ to -80℃ for 1 year. Recommend to aliquot the protein into smaller quantities when first used and avoid repeated freeze-thaw cycles.   Cautions 1. Avoid repeated freeze-thaw cycles. 2. For your safety and health, please wear lab coats and disposable gloves for operation. 3. For research use only!

Read more less

FGF basic, also known as FGF-2 and HBGF-2, is a member of the FGF superfamily of mitogenic proteins which show 35-60% amino acid conservation. Human FGF acidic shares 54% amino acid (aa) sequence identity with FGF basic and 17%-33% with other human FGFs. It shares 92%, 96%, 96%, and 96% aa sequence identity with bovine, mouse, porcine, and rat FG F acidic, respectively, andexhibits considerable species crossreactivity. Alternate splicing generates a truncated isoform of human FG F acidic that consists of the Nterminal 40% of themolecule and functions as a receptor antagonist. The effects of androgen and FGF-2 could be partly reversed with a specific anti-FGF-2 immunoglobulin G or by suramin, which inhibits binding of FGFs to their high affinity receptors. Additionally, bFGF is frequently used for a critical component of cell culture medium, e.g., human embryonic stem cell culture medium, serum-free culture systems.   Product Properties Synonyms bFGF, FGF basic, FGF2, FGF-2, fibroblast growth factor 2 (basic), HBGF-2, Prostatropin Accession P15655 GeneID 14173 Source E.coli-derived mouse bFGF, Pro10-Ser154, with an N-terminal Met. Molecular Weight Approximately 16.5 kDa. AA Sequence MPALPEDGGA AFPPGHFKDP KRLYCKNGGF FLRIHPDGRV DGVREKSDPH VKLQLQAEER GVVSIKGVCA NRYLAMKEDG RLLASKCVTE ECFFFERLES NNYNTYRSRK YSSWYVALKR TGQYKLGSKT GPGQKAILFL PMSAKS Tag None Physical Appearance Sterile Filtered White lyophilized (freeze-dried) powder. Purity >98% by SDS-PAGE and HPLC analyses. Biological Activity The ED50 as determined by a cell proliferation assay using murine balb/c 3T3 cells is less than 1.0 ng/mL, corresponding to a specific activity of > 1.0 × 10 6 IU/mg. Fully biologically active when compared to standard. Endotoxin < 1.0 EU per 1μg of the protein by the LAL method. Formulation Lyophilized from a 0.2 μm filtered concentrated solution in PBS, pH 7.4. Reconstitution We recommend that this vial be briefly centrifuged prior to opening to bring the contents to the bottom. Reconstitute in sterile distilled water or aqueous buffer containing 0.1% BSA to a concentration of 0.1-1.0 mg/mL. Stock solutions should be apportioned into working aliquots and stored at ≤ -20℃. Further dilutions should be made in appropriate buffered solutions.   Shipping and Storage The products are shipped with ice pack and can be stored at -20 ℃ for 1 year. 1 month, 2 to 8 °C under sterile conditions after reconstitution. 3 months, -20 °C under sterile conditions after reconstitution. Recommend to aliquot the protein into smaller quantities when first used and avoid repeated freeze-thaw cycles.   Cautions 1. Avoid repeated freeze-thaw cycles. 2. For your safety and health, please wear lab coats and disposable gloves for operation. 3. For research use only!

Read more less

Bcl-xL is a member of the Bcl-2 family of proteins that regulates outer mitochondrial membrane permeability. Bcl-xL is an anti- apoptotic member that prevents release of cytochrome c from the mitochondria intermembrane space into the cytosol. Bcl-xL is present on the outer mitochondrial membrane and is also found on other membranes in some cell types. Natural Bcl-xL contains a carboxyl-terminal mitochondria targeting sequence. Recombinant Bcl-xL missing the mitochondrial targeting sequence maintains its ability to neutralize pro- apoptotic Bcl-2 family members. Neutralization by Bcl-xL appears to be through binding the BH3 region of pro- apoptotic Bcl-2 family members. This activity does not require the mitochondrial targeting sequence.   Product Properties Synonyms Apoptosis regulator Bcl-X; bcl2-L-1 Accession Q64373 GeneID 12048 Source E.coli-derived Human Mouse Bcl-xL, Ser2-Arg212, with an N-terminal Met. Molecular Weight Approximately 23.7 kDa. AA Sequence SQSNRELVVD FLSYKLSQKG YSWSQFSDVE ENRTEAPEET EAERETPSAI NGNPSWHLAD SPAVNGATGH SSSLDAREVI PMAAVKQALR EAGDEFELRY RRAFSDLTSQ LHITPGTAYQ SFEQVVNELF RDGVNWGRIV AFFSFGGALC VESVDKEMQV LVSRIASWMA TYLNDHLEPW IQENGGWDTF VDLYGNNAAA ESRKGQERFN R Tag None Physical Appearance Sterile Filtered White lyophilized (freeze-dried) powder. Purity > 97% by SDS-PAGE and HPLC analyses. Biological Activity Test in Process. Endotoxin Less than 0.1 EU/µg of rMuBcl-xL as determined by LAL method. Formulation Lyophilized from a 0.2 µm filtered concentrated solution in 2 × PBS, pH 7.4, 5% Trehalose. Reconstitution We recommend that this vial be briefly centrifuged prior to opening to bring the contents to the bottom. Reconstitute in sterile distilled water or aqueous buffer containing 0.1% BSA to a concentration of 0.1-1.0 mg/mL. Stock solutions should be apportioned into working aliquots and stored at ≤ -20℃. Further dilutions should be made in appropriate buffered solutions.   Shipping and Storage The products are shipped with ice pack and can be stored at -20℃ to -80℃ for 1 year. Recommend to aliquot the protein into smaller quantities when first used and avoid repeated freeze-thaw cycles.   Cautions 1. Avoid repeated freeze-thaw cycles. 2. For your safety and health, please wear lab coats and disposable gloves for operation. 3. For research use only!

Read more less

Betacellulin (BTC) is a new member of the EGF family of cytokines that is comprised of at least ten proteins including EGF, TGF-alpha, amphiregulin, HB-EGF, and the various heregulins. All of these cytokines are synthesized as transmembrane precursors and are characterized by the presence of one or more EGF structural units in their extracellular domain. The soluble forms of these cytokines are released by proteolytic cleavage. BTC, a heparin-binding protein, was originally isolated from the conditioned media of mouse pancreatic beta tumor cells as a 32 kDa glycoprotein composed of 80 amino acid residues. The cDNA encoding human BTC was cloned from a human breast adenocarcinoma cell line (MCF-7) cDNA library. Human and mouse cDNAs encode BTC precursor proteins of 178 and 177 amino acid residues, respectively. At the amino acid sequence level, human BTC precursor protein exhibits 79% identity with that of the mouse BTC precursor. In a mouse cell line transfected with human BTC cDNA, three forms of soluble human BTC have been detected: the glycosylated, intact BTC composed of 80 amino acid residues, a truncated molecule lacking 12 amino acid residues from the amino terminus, and a second truncated molecule lacking 30 amino acid residues from the amino terminus. The biological activities of these BTC forms were shown to be identical. BTC can bind to the EGF receptor and is a potent mitogen for Balb/c 3T3 fibroblasts, retinal pigment epithelial cells and vascular smooth muscle cells.   Product Properties Synonyms BTC, probetacellulin Accession Q05928 GeneID 12223 Source E.coli-derived mouse Betacellulin protein, Asp32-Tyr111. Molecular Weight Approximately 9.0 kDa. AA Sequence DGNTTRTPET NGSLCGAPGE NCTGTTPRQK VKTHFSRCPK QYKHYCIHGR CRFVVDEQTP SCICEKGYFG ARCERVDLFY Tag None Physical Appearance Sterile Filtered White lyophilized (freeze-dried) powder. Purity >96% by SDS-PAGE and HPLC analyses. Biological Activity The ED50 as determined by a cell proliferation assay using murine Balb/c 3T3 cells is less than 0.01 ng/mL, corresponding to a specific activity of > 1.0 × 10 8 IU/mg. Fully biologically active when compared to standard. Endotoxin < 1.0 EU per 1μg of the protein by the LAL method. Formulation Lyophilized from a 0.2 μm filtered concentrated solution in 2 × PBS, pH 7.4. Reconstitution We recommend that this vial be briefly centrifuged prior to opening to bring the contents to the bottom. Reconstitute in sterile distilled water or aqueous buffer containing 0.1% BSA to a concentration of 0.1-1.0 mg/mL. Stock solutions should be apportioned into working aliquots and stored at ≤ -20℃. Further dilutions should be made in appropriate buffered solutions.   Shipping and Storage The products are shipped with ice pack and can be stored at -20℃ to -80℃ for 1 year. Recommend to aliquot the protein into smaller quantities when first used and avoid repeated freeze-thaw cycles.   Cautions 1. Avoid repeated freeze-thaw cycles. 2. For your safety and health, please wear lab coats and disposable gloves for operation. 3. For research use only!

Read more less

Defensins (alpha and beta) are cationic peptides with antimicrobial activity against Gram-negative and Gram-positive bacteria, fungi, and enveloped viruses. They are 2-6 kDa proteins and take important roles in innate immune system. On the basis of their size and pattern of disulfide bonding, mammalian defensins are classified into alpha, beta and theta categories. β-Defensins are expressed on some leukocytes and at epithelial surfaces. They contain a six-cysteine motif that forms three intra-molecular disulfide bonds. Because β-defensins are cationic peptides, they can therefore interact with the membrane of invading microbes, which are negative due to lipopolysaccharides (LPS) and lipoteichoic acid (LTA) found in the cell membrane. Especially, they have higher affinity to the binding site compared to Ca2+ and Mg2+ ions. Furthermore, they can affect the stability of the membrane. Additionally, they are not only have the ability to strengthen the innate immune system but can also enhance the adaptive immune system by chemotaxis of monocytes, T-lymphocytes, dendritic cells and mast cells to the infection site.   Product Properties Synonyms BD1 Protein, DEFB-1 Protein, DEFB101 Protein, BD1 Protein Accession P56386 GeneID 13214 Source E.coli-derived mouse Beta-defensin 1 protein, Val22-Ser69 Molecular Weight Approximately 5.2 kDa. AA Sequence VGILTSLGRR TDQYKCLQHG GFCLRSSCPS NTKLQGTCKP DKPNCCKS Tag None Physical Appearance Sterile Filtered White lyophilized (freeze-dried) powder. Purity > 97 % by SDS-PAGE and HPLC analyses. Biological Activity Fully biologically active when compared to standard. The biologically active determined by a chemotaxis bioassay using CD34+ dendritic cells is in a concentration range of 100.0-1000.0 ng/ml. Endotoxin < 1.0 EU per 1μg of the protein by the LAL method. Formulation Lyophilized from a 0.2 µm filtered concentrated solution in PBS, pH 7.4. Reconstitution We recommend that this vial be briefly centrifuged prior to opening to bring the contents to the bottom. Reconstitute in sterile distilled water or aqueous buffer containing 0.1 % BSA to a concentration of 0.1-1.0 mg/mL. Stock solutions should be apportioned into working aliquots and stored at ≤ -20 °C. Further dilutions should be made in appropriate buffered solutions.   Shipping and Storage The products are shipped with ice pack and can be stored at -20℃ to -80℃ for 1 year. Recommend to aliquot the protein into smaller quantities when first used and avoid repeated freeze-thaw cycles.   Cautions 1. Avoid repeated freeze-thaw cycles. 2. For your safety and health, please wear lab coats and disposable gloves for operation. 3. For research use only.

Read more less

Defensins (alpha and beta) are cationic peptides with antimicrobial activity against Gram-negative and Gram-positive bacteria, fungi, and enveloped viruses. They are 2-6 k Da proteins and take important roles in innate immune system. On the basis of their size and pattern of disulfide bonding, mammalian defensins are classified into alpha, beta and theta categories. β-Defensins contain a six-cysteine motif that forms three intra-molecular disulfide bonds. Four human β-defensins have been identified and they are expressed on some leukocytes and at epithelial surfaces. Because β-defensins is cationic peptides, they can therefore interact with the membrane of invading microbes, which are negative due to lipopolysaccharides (LPS) and lipoteichoic acid (LTA) found in the cell membrane. Especially, they have higher affinity to the binding site compared to Ca2+ and Mg2+ ions. Furthermore, they can affect the stability of the membrane.   Product Properties Synonyms Defensin beta 14, Beta-defensin 14,BD-14, Defensin, beta 14 Accession Q7TNV9 GeneID 244332 Source E.coli-derived mouse Beta-defensin 14 protein, Phe23-Lys67 Molecular Weight Approximately 5.2 kDa. AA Sequence FLPKTLRKFF CRIRGGRCAV LNCLGKEEQI GRCSNSGRKC CRKKK Tag None Physical Appearance Sterile Filtered White lyophilized (freeze-dried) powder. Purity > 96 % by SDS-PAGE and HPLC analyses. Biological Activity Testing in progress. Endotoxin < 0.1 EU per 1μg of the protein by the LAL method. Formulation Lyophilized from a 0.2 µm filtered concentrated solution in PBS, pH 7.4. Reconstitution We recommend that this vial be briefly centrifuged prior to opening to bring the contents to the bottom. Reconstitute in sterile distilled water or aqueous buffer containing 0.1 % BSA to a concentration of 0.1-1.0 mg/mL. Stock solutions should be apportioned into working aliquots and stored at ≤ -20 °C. Further dilutions should be made in appropriate buffered solutions.   Shipping and Storage The products are shipped with ice pack and can be stored at -20℃ to -80℃ for 1 year. Recommend to aliquot the protein into smaller quantities when first used and avoid repeated freeze-thaw cycles.   Cautions 1. Avoid repeated freeze-thaw cycles. 2. For your safety and health, please wear lab coats and disposable gloves for operation. 3. For research use only!

Read more less

Defensins (alpha and beta) are cationic peptides with antimicrobial activity against Gram-negative and Gram-positive bacteria, fungi, and enveloped viruses. They are 2-6 kDa proteins and take important roles in innate immune system. On the basis of their size and pattern of disulfide bonding, mammalian defensins are classified into alpha, beta and theta categories. β-Defensins are expressed on some leukocytes and at epithelial surfaces. They contain a six-cysteine motif that forms three intra-molecular disulfide bonds. Because β-defensins are cationic peptides, they can therefore interact with the membrane of invading microbes, which are negative due to lipopolysaccharides (LPS) and lipoteichoic acid (LTA) found in the cell membrane. Especially, they have higher affinity to the binding site compared to Ca2+ and Mg2+ ions. Furthermore, they can affect the stability of the membrane. Additionally, they are not only have the ability to strengthen the innate immune system but can also enhance the adaptive immune system by chemotaxis of monocytes, T-lymphocytes, dendritic cells and mast cells to the infection site.   Product Properties Synonyms Beta-defensin 2, Beta-defensin 4A, BD-2, Defensin beta2 Accession P82020 GeneID 13215 Source E.coli-derived mouse Beta-defensin 2 protein, Ala21-Lys71. Molecular Weight Approximately 5.5 kDa. AA Sequence AVGSLKSIGY EAELDHCHTN GGYCVRAICP PSARRPGSCF PEKNPCCKYM K Tag None Physical Appearance Sterile Filtered White lyophilized (freeze-dried) powder. Purity > 98 % by SDS-PAGE and HPLC analyses. Biological Activity Fully biologically active when compared to standard. The biologically active determined by a chemotaxis bioassay using immature human dendritic cells is in a concentration of 10-100 ng/ml. Endotoxin < 1.0 EU per 1μg of the protein by the LAL method. Formulation Lyophilized from a 0.2 µm filtered concentrated solution in PBS, pH 7.4. Reconstitution We recommend that this vial be briefly centrifuged prior to opening to bring the contents to the bottom. Reconstitute in sterile distilled water or aqueous buffer containing 0.1 % BSA to a concentration of 0.1-1.0 mg/mL. Stock solutions should be apportioned into working aliquots and stored at ≤ -20 °C. Further dilutions should be made in appropriate buffered solutions.   Shipping and Storage The products are shipped with ice pack and can be stored at -20℃ to -80℃ for 1 year. Recommend to aliquot the protein into smaller quantities when first used and avoid repeated freeze-thaw cycles.   Cautions 1. Avoid repeated freeze-thaw cycles. 2. For your safety and health, please wear lab coats and disposable gloves for operation. 3. For research use only.

Read more less

Defensins (alpha and beta) are cationic peptides with antimicrobial activity against Gram-negative and Gram-positive bacteria, fungi, and enveloped viruses. They are 2-6 kDa proteins and take important roles in innate immune system. On the basis of their size and pattern of disulfide bonding, mammalian defensins are classified into alpha, beta and theta categories. β-Defensins are expressed on some leukocytes and at epithelial surfaces. They contain a six-cysteine motif that forms three intra-molecular disulfide bonds. Because β-defensins are cationic peptides, they can therefore interact with the membrane of invading microbes, which are negative due to lipopolysaccharides (LPS) and lipoteichoic acid (LTA) found in the cell membrane. Especially, they have higher affinity to the binding site compared to Ca2+ and Mg2+ ions. Furthermore, they can affect the stability of the membrane. Additionally, they are not only have the ability to strengthen the innate immune system but can also enhance the adaptive immune system by chemotaxis of monocytes, T-lymphocytes, dendritic cells and mast cells to the infection site.   Product Properties Synonyms BD-3 Protein, DEFB-3 Protein, DEFB103 Protein, DEFB3 Protein, BD-3 Protein, BD3 Protein, BP-3 Protein, BP3 Protein Accession Q9WTL0 GeneID 27358 Source E.coli-derived mouse Beta-defensin 3 protein, Lys23-Lys63 Molecular Weight Approximately 4.6 kDa. AA Sequence KKINNPVSCL RKGGRCWNRC IGNTRQIGSC GVPFLKCCKR K Tag None Physical Appearance Sterile Filtered White lyophilized (freeze-dried) powder. Purity > 95 % by SDS-PAGE and HPLC analyses. Biological Activity Fully biologically active when compared to standard. The ED50 as determined by anti-microbial activity against E.coli. is less than 20 μg/ml, corresponding to a specific activity of > 50 IU/mg. Endotoxin < 1.0 EU per 1μg of the protein by the LAL method. Formulation Lyophilized from a 0.2 µm filtered concentrated solution in 2 × PBS, pH 7.4. Reconstitution We recommend that this vial be briefly centrifuged prior to opening to bring the contents to the bottom. Reconstitute in sterile distilled water or aqueous buffer containing 0.1 % BSA to a concentration of 0.1-1.0 mg/mL. Stock solutions should be apportioned into working aliquots and stored at ≤ -20 °C. Further dilutions should be made in appropriate   Shipping and Storage The products are shipped with ice pack and can be stored at -20℃ to -80℃ for 1 year. Recommend to aliquot the protein into smaller quantities when first used and avoid repeated freeze-thaw cycles.   Cautions 1. Avoid repeated freeze-thaw cycles. 2. For your safety and health, please wear lab coats and disposable gloves for operation. 3. For research use only.

Read more less

Chemokine (C-X-C motif) ligand 14 (CXCL14), also named BRAK, is a small cytokine belonging to the CXC chemokine family. Recombinant mouse CXCL14 contains 77 amino acid residues and it shares 97 % and 99 % a.a. sequence identity with human and rat CXCL14. CXCL14 serves as a chemoattractant for activated macrophages, immature dendritic cells and natural killer cells, as well as an antiangiogenic factor by preventing the migration of endothelial cells. CXCL14 also exerts an inhibitory effect on the CXCL12/ CXCR4 signaling pathway, which is involved in the maintenance of T‐helper (Th)2 bias, and promotes Th1 immune response under the physiological and pathological conditions. CXCL14 has been shown to be a highly selective chemoattractant for monocytes that have been treated with prostaglandin E2 or forskolin, agents that activate adenylate cyclase.   Product Properties Synonyms B-cell and Monocyte-activating Chemokine, Chemokine BRAK, Kidney-expressed Chemokine CXC, CXCL14, MIP-2G, Small-inducible Cytokine B14 Accession Q9WUQ5 GeneID 57266 Source E.coli-derived mouse BRAK/CXCL14 protein, Ser23-Glu99. Molecular Weight Approximately 9.4 kDa. AA Sequence SKCKCSRKGP KIRYSDVKKL EMKPKYPHCE EKMVIVTTKS MSRYRGQEHC LHPKLQSTKR FIKWYNAWNE KRRVYEE Tag None Physical Appearance Sterile Filtered White lyophilized (freeze-dried) powder. Purity >95% by SDS-PAGE and HPLC analyses. Biological Activity The biological activity determined by a chemotaxis bioassay using human monocytes is in a concentration range of 1.0-10 ng/mL. Fully biologically active when compared to standard. Endotoxin < 1.0 EU per 1μg of the protein by the LAL method. Formulation Lyophilized from a 0.2 μm filtered concentrated solution in 20 mM PB, 400 mM NaCl, pH 7.4, 5% trehalose. Reconstitution We recommend that this vial be briefly centrifuged prior to opening to bring the contents to the bottom. Reconstitute in sterile distilled water or aqueous buffer containing 0.1% BSA to a concentration of 0.1-1.0 mg/ml. Stock solutions should be apportioned into working aliquots and stored at ≤-20℃. Further dilutions should be made in appropriate buffered solutions.   Shipping and Storage The products are shipped with ice pack and can be stored at -20℃ to -80℃ for 1 year. Recommend to aliquot the protein into smaller quantities when first used and avoid repeated freeze-thaw cycles.   Cautions 1. Avoid repeated freeze-thaw cycles. 2. For your safety and health, please wear lab coats and disposable gloves for operation. 3. For research use only!

Read more less

Cardiotrophin1 (CT1) is a member of the cytokine family which also includes IL-6, IL-11, leukemia inhibitory factor (LIF), oncostatin M (OSM), and ciliary neurotrophic factor (CNTF). CT-1 is a pleiotropic cytokine which is expressed in various tissues including the adult heart, skeletal muscle, ovary, colon, prostate and fetal lung. Studies showed CT-1 which induces cardiac myocyte hypertrophy in vitro can bind to and activate the ILST/gp130 receptor. Rat CT1 encodes a 203 amino acid (a.a.) residue protein that lacks a hydrophobic signal peptide and it shares 94% a.a. and 79% a.a. sequence identity with human and murine CT-1.   Product Properties Synonyms CT-1CT1; CTF1 Accession Q60753 GeneID 13019 Source E.coli-derived Mouse CT-1, Met1-Ala203, with an N-terminal Met. Molecular Weight Approximately 21.5 kDa. AA Sequence MSQREGSLED HQTDSSISFL PHLEAKIRQT HNLARLLTKY AEQLLEEYVQ QQGEPFGLPG FSPPRLPLAG LSGPAPSHAG LPVSERLRQD AAALSVLPAL LDAVRRRQAE LNPRAPRLLR SLEDAARQVR ALGAAVETVL AALGAAARGP GPEPVTVATL FTANSTAGIF SAKVLGFHVC GLYGEWVSRT EGDLGQLVPG GVA Tag None Physical Appearance Sterile Filtered White lyophilized (freeze-dried) powder. Purity > 95% by SDS-PAGE and HPLC analyses. Biological Activity The ED50 as determined by a cell proliferation assay using human TF-1 cells is less than 0.5 ng/ml, corresponding to a specific activity of > 2.0 × 10 6 IU/mg. Fully biologically active when compared to standard. Endotoxin Less than 1 EU/µg of rMuCT-1 as determined by LAL method. Formulation Lyophilized from a 0.2 µm filtered concentrated solution in 20 mM Tris, 300 mM NaCl, pH 8.5. Reconstitution We recommend that this vial be briefly centrifuged prior to opening to bring the contents to the bottom. Reconstitute in sterile distilled water or aqueous buffer containing 0.1% BSA to a concentration of 0.1-1.0 mg/mL. Stock solutions should be apportioned into working aliquots and stored at ≤ -20℃. Further dilutions should be made in appropriate buffered solutions.   Shipping and Storage The products are shipped with ice pack and can be stored at -20℃ to -80℃ for 1 year. Recommend to aliquot the protein into smaller quantities when first used and avoid repeated freeze-thaw cycles.   Cautions 1. Avoid repeated freeze-thaw cycles. 2. For your safety and health, please wear lab coats and disposable gloves for operation. 3. For research use only!

Read more less

Ciliary neurotrophic factor (CNTF) is one of a small number of proteins with neurotrophic activities distinct from nerve growth factor (NGF). The cDNA for human CNTF encodes a 200 amino acid residue polypeptide that lacks a signal sequence. Recombinant human CNTF containing 200 amino acids and it shares 82% and 83% a.a. sequence identity with mouse and rat CNTF. The protein is a potent survival factor for neurons and oligodendrocytes and may be relevant in reducing tissue destruction during inflammatory attacks. In addition, CNTF is useful for treatment of motor neuron disease and it could reduce food intake without causing hunger or stress. CNTF is structurally related to IL-6, IL-11, LIF and OSM. Among factors belonging to the CNTF family, CNTF, leukemia inhibitory factor, cardiotrophin-1, and oncostatin M induced a strong promyelinating effect.   Product Properties Synonyms ciliary neurotrophic factor, CNTF, HCNTF Accession P51642 GeneID 12803 Source E.coli-derived mouse CNTF, Ala2-Met198. Molecular Weight Approximately 22.5 kDa. AA Sequence AFAEQSPLTL HRRDLCSRSI WLARKIRSDL TALMESYVKH QGLNKNISLD SVDGVPVAST DRWSEMTEAE RLQENLQAYR TFQGMLTKLL EDQRVHFTPT EGDFHQAIHT LTLQVSAFAY QLEELMALLE QKVPEKEADG MPVTIGDGGL FEKKLWGLKV LQELSQWTVR SIHDLRVISS HHMGISAHES HYGAKQM Tag None Physical Appearance Sterile Filtered White lyophilized (freeze-dried) powder. Purity >95% by SDS-PAGE and HPLC analyses. Biological Activity The ED50 as determined by a cell proliferation assay using human TF-1 cells is less than 30 ng/mL, corresponding to a specific activity of > 3.3 × 10 4 IU/mg. Fully biologically active when compared to standard. Endotoxin < 1.0 EU per 1μg of the protein by the LAL method. Formulation Lyophilized from a 0.2 μm filtered concentrated solution in in 2 × PBS, pH 7.4, 2% trehalose. Reconstitution We recommend that this vial be briefly centrifuged prior to opening to bring the contents to the bottom. Reconstitute in sterile distilled water or aqueous buffer containing 0.1% BSA to a concentration of 0.1-1.0 mg/mL. Stock solutions should be apportioned into working aliquots and stored at ≤ -20℃. Further dilutions should be made in appropriate buffered solutions.   Shipping and Storage The products are shipped with ice pack and can be stored at -20℃ to -80℃ for 1 year. Recommend to aliquot the protein into smaller quantities when first used and avoid repeated freeze-thaw cycles.   Cautions 1. Avoid repeated freeze-thaw cycles. 2. For your safety and health, please wear lab coats and disposable gloves for operation. 3. For research use only!

Read more less

CTACK is a keratinocyte-derived CC chemokine which signals through the CCR10 receptor. Both CTACK and CCR10 are expressed in normal and irritated epithelial cells. CTACK selectively attracts CLA+ T cells and directs them into the skin. CTACK contains the four highly conserved cysteine residues present in most CC chemokines. The mature protein contains 88 amino acid residues. Recombinant Murine CTACK is a 10.9 kDa protein containing 95 amino acid residues.   Product Properties Synonyms CCL27 Accession Q9Z1X0 GeneID 20301 Source E.coli-derived Mouse CCL27 protein,Leu26-Asn120. Molecular Weight Approximately 10.9 kDa AA Sequence LPLPSSTSCC TQLYRQPLPS RLLRRIVHME LQEADGDCHL QAVVLHLARR SVCVHPQNRS LARWLERQGK RLQGTVPSLN LVLQKKMYSN PQQQN Tag None Physical Appearance Sterile Filtered White lyophilized (freeze-dried) powder. Purity > 98% by SDS-PAGE and HPLC analyses. Biological Activity Fully biologically active when compared to standard. The biological activity determined by a chemotaxis bioassay using human peripheral blood lymphocytes is in a concentration range of 10-100 ng/ml. Endotoxin <1 EU/μg of protein as determined by LAL method. Formulation Lyophilized from a 0.2 µm filtered concentrated solution in 2 × PBS, pH 7.4, with 5% trehalose. Reconstitution We recommend that this vial be briefly centrifuged prior to opening to bring the contents to the bottom. Reconstitute in sterile distilled water or aqueous buffer containing 0.1% BSA to a concentration of 0.1-1.0 mg/mL. Stock solutions should be apportioned into working aliquots and stored at ≤ -20°C. Further dilutions should be made in appropriate buffered solutions.   Shipping and Storage The products are shipped with ice pack and can be stored at -20℃ to -80℃ for 1 year. Recommend to aliquot the protein into smaller quantities when first used and avoid repeated freeze-thaw cycles.   Cautions 1. Avoid repeated freeze-thaw cycles. 2. For your safety and health, please wear lab coats and disposable gloves for operation. 3. For research use only.

Read more less

CXCL16 is a member of the CXC chemokine family. Mouse CXCL16 has 246 a.a. and consists of a 26 a.a. residue putative signal peptide, an 88 a.a. residue chemokine domain, an 87 a.a. residue mucin-like spacer region, a 22 a.a. residue transmembrane domain, and a 23 a.a. residue cytoplasmic tail. Mouse and human CXCL16 share 49% overall aa identity and 70% similarity in the chemokine domains. CXCL16 is a transmembrane chemokine and is implicated in activated CD8+ T cell trafficking. CXCL16 mediates adhesion and phagocytosis of both Gram-negative and Gram-positive bacteria and is a strong chemoattractant for CXCR6+ T cells. It facilitates uptake of low density lipoproteins by macrophages, resulting in foam cell formation.   Product Properties Synonyms SR-PXOX, Scavenger Peceptor for Phosphatidylserine and Oxidized Low Density Lipoprotein, Small-inducible Cytokine B16, Transmembrane Chemokine CXCL16 Accession Q8BSU2 GeneID 66102 Source E.coli-derived mouse CXCL16 protein, Asn27-Pro114. Molecular Weight Approximately 9.9 kDa. AA Sequence NQGSVAGSCS CDRTISSGTQ IPQGTLDHIR KYLKAFHRCP FFIRFQLQSK SVCGGSQDQW VRELVDCFER KECGTGHGKS FHHQKHLP Tag None Physical Appearance Sterile Filtered White lyophilized (freeze-dried) powder. Purity >98% by SDS-PAGE and HPLC analyses. Biological Activity The biological activity determined by a chemotaxis bioassay using mouse lymphocytes is in a concentration of 20-1000 ng/mL. Fully biologically active when compared to standard. Endotoxin < 1.0 EU per 1μg of the protein by the LAL method. Formulation Lyophilized from a 0.2 μm filtered concentrated solution in PBS. Reconstitution We recommend that this vial be briefly centrifuged prior to opening to bring the contents to the bottom. Reconstitute in sterile distilled water or aqueous buffer containing 0.1% BSA to a concentration of 0.1-1.0 mg/mL. Stock solutions should be apportioned into working aliquots and stored at ≤ -20℃. Further dilutions should be made in appropriate buffered solutions.   Shipping and Storage The products are shipped with ice pack and can be stored at -20℃ to -80℃ for 1 year. Recommend to aliquot the protein into smaller quantities when first used and avoid repeated freeze-thaw cycles.   Cautions 1. Avoid repeated freeze-thaw cycles. 2. For your safety and health, please wear lab coats and disposable gloves for operation. 3. For research use only!

Read more less

CXCL3, also known as DCIP1 in mouse, CINC2 in rat, and GROγ in humans, is belonging to the CXC chemokine family. The amino acid sequence of mouse CXCL3 is 57 % identical to human CXCL3. CXCL3 plays a role in inflammation and exert its effects on endothelial cells in an autocrine fashion. Similar to other alpha chemokines, the three GRO proteins are potent neutrophil attractants and activators. In addition, these chemokines are also active toward basophils. CXCL3 was reportedly associated with the invasion and metastasis of various malignancies. As a member of the chemokine family, CXCL3 was previously known to participate in many pathophysiological events. CXCL3 was found to be upregulated in aggressive cancer cells.   Product Properties Synonyms chemokine (C-X-C motif) ligand 3, CINC-2, CINC-2b, CXCL3, Dcip1, Gm1960, GRO gamma, GRO3 oncogene, GRO3, GROG, GRO-gamma, Growth-regulated protein gamma, Macrophage inflammatory protein 2-beta, MGSA gamma, MIP2B, MIP-2b, MIP2-beta, SCYB3 Accession Q6W5C0 GeneID 330122 Source E.coli-derived mouse DCIP-1/CXCL3 protein, Ala28-Ser100. Molecular Weight Approximately 7.9 kDa. AA Sequence AVVASELRCQ CLNTLPRVDF ETIQSLTVTP PGPHCTQTEV IATLKDGQEV CLNPQGPRLQ IIIKKILKSG KSS Tag None Physical Appearance Sterile Filtered White lyophilized (freeze-dried) powder. Purity >97% by SDS-PAGE and HPLC analyses. Biological Activity The biological activity determined by a chemotaxis bioassay using human CXCR2 transfected human 293 cells is in a concentration range of 10-100 ng/ml. Fully biologically active when compared to standard. Endotoxin < 1.0 EU per 1μg of the protein by the LAL method. Formulation Lyophilized from a 0.2 μm filtered concentrated solution in PBS, pH 7.4. Reconstitution We recommend that this vial be briefly centrifuged prior to opening to bring the contents to the bottom. Reconstitute in sterile distilled water or aqueous buffer containing 0.1% BSA to a concentration of 0.1-1.0 mg/mL. Stock solutions should be apportioned into working aliquots and stored at ≤ -20℃. Further dilutions should be made in appropriate buffered solutions.   Shipping and Storage The products are shipped with ice pack and can be stored at -20℃ to -80℃ for 1 year. Recommend to aliquot the protein into smaller quantities when first used and avoid repeated freeze-thaw cycles.   Cautions 1. Avoid repeated freeze-thaw cycles. 2. For your safety and health, please wear lab coats and disposable gloves for operation. 3. For research use only!

Read more less

Desert Hedgehog (Dhh) belongs to the highly conserved Hedgehog family of proteins which are involved in multiple developmental processes. Hedgehogs are synthesized as 45 kDa precursors that are cleaved autocatalytically. The 19 kDa N-terminal fragment remains membrane associated due to its cholesterol and palmitate modifications. Binding of this fragment to Patched receptors results in the loss of Patched repression of Smoothened signaling. Dhh binds both Patched and Patched 2 as well as Hedgehog interacting protein (Hip)\. Within the N-terminal peptide, mouse Dhh shares 97% and 100% amino acid (aa) sequence identity with human and rat Dhh, respectively. It shares 74% aa seqeuence identity with mouse Indian (Ihh) and Sonic hedgehog (Shh). Dhh is produced by Sertoli cells and is required for testis development and spermatogenesis. It induces steroidogenic factor 1 which is instrumental in promoting Leydig cell differentiation. It also promotes the deposition of basal lamina surrounding seminiferous tubules. In humans, mutations of Dhh are associated with pure gonadal dysgenesis. Dhh is expressed in the female by ovarian granulosa cells and the corpus luteum. Its upregulation in human ovarian cancer correlates positively with proliferative index and negatively with prognosis. Dhh is also expressed by Schwann cells and is upregulated following nerve injury. It induces the expression of Patched and Hip in nerve fibroblasts and promotes the formation of the connective tissue sheath surrounding peripheral nerves.   Product Properties Synonyms DHH; HHG-3MGC35145 Accession Q61488 GeneID 13363 Source E.coli-derived Mouse DHH C23II, Cys23-Gly198 Molecular Weight Approximately 20.0 kDa. AA Sequence IIGPGRGPVG RRRYVRKQLV PLLYKQFVPS MPERTLGASGPAEGRVTRGSERFRDLVPNY NPDIIFKDEE NSGADRLMTE RCKERVNALA IAVMNMWPGV RLRVTEGWDEDGHHAQDSLH YEGRALDITT SDRDRNKYGL LARLAVEAGF DWVYYESRNH IHVSVKADNS LAVRAGG Tag None Physical Appearance Sterile Filtered White lyophilized (freeze-dried) powder. Purity >98% by SDS-PAGE and HPLC analyses. Biological Activity The ED50 as determined by its ability to induce alkaline phosphatase production by murine MC3T3-E1 cells is 5-20 μg/ml. Fully biologically active when compared to standard. Endotoxin < 0.1 EU per 1μg of the protein by the LAL method. Formulation Lyophilized from a 0.2 μm filtered concentrated solution in PBS, pH 7.4, 1 mM DTT, 0.05% Tween-80. Reconstitution We recommend that this vial be briefly centrifuged prior to opening to bring the contents to the bottom. Reconstitute in sterile distilled water or aqueous buffer containing 0.1% BSA to a concentration of 0.1-1.0 mg/mL. Stock solutions should be apportioned into working aliquots and stored at ≤ -20℃. Further dilutions should be made in appropriate buffered solutions.   Shipping and Storage The products are shipped with ice pack and can be stored at -20℃ to -80℃ for 1 year. Recommend to aliquot the protein into smaller quantities when first used and avoid repeated freeze-thaw cycles.   Cautions 1. Avoid repeated freeze-thaw cycles. 2. For your safety and health, please wear lab coats and disposable gloves for operation. 3. For research use only!

Read more less

Endocrine gland-derived vascular endothelial growth factor (EG-VEGF), also called prokineticin 1 (PK1), is a member of the prokineticin family of secreted proteins that share a common structural motif containing ten conserved cysteine residues that form five pairs of disulfide bonds. The mature region in mouse is 93% and 87% aa identical to the mature regions in rat and human. Mouse EG- VEGF stimulates proliferation and survival of liver sinusoidal endothelial cells, and, in mouse, EG-VEGF acts to induce monocyte migration and stimulate hematopoiesis.   Product Properties Synonyms EGVEGF, Mambakine, PROK1, Prokineticin 1 Accession Q14A28 GeneID 246691 Source E.coli-derived Mouse EG-VEGF protein, Ala20-Phe105. Molecular Weight Approximately 9.6 kDa. AA Sequence AVITGACERD IQCGAGTCCA ISLWLRGLRL CTPLGREGEE CHPGSHKIPF LRKRQHHTCP CSPSLLCSRF PDGRYRCFRD LKNANF Tag None Physical Appearance Sterile Filtered White lyophilized (freeze-dried) powder. Purity >95% by SDS-PAGE and HPLC analyses. Biological Activity The ED50 as Measured in a cell proliferation assay using EJG bovine adrenal-derived endothelial cells. Fully biologically active when compared to standard. Endotoxin < 0.1 EU per 1μg of the protein by the LAL method. Formulation Lyophilized from a 0.2 μm filtered concentrated solution in PBS, pH7.4, with 3% Trehalose. Reconstitution We recommend that this vial be briefly centrifuged prior to opening to bring the contents to the bottom. Reconstitute in sterile distilled water or aqueous buffer containing 0.1% BSA to a concentration of 0.1-1.0 mg/mL. Stock solutions should be apportioned into working aliquots and stored at ≤ -20℃. Further dilutions should be made in appropriate buffered solutions.   Shipping and Storage The products are shipped with ice pack and can be stored at -20℃ to -80℃ for 1 year. Recommend to aliquot the protein into smaller quantities when first used and avoid repeated freeze-thaw cycles.   Cautions 1. Avoid repeated freeze-thaw cycles. 2. For your safety and health, please wear lab coats and disposable gloves for operation. 3. For research use only!

Read more less

Fatty acid binding proteins (FABP) are small cytoplasmic lipid binding proteins that are expressed in a tissue specific manner and are involved in intracellular lipid transport. All FABPs bind free fatty acids, cholesterol, and retinoids, which differ in their selectivity, affinity and binding mechanism (1). Circulating FABP levels are used as indicators of tissue damage. Some FABP polymorphisms have been associated with disorders of lipid metabolism and the development of atherosclerosis (2). FABPs are structurally conserved, consisting of a water-filled, ligand-binding pocket surrounded by ten anti-parallel beta-barrel structures, capped by an N-terminal helix-turn-helix motif. The helical N-terminus is involved in the regulation of FA transfer from membranes (3).FABP1, also known as liver FABP (L-FABP) is highly expressed in the liver, intestine, kidney and lung (1). FABP1 binds free fatty acids and their co-enzyme A derivatives. FABP1 is unique among other members in FABP family, attributed to its ability to bind multiple ligands at once. It has a larger solvent-accessible core in comparison to other FABPs, and this allows for more diverse binding to substrates (1). Mouse FABP1 is 127 amino acids (aa) in length. It is a two beta-sheet molecule that contains an acetylated initiating methionine. Full-length mouse FABP1 shares 94% and 84% aa identity with rat and human FABP1, respectively (4).   Product Properties Synonyms FABP1; FABPL; fatty acid binding protein 1, liver; fatty acid-binding protein, liver; LFABP; L-FABP; L-FABPFatty acid-binding protein 1; Liver-type fatty acid-binding protein Accession P12710 GeneID 14080 Source E.coli-derived Mouse FABP1, with an N-terminal Met Molecular Weight Approximately 14.2 kDa. AA Sequence MNFSGKYQLQ SQENFEPFMK AIGLPEDLIQ KGKDIKGVSE IVHEGKKIKL TITYGPKVVR NEFTLGEECE LETMTGEKVK AVVKLEGDNK MVTTFKGIKS VTELNGDTIT NTMTLGDIVY KRVSKRI Tag None Physical Appearance Sterile Filtered White lyophilized (freeze-dried) powder. Purity >95% by SDS-PAGE and HPLC analyses. Biological Activity Fully biologically active when compared to standard. The binding affinity of rMuFABP1 for the synthetic ligand cis-parinaric acid has been measured by fluorescence titration. Half maximal fluorescence of 2.5 μM rMuFABP1 is achieved with approximately 5 μM cis-paranaric acid. Endotoxin < 1.0 EU per 1μg of the protein by the LAL method. Formulation Lyophilized from a 0.2 µm filtered concentrated solution in PBS, pH 7.4, 2 % trehalose. Reconstitution We recommend that this vial be briefly centrifuged prior to opening to bring the contents to the bottom. Reconstitute in sterile distilled water or aqueous buffer containing 0.1% BSA to a concentration of 0.1-1.0 mg/mL. Stock solutions should be apportioned into working aliquots and stored at ≤ -20℃. Further dilutions should be made in appropriate buffered solutions.   Shipping and Storage The products are shipped with ice pack and can be stored at -20℃ to -80℃ for 1 year. Recommend to aliquot the protein into smaller quantities when first used and avoid repeated freeze-thaw cycles.   Cautions 1. Avoid repeated freeze-thaw cycles. 2. For your safety and health, please wear lab coats and disposable gloves for operation. 3. For research use only!

Read more less

Fibroblast growth factor 16 (FGF-16) belongs to the large FGF family. All FGF family members are heparin-binding growth factors with a core 120 amino acid (a.a.) FGF domain that allows for a common tertiary structure. FGF-16 was originally identified in rat heart tissue by homology based polymerase chain reaction. Murine FGF-16 cDNA predicts a 207 aa precursor protein with one N-linked glycosylation site. FGF-16 lacks a typical signal peptide, but is efficiently generated by mechanisms other than the classical protein secretion pathway. Among FGF family members, FGF-16 is most similar to FGF-9, sharing 73% aa sequence homology. Murine FGF-16 shares 99.5% and 99% aa sequence identity with the human and rat FGF-16, respectively   Product Properties Synonyms Fibroblast growth factor 16；FGF-16 Accession Q9ESL8 GeneID 80903 Source E.coli-derived mouse FGF 16 protein, Met1-Arg207 Molecular Weight Approximately 23.8 kDa. AA Sequence MAEVGGVFAS LDWDLHGFSS SLGNVPLADS PGFLNERLGQ IEGKLQRGSP TDFAHLKGIL RRRQLYCRTG FHLEIFPNGT VHGTRHDHSR FGILEFISLA VGLISIRGVD SGLYLGMNER GELYGSKKLT RECVFREQFE ENWYNTYAST LYKHSDSERQ YYVALNKDGS PREGYRTKRH QKFTHFLPRP VDPSKLPSMS RDLFRYR Tag None Physical Appearance Sterile Filtered White lyophilized (freeze-dried) powder. Purity >98% by SDS-PAGE and HPLC analyses. Biological Activity Data not available. Endotoxin < 0.1 EU per 1μg of the protein by the LAL method. Formulation Supplied as a 0.2 μm filtered solution in 20 mM Tris-HCl, pH 9.0, 1 M NaCl, 0.02 % Tween-20, 10 % Glycerol. Reconstitution We recommend that this vial be briefly centrifuged prior to opening to bring the contents to the bottom. Reconstitute in sterile distilled water or aqueous buffer containing 0.1% BSA to a concentration of 0.1-1.0 mg/mL. Stock solutions should be apportioned into working aliquots and stored at ≤ -20℃. Further dilutions should be made in appropriate buffered solutions.   Shipping and Storage The products are shipped with ice pack and can be stored at -20℃ to -80℃ for 1 year. Recommend to aliquot the protein into smaller quantities when first used and avoid repeated freeze-thaw cycles.   Cautions 1. Avoid repeated freeze-thaw cycles. 2. For your safety and health, please wear lab coats and disposable gloves for operation. 3. For research use only!

Read more less

FGF-17 is a member of the FGF superfamily of heparin-binding mitogenic molecules characterized by the presence of a core, 120 amino acid (aa) beta-trefoil structure. The mRNA of FGF-17 was found in midgestation of embryo and multiple adult tissues, and is preferentially expressed in specific sites, such as embryonic brain, developing skeleton and arteries.   Product Properties Synonyms FGF-13 Protein; FGF-17 Protein; HH20 Protein Accession P63075 GeneID 1417 Source E.coli-derived mouse FGF 17 protein, Thr23-Thr216 Molecular Weight Approximately 22.5 kDa. AA Sequence TQGENHPSPN FNQYVRDQGA MTDQLSRRQI REYQLYSRTS GKHVQVTGRR ISATAEDGNK FAKLIVETDT FGSRVRIKGA ESEKYICMNK RGKLIGKPSG KSKDCVFTEI VLENNYTAFQ NARHEGWFMA FTRQGRPRQA SRSRQNQREA HFIKRLYQGQ LPFPNHAERQ KQFEFVGSAP TRRTKRTRRP QSQT Tag None Physical Appearance Sterile Filtered White lyophilized (freeze-dried) powder. Purity >98% by SDS-PAGE and HPLC analyses. Biological Activity Fully biologically active when compared to standard. The ED50 as determined by a cell proliferation assay using murine balb/c 3T3 cells is less than 10 ng/ml, corresponding to a specific activity of > 1.0×105 IU/mg in the presence of 10 μg/ml of heparin. Endotoxin < 0.1 EU per 1μg of the protein by the LAL method. Formulation Lyophilized from a 0.2 µm filtered concentrated solution in 20 mM Tris-HCl, pH 8.0, 700 mM NaCl, with 0.02 % Tween-20. Reconstitution We recommend that this vial be briefly centrifuged prior to opening to bring the contents to the bottom. Reconstitute in sterile distilled water or aqueous buffer containing 0.1% BSA to a concentration of 0.1-1.0 mg/mL. Stock solutions should be apportioned into working aliquots and stored at ≤ -20℃. Further dilutions should be made in appropriate buffered solutions.   Shipping and Storage The products are shipped with ice pack and can be stored at -20℃ to -80℃ for 1 year. Recommend to aliquot the protein into smaller quantities when first used and avoid repeated freeze-thaw cycles.   Cautions 1. Avoid repeated freeze-thaw cycles. 2. For your safety and health, please wear lab coats and disposable gloves for operation. 3. For research use only!

Read more less

Fibroblast Growth Factor 18 (FGF-18) is a 20 kDa protein that plays an important role in skeletal development and bone homeostasis. Mature mouse FGF-18 shares 99% amino acid sequence identity with human and rat FGF-18. It is expressed in embryonic somites and the neural fold, adult lung, cerebellar and hippocampal neurons, hair follicle root sheath cells, and osteogenic mesenchymal cells. FGF-18 binds to FGF R2c, FGF R3c as well as the Golgi protein GLG1 and induces the proliferation of astrocytes and microglia, vascular endothelial cells, dermal fibroblasts, papilla cells, and keratinocytes. FGF-18 is required for normal skeletal development. It recruits osteoclasts and osteoblasts to the growth plate, promotes osteoclast formation and function, inhibits osteoblast differentiation, promotes skeletal vascularization, and induces chondrocyte hypertrophy and cartilage matrix formation.   Product Properties Synonyms zFGF5 Accession O89101 GeneID 14172 Source E.coli-derived Mouse FGF-18, Glu28-Gly207. Molecular Weight Approximately 21.0 kDa. AA Sequence EENVDFRIHV ENQTRARDDV SRKQLRLYQL YSRTSGKHIQ VLGRRISARG EDGDKYAQLL VETDTFGSQV RIKGKETEFY LCMNRKGKLV GKPDGTSKEC VFIEKVLENN YTALMSAKYS GWYVGFTKKG RPRKGPKTRE NQQDVHFMKR YPKGQAELQK PFKYTTVTKR SRRIRPTHPG Tag None Physical Appearance Sterile Filtered White lyophilized (freeze-dried) powder. Purity >95% by SDS-PAGE and HPLC analyses. Biological Activity The ED50 as determined by thymidine uptake assay using FGF-receptors transfected BaF3 cells is less than 0.5 ng/mL, corresponding to a specific activity of > 2.0×106 IU/mg. Fully biologically active when compared to standard. Endotoxin < 1.0 EU per 1μg of the protein by the LAL method. Formulation Lyophilized from a 0.2 µm filtered concentrated solution in PBS, pH 7.4, 500 mM NaCl. Reconstitution We recommend that this vial be briefly centrifuged prior to opening to bring the contents to the bottom. Reconstitute in sterile distilled water or aqueous buffer containing 0.1% BSA to a concentration of 0.1-1.0 mg/mL. Stock solutions should be apportioned into working aliquots and stored at ≤ -20℃. Further dilutions should be made in appropriate buffered solutions.   Shipping and Storage The products are shipped with ice pack and can be stored at -20℃ to -80℃ for 1 year. Recommend to aliquot the protein into smaller quantities when first used and avoid repeated freeze-thaw cycles.   Cautions 1. Avoid repeated freeze-thaw cycles. 2. For your safety and health, please wear lab coats and disposable gloves for operation. 3. For research use only!

Read more less

Fgf-8 is a member of the fibroblast growth factor (FGF) family that was initially identified as an androgen-inducible growth factor in a mammary carcinoma cell line. Fgf-8 is one of the key signaling molecules implicated in the initiation, outgrowth, and patterning of vertebrate limbs. The cloned 1.26-kb cDNA contained an open reading frame encoding 212 amino acid residues with 84%, 86%, and 80% amino acid identities to those of Xenopus, chick, and mouse, respectively. None of the FGF-8 isoforms exhibited activity to FGFR1b, 2b, 3b, but FGFR2c, 3c and FGFR4 can be activated by several FGF-8 isoforms. FGF-8 plays an important role in the regulation of embryonic development, cell proliferation, cell differentiation and cell migration, and it is required for normal brain, eye, ear and limb development during embryogenesis. FGF-8 shows limited expression in the normal adult, but low levels are found in the reproductive and genitourinary tract, peripheral leukocytes and bone marrow hematopoietic cells.    Product Properties Synonyms AIGF, AIGFKAL6, HBGF-8, FGF-8c Accession P37237 GeneID 14179 Source E.coli-derived mouse FGF-8, Gln23-Arg268. Molecular Weight Approximately 28.1 kDa. AA Sequence QVRSAAQKRG PGAGNPADTL GQGHEDRPFG QRSRAGKNFT NPAPNYPEEG SKEQRDSVLP KVTQRHVREQ SLVTDQLSRR LIRTYQLYSR TSGKHVQVLA NKRINAMAED GDPFAKLIVE TDTFGSRVRV RGAETGLYIC MNKKGKLIAK SNGKGKDCVF TEIVLENNYT ALQNAKYEGW YMAFTRKGRP RKGSKTRQHQ REVHFMKRLP RGHHTTEQSL RFEFLNYPPF TRSLRGSQRT WAPEPR Tag None Physical Appearance Sterile Filtered White lyophilized (freeze-dried) powder. Purity >97% by SDS-PAGE and HPLC analyses. Biological Activity The ED50 as determined by a cell proliferation assay using murine balb/c 3T3 cells is less than 5.0 ng/mL, corresponding to a specific activity of >2.0×105 IU/mg in the presence of 10 μg/ml of heparin. Fully biologically active when compared to standard. Endotoxin < 1.0 EU per 1μg of the protein by the LAL method. Formulation Lyophilized from a 0.2 µm filtered concentrated solution in PBS, pH 7.4, 500 mM NaCl. Reconstitution We recommend that this vial be briefly centrifuged prior to opening to bring the contents to the bottom. Reconstitute in sterile distilled water or aqueous buffer containing 0.1% BSA to a concentration of 0.1-1.0 mg/mL. Stock solutions should be apportioned into working aliquots and stored at ≤ -20℃. Further dilutions should be made in appropriate buffered solutions.   Shipping and Storage The products are shipped with ice pack and can be stored at -20 ℃ for 1 year. 1 month, 2 to 8 °C under sterile conditions after reconstitution. 3 months, -20 °C under sterile conditions after reconstitution. Recommend to aliquot the protein into smaller quantities when first used and avoid repeated freeze-thaw cycles.   Cautions 1. Avoid repeated freeze-thaw cycles. 2. For your safety and health, please wear lab coats and disposable gloves for operation. 3. For research use only!

Read more less

CX3CL1, also named neurotactin, is a novel chemokine identified through bioinformatics. CX3CL1 has a unique C-X3-C cysteine motif near the amino-terminus and is the first member of a fourth branch of the chemokine superfamily. Unlike other known chemokines, CX3CL1 is a type 1 membrane protein containing a chemokine domain tethered on a long mucin-like stalk. The extracellular domain of human CX3CL1 can be released, possibly by proteolysis at the dibasic cleavage site proximal to the membrane, to generate soluble CX3CL1. CX3CL1 mRNA has been detected in various tissues including the brain and heart. The expression of CX3CL1 was also reported to be up-regulated in endothelial cells and microglia by inflammatory signals. Membrane-bound CX3CL1 has been shown to promote adhesion of leukocytes. The soluble chemokine domain of human CX3CL1 was reported to be chemotactic for T cells and monocytes while the soluble chemokine domain of mouse CX3CL1 was reported to chemoattract neutrophils and T-lymphocytes but not monocytes. The gene for human CX3CL1 has been mapped to chromosome 16q.     Product Properties Synonyms C-X3-C motif chemokine 1, CX3C membrane-anchored chemokine, Neurotactin, Small-inducible cytokine D1 Accession O3518 GeneID 20312 Source E.coli-derived mouse  Fractalkine/CX3CL1, Gln25-Gly100. Molecular Weight Approximately 8.7 kDa. AA Sequence QHLGMTKCEI MCGKMTSRIP VALLIRYQLN QESCGKRAIV LETTQHRRFC ADPKEKWVQD AMKHLDHQAA ALTKNG Tag None Physical Appearance Sterile Filtered White lyophilized (freeze-dried) powder. Purity >97% by SDS-PAGE and HPLC analyses. Biological Activity The ED50 as determined by a cell proliferation assay using human peripheral blood lymphocytes (PBL) is less than 0.5 μg/mL, corresponding to a specific activity of > 2000 IU/mg. Fully biologically active when compared to standard. Endotoxin < 0.1 EU per 1μg of the protein by the LAL method. Formulation Lyophilized from a 0.2 µm filtered concentrated solution in PBS, pH 7.4. Reconstitution We recommend that this vial be briefly centrifuged prior to opening to bring the contents to the bottom. Reconstitute in sterile distilled water or aqueous buffer containing 0.1% BSA to a concentration of 0.1-1.0 mg/mL. Stock solutions should be apportioned into working aliquots and stored at ≤ -20℃. Further dilutions should be made in appropriate buffered solutions.   Shipping and Storage The products are shipped with ice pack and can be stored at -20℃ to -80℃ for 1 year. Recommend to aliquot the protein into smaller quantities when first used and avoid repeated freeze-thaw cycles. Cautions 1. Avoid repeated freeze-thaw cycles. 2. For your safety and health, please wear lab coats and disposable gloves for operation. 3. For research use only!

Read more less

CXCL10 is a cytokine belonging to the CXC chemokine family. Mouse CXCL10 shares approximately 67% amino acid sequence identity with human CXCL10. CXCL10 has been shown to be a chemoattractant for activated T-lymphocytes and monocytes. It also has the effect of promoting the adhesion of T cells to endothelial cells, as well as inhibiting bone marrow colony formation and angiogenesis.   Product Properties Synonyms Gamma-IP10, Small-inducible Cytokine B10, C7, CXCL10, gIP-10, IFI10, Interferon-gamma Induced Protein CRG-2 Accession P17515 GeneID 15945 Source E.coli-derived mouse IP-10/CXCL10 protein, Ile22-Pro98. Molecular Weight Approximately 8.7 kDa. AA Sequence IPLARTVRCN CIHIDDGPVR MRAIGKLEII PASLSCPRVE IIATMKKNDE QRCLNPESKT IKNLMKAFSQ KRSKRAP Tag None Physical Appearance Sterile Filtered White lyophilized (freeze-dried) powder. Purity >97% by SDS-PAGE and HPLC analyses. Biological Activity The biologically active determined by a chemotaxis bioassay using human peripheral blood lymphocytes is in a concentration range of 0.1-10.0 ng/mL in the presence of IL-2.   Endotoxin < 1.0 EU per 1μg of the protein by the LAL method. Formulation Lyophilized from a 0.2 µm filtered concentrated solution in PBS, pH 7.4. Reconstitution We recommend that this vial be briefly centrifuged prior to opening to bring the contents to the bottom. Reconstitute in sterile distilled water or aqueous buffer containing 0.1% BSA to a concentration of 0.1-1.0 mg/mL. Stock solutions should be apportioned into working aliquots and stored at ≤ -20℃. Further dilutions should be made in appropriate buffered solutions.   Shipping and Storage The products are shipped with ice pack and can be stored at -20℃ for 1 year. 1 month, 2 to 8 °C under sterile conditions after reconstitution. 3 months, -20 °C under sterile conditions after reconstitution. Recommend to aliquot the protein into smaller quantities when first used and avoid repeated freeze-thaw cycles. Cautions 1. Avoid repeated freeze-thaw cycles. 2. For your safety and health, please wear lab coats and disposable gloves for operation. 3. For research use only!

Read more less

IL- 28A (Interferon-lambda 2; IFN-lambda 2), IL-28B/IFN-lambda 3, and IL-29/IFN-lambda 1 are type III interferons which are distantly related to IL-10 family and type I IFN family cytokines. Mature human IL-28A is an approximately 22-25 kDa protein that shares 66% amino acid (aa) sequence identity with mouse and rat IL-28A and shows cross-species activity. It shares 96% and 70% aa sequence identity with human IL-28B and IL-29, respectively. Type III interferons are upregulated in response to viral infection, and they act predominantly on epithelial cells through a receptor complex that contains IL-10 R beta and IL-28 R alpha /IFN-gamma R1. Type III IFNs function as anti-viral molecules and induce the upregulation of MHC class I antigen. IL-28A promotes the Th1 polarization of dendritic cells in the airway (e.g. production of IL-12 p70 and IFN-gamma ) and inhibits Th2 and Th17 mediated inflammation. In the liver, however, the IL-28A induced Th1 cytokine response contributes to inflammation in T cell mediated hepatitis. IL-28A additionally exhibits anti-tumor activity, in part by enhancing IL-12 dependent anti-tumor CTL responses in vivo. In contrast, it is up-regulated in invasive bladder cancer where it promotes tumor cell migration   Product Properties Synonyms Interleukin 28A；Interferon lambda-2；Interleukin-28A；IFN-lambda-2 Accession Q4VK74 GeneID 330496 Source E.coli-derived Mouse IFN-λ2/IL-28A, Asp20-Val193 Molecular Weight Approximately 19.7 kDa. AA Sequence DPVPRATRLP VEAKDCHIAQ FKSLSPKELQ AFKKAKDAIE KRLLEKDMRC SSHLISRAWD LKQLQVQERP KALQAEVALT LKVWENMTDS ALATILGQPL HTLSHIHSQL QTCTQLQATA EPKPPSRRLS RWLHRLQEAQ SKETPGCLED SVTSNLFRLL TRDLKCVASG DQCV Tag None Physical Appearance Sterile Filtered White lyophilized (freeze-dried) powder. Purity >95% by SDS-PAGE and HPLC analyses. Biological Activity Fully biologically active when compared to standard. The ED50 as determined by an anti-viral assay usinghuman HepG2 cells infected with encephalomyocarditis is less than 3 ng/ml, corresponding to a specificactivity of > 3.3 × 105 IU/mg. Endotoxin < 0.1 EU per 1μg of the protein by the LAL method. Formulation Lyophilized from a 0.2 µm filtered concentrated solution in PBS, pH 7.4, with 5 % trehalose. Reconstitution We recommend that this vial be briefly centrifuged prior to opening to bring the contents to the bottom. Reconstitute in sterile distilled water or aqueous buffer containing 0.1% BSA to a concentration of 0.1-1.0 mg/mL. Stock solutions should be apportioned into working aliquots and stored at ≤ -20℃. Further dilutions should be made in appropriate buffered solutions.   Shipping and Storage The products are shipped with ice pack and can be stored at -20℃ to -80℃ for 1 year. Recommend to aliquot the protein into smaller quantities when first used and avoid repeated freeze-thaw cycles. Cautions 1. Avoid repeated freeze-thaw cycles. 2. For your safety and health, please wear lab coats and disposable gloves for operation. 3. For research use only!

Read more less

Fibroblast growth factor-9, also called FGF-9, is an approximately 26 kDa secreted glycoprotein of the FGF family. Secreted human FGF-9 is a 205-207 aa protein that lacks the N-terminal 1-3 aa and shares 98% sequence identity with mouse, rat, equine, porcine and bovine FGF-9. In addition to FGF R3 (IIIb), FGF-9 binding to the IIIc splice forms of FGF R1, R2 and R3 are variably reported. FGF-9 is an autocrine/paracrine growth factor considered to be important for the growth and survival of motorneurons and prostate. Meanwhile, FGF9 is a potent mitogen and survival factor required for morphogenesis during embryonic development and numerous biological functions at adulthood. FGF9 have been shown to improve systolic function after myocardial infarction in a clinical trial. FGF9 promotes cardiac vascularization during embryonic development but is only weakly expressed in the adult heart.   Product Properties Synonyms FGF9, FGF-9, Glia-activating factor, GAF, glia-activating factor, HBFG-9, HBGF-9 Accession P54130 GeneID 14180 Source E.coli-derived mouse FGF-9, Pro3-Ser208, with an N-terminal Met. Molecular Weight Approximately 23.4 kDa. AA Sequence MPLGEVGSYF GVQDAVPFGN VPVLPVDSPV LLNDHLGQSE AGGLPRGPAV TDLDHLKGIL RRRQLYCRTG FHLEIFPNGT IQGTRKDHSR FGILEFISIA VGLVSIRGVD SGLYLGMNEK GELYGSEKLT QECVFREQFE ENWYNTYSSN LYKHVDTGRR YYVALNKDGT PREGTRTKRH QKFTHFLPRP VDPDKVPELY KDILSQS Tag None Physical Appearance Sterile Filtered White lyophilized (freeze-dried) powder. Purity >95% by SDS-PAGE and HPLC analyses. Biological Activity The ED50 as determined by thymidine uptake assay using FGF-receptors transfected BaF3 cells is less than0.5 ng/mL, corresponding to a specific activity of > 2.0×106 IU/mg. Fully biologically active whencompared to standard. Endotoxin < 1.0 EU per 1μg of the protein by the LAL method. Formulation Lyophilized from a 0.2 μm filtered concentrated solution in 20 mM Tris, 500 mM NaCl, pH 8.5. Reconstitution We recommend that this vial be briefly centrifuged prior to opening to bring the contents to the bottom. Reconstitute in sterile distilled water or aqueous buffer containing 0.1% BSA to a concentration of 0.1-1.0 mg/mL. Stock solutions should be apportioned into working aliquots and stored at ≤ -20℃. Further dilutions should be made in appropriate buffered solutions.   Shipping and Storage The products are shipped with ice pack and can be stored at -20℃ to -80℃ for 1 year. Recommend to aliquot the protein into smaller quantities when first used and avoid repeated freeze-thaw cycles. Cautions 1. Avoid repeated freeze-thaw cycles. 2. For your safety and health, please wear lab coats and disposable gloves for operation. 3. For research use only!

Read more less

The glia maturation factor beta belongs to the actin-binding proteins ADF family, GMF subfamily. It contains an ADF-H domain, but the research of crystallography and NMR reveals that there are structures different between human and mouse ADF-H domain. GMF-β is involved in the differentiation, maintenance, and regeneration of the nervous system. It also inhibition of proliferation of tumor cells.   Product Properties Synonyms Glia maturation factor beta, GMF-beta, GMFB Accession Q9CQI3 GeneID 63985 Source E.coli-derived mouse Glia Maturation Factor beta protein, Ser-His142 Molecular Weight Approximately 16.6 kDa. AA Sequence SESLVVCDVA EDLVEKLRKF RFRKETHNAA IIMKIDKDER LVVLDEELEG VSPDELKDEL PERQPRFIVY SYKYQHDDGR VSYPLCFIFS SPVGCKPEQQ MMYAGSKNKL VQTAELTKVF EIRNTEDLTE EWLREKLGFF H Tag None Physical Appearance Sterile Filtered White lyophilized (freeze-dried) powder. Purity >97% by SDS-PAGE and HPLC analyses. Biological Activity Data not available.   Endotoxin < 1.0 EU per 1μg of the protein by the LAL method. Formulation Lyophilized from a 0.2 μm filtered concentrated solution in PBS, pH 7.4. Reconstitution We recommend that this vial be briefly centrifuged prior to opening to bring the contents to the bottom. Reconstitute in sterile distilled water or aqueous buffer containing 0.1% BSA to a concentration of 0.1-1.0 mg/mL. Stock solutions should be apportioned into working aliquots and stored at ≤ -20℃. Further dilutions should be made in appropriate buffered solutions.   Shipping and Storage The products are shipped with ice pack and can be stored at -20℃ to -80℃ for 1 year. Recommend to aliquot the protein into smaller quantities when first used and avoid repeated freeze-thaw cycles. Cautions 1. Avoid repeated freeze-thaw cycles. 2. For your safety and health, please wear lab coats and disposable gloves for operation. 3. For research use only!

Read more less

Glial cell line-derived neurotrophic factor (GDNF) is a glycosylated, disulfide-bonded homodimer that is a distantly related member of the transforming growth factor-β superfamily. It is a founding member of the GDNF family of ligands (GFL) and has been shown to interact with GFRA2 and GDNF family receptor alpha. Mature rat and human GDNF exhibit approximately 93% amino acid sequence identity and show considerable species cross-reactivity. Cells known to express GDNF include Sertoli cells, type 1 astrocytes, Schwann cells, neurons, pinealocytes and skeletal muscle cells. In embryonic midbrain cultures, recombinant human GDNF promoted the survival and morphological differentiation of dopaminergic neurons and increased their high-affinity dopamine uptake.   Product Properties Synonyms Astrocyte-derived trophic factor, ATF, ATF-1, ATF2, GDNF, HFB1-GDNF, HGDNF, HSCR3 Accession P48540 GeneID 14573 Source E.coli-derived mouse GDNF, Ser78-Ile211. Molecular Weight Approximately 29.9 kDa. AA Sequence SPDKQAAALP RRERNRQAAA ASPENSRGKG RRGQRGKNRG CVLTAIHLNV TDLGLGYETK EELIFRYCSG SCESAETMYD KILKNLSRSR RLTSDKVGQA CCRPVAFDDD LSFLDDNLVY HILRKHSAKR CGCI Tag None Physical Appearance Sterile Filtered White lyophilized (freeze-dried) powder. Purity >95% by SDS-PAGE and HPLC analyses. Biological Activity The ED50 as determined by a cell proliferation assay using rat C6 cells is less than 0.2 ng/mL, corresponding to a specific activity of > 5.0 × 106 IU/mg. Fully biologically active when compared to standard. Endotoxin < 0.1 EU per 1μg of the protein by the LAL method. Formulation Lyophilized from a 0.2 μm filtered concentrated solution in PBS, pH 7.4, with 0.05% Tween-20. Reconstitution We recommend that this vial be briefly centrifuged prior to opening to bring the contents to the bottom. Reconstitute in sterile distilled water or aqueous buffer containing 0.1% BSA to a concentration of 0.1-1.0 mg/mL. Stock solutions should be apportioned into working aliquots and stored at ≤ -20℃. Further dilutions should be made in appropriate buffered solutions.   Shipping and Storage The products are shipped with ice pack and can be stored at -20℃ to -80℃ for 1 year. Recommend to aliquot the protein into smaller quantities when first used and avoid repeated freeze-thaw cycles. Cautions 1. Avoid repeated freeze-thaw cycles. 2. For your safety and health, please wear lab coats and disposable gloves for operation. 3. For research use only!

Read more less

Growth Differentiation Factor-5 (GDF-5; also called BMP-14 and CDMP-1) is a member of the BMP family of TGF-beta superfamily proteins. Mature mouse GDF-5 shares 99% aa sequence identity with both mature human and rat GDF-5. Growth/differentiation factors (GDF-1 to GDF-15) are members of the BMP family of TGF-beta superfamily proteins. They are produced as inactive preproproteins which are then cleaved and assembled into active secreted homodimers. GDF dimers are disulfide-linked with the exception of GDF-3 and -9. GDF proteins are important during embryonic development, particularly in the skeletal, nervous, and muscular systems. GDF-5 is involved in multiple developmental processes including limb generation, cartilage development, joint formation, bone morphogenesis, cell survival, and neuritogenesis.   Product Properties Synonyms CDMP-1, GDF5, OS5, radotermin, SYNS2 Accession P43027 GeneID 14563 Source E.coli-derived mouse GDF-5/BMP-14 protein, Ala376-Arg495. Molecular Weight Approximately 27.2 kDa. AA Sequence APLANRQGKR PSKNLKARCS RKALHVNFKD MGWDDWIIAP LEYEAFHCEG LCEFPLRSHL EPTNHAVIQT LMNSMDPEST PPTCCVPTRL SPISILFIDS ANNVVYKQYE DMVVESCGCR Tag None Physical Appearance Sterile Filtered White lyophilized (freeze-dried) powder. Purity >96% by SDS-PAGE and HPLC analyses. Biological Activity The ED50 as determined by inducing alkaline phosphatase production of mouse ATDC5 cells is less than 1.0 μg/ml, corresponding to a specific activity of > 1000 IU/mg. Fully biologically active when compared to standard.  Endotoxin < 0.1 EU per 1μg of the protein by the LAL method. Formulation Lyophilized from a 0.2 μm filtered concentrated solution in 30% Acetonitrile and 0.1% TFA. Reconstitution We recommend that this vial be briefly centrifuged prior to opening to bring the contents to the bottom. Reconstitute in sterile distilled water or aqueous buffer containing 0.1% BSA to a concentration of 0.1-1.0 mg/mL. Stock solutions should be apportioned into working aliquots and stored at ≤ -20℃. Further dilutions should be made in appropriate buffered solutions.   Shipping and Storage The products are shipped with ice pack and can be stored at -20℃ to -80℃ for 1 year. Recommend to aliquot the protein into smaller quantities when first used and avoid repeated freeze-thaw cycles. Cautions 1. Avoid repeated freeze-thaw cycles. 2. For your safety and health, please wear lab coats and disposable gloves for operation. 3. For research use only!

Read more less

Growth/differentiation factors (GDF-1 to GDF-15) are members of the BMP family of TGF-beta superfamily proteins. At the amino acid level, mature human GDF-7 shares 85% and 88% aa sequence identity with mature GDF-7 in mouse and rat. They are produced as inactive preproproteins which are then cleaved and assembled into active secreted homodimers. GDF dimers are disulfide-linked with the exception of GDF-3 and -9. GDF proteins are important during embryonic development, particularly in the skeletal, nervous, and muscular systems. GDF-7 is involved in tendon and ligament formation and repair. GDF-7 also regulates bone formation, mesenchymal stem cell differentiation, neuronal differentiation, and axon guidance in the central nervous system.   Product Properties Synonyms BMP12, GDF7, growth differentiation factor 7 Accession P43029 GeneID 238057 Source E.coli-derived mouse GDF-7/BMP-12 protein, Thr316-Arg461. Molecular Weight Approximately 29.8 kDa. AA Sequence TALAGTRGAQ GSGGGGGGGG GGGGGGGGGG GGAGRGHGRR GRSRCSRKSL HVDFKELGWD DWIIAPLDYE AYHCEGVCDF PLRSHLEPTN HAIIQTLLNS MAPDAAPASC CVPARLSPIS ILYIDAANNV VYKQYEDMVV EACGCR Tag None Physical Appearance Sterile Filtered White lyophilized (freeze-dried) powder. Purity >95% by SDS-PAGE and HPLC analyses. Biological Activity The ED50 as determined by inducing alkaline phosphatase production of mouse ATDC5 cells is less than 0.5 μg/ml, corresponding to a specific activity of > 2000 IU/mg. Fully biologically active when compared to standard.  Endotoxin < 0.1 EU per 1μg of the protein by the LAL method. Formulation Lyophilized from a 0.2 μm filtered concentrated solution in 30% Acetonitrile and 0.1% TFA. Reconstitution We recommend that this vial be briefly centrifuged prior to opening to bring the contents to the bottom. Reconstitute in sterile distilled water or aqueous buffer containing 0.1% BSA to a concentration of 0.1-1.0 mg/mL. Stock solutions should be apportioned into working aliquots and stored at ≤ -20℃. Further dilutions should be made in appropriate buffered solutions.   Shipping and Storage The products are shipped with ice pack and can be stored at -20℃ to -80℃ for 1 year. Recommend to aliquot the protein into smaller quantities when first used and avoid repeated freeze-thaw cycles. Cautions 1. Avoid repeated freeze-thaw cycles. 2. For your safety and health, please wear lab coats and disposable gloves for operation. 3. For research use only!

Read more less

Insulin-like Growth Factor I (IGF-I), is the dominant effector of Growth Hormone (GH) and is structurally homologous to Proinsulin. The 7.6 kDa mature IGF-I is identical between isoforms and is generated by proteolytic removal of the N- and C-terminal regions. Mature human IGF-I shares 94% and 96% amino acid (aa) sequence identity with the mouse and rat orthologs, respectively. The body growth of animals is regulated by growth hormone and IGF-I. The classical theory of this regulation is that most IGF-I in the blood originates in the liver and that body growth is controlled by the concentration of IGF-I in the blood. Meanwhile, IGF-I has been shown to enhance neuronal survival and inhibit apoptosis. IGF-1 promote the proliferation of multiple myeloma (MM) cells and protect them against dexamethasone (Dex)-induced apoptosis.   Product Properties Synonyms Somatomedin C, IGF-I, IGF-IA, Mechano growth factor, MGF Accession P05017 GeneID 16000 Source E.coli-derived mouse IGF-1 protein, Gly49-Ala118. Molecular Weight Approximately 7.7 kDa. AA Sequence GPETLCGAEL VDALQFVCGP RGFYFNKPTG YGSSIRRAPQ TGIVDECCFR SCDLRRLEMY CAPLKPTKAA Tag None Physical Appearance Sterile Filtered White lyophilized (freeze-dried) powder. Purity >97% by SDS-PAGE and HPLC analyses. Biological Activity The ED50 as determined by a cell proliferation assay using serum free human MCF-7 cells is less than 2 ng/mL, corresponding to a specific activity of > 5.0×105 IU/mg. Fully biologically active when comparedto standard. Endotoxin < 0.1 EU per 1μg of the protein by the LAL method. Formulation Lyophilized from a 0.2 μm filtered concentrated solution in PBS, pH 7.4. Reconstitution We recommend that this vial be briefly centrifuged prior to opening to bring the contents to the bottom. Reconstitute in sterile distilled water or aqueous buffer containing 0.1% BSA to a concentration of 0.1-1.0 mg/mL. Stock solutions should be apportioned into working aliquots and stored at ≤ -20℃. Further dilutions should be made in appropriate buffered solutions.   Shipping and Storage The products are shipped with ice pack and can be stored at -20℃ to -80℃ for 1 year. Recommend to aliquot the protein into smaller quantities when first used and avoid repeated freeze-thaw cycles. Cautions 1. Avoid repeated freeze-thaw cycles. 2. For your safety and health, please wear lab coats and disposable gloves for operation. 3. For research use only!

Read more less

Epidermal growth factor (EGF) is a small, potent growth factor capable of inducing cell proliferation, differentiation, and survival. EGF is the founding member of the EGF family that also includes TGF-alpha, amphiregulin (AR), betacellulin (BTC), epiregulin (EPR), heparin- binding EGF-like growth factor (HB-EGF), epigen, and the neuregulins (NRG)-1 through -6. Members of The EGF family are characterized by a shared structural motif, the EGF-like domain, which contains three intramolecular disulfide bonds that are formed by six similarly spaced, conserved cysteine residues. These disulfide bonds are essential for proper protein conformation and receptor binding. All EGF family members are synthesized as type I transmembrane precursor proteins that may contain several EGF domains in the extracellular region. The mature proteins are released from the cell surface by regulated proteolysis. The full length EGF protein is 1207 amino acids (aa) (EGF precursor) containing nine EGF domains and nine LDLR class B repeats. However, the mature protein is much smaller, only 53 aa, and is generated by proteolytic cleavage of the EGF domain proximal to the transmembrane region. EGF is well conserved across mammals with mature human EGF 70% identical to mature mouse and rat EGF. Physiologically, EGF is found in various body fluids, including blood, milk, urine, saliva, seminal fluid, pancreatic juice, cerebrospinal fluid, and amniotic fluid. EGF is a high affinity ligand of the EGF receptor (ErbB). Four ErbB (HER) family receptor tyrosine kinases including EGFR/ErbB1, ErbB2, ErbB3 and ErbB4, mediate responses to EGF family members. EGF binding induces dimerization of the EGF receptor resulting in activation of the protein tyrosine kinase signaling pathway. These receptors undergo a complex pattern of ligand-induced homo- or hetero-dimerization to transduce EGF family signals. EGF binds ErbB1 and depending on the context, induces the formation of homodimers or heterodimers containing ErbB2.     Product Properties Synonyms Urogastrone, URG Accession P01132 GeneID 13645 Source E.coli-derived Mouse EGF, Asn977-Arg1029. Molecular Weight Approximately 6.0 kDa. AA Sequence NSYPGCPSSY DGYCLNGGVC MHIESLDSYT CNCVIGYSGD RCQTRDLRWW ELR Tag None Physical Appearance Sterile Filtered White lyophilized (freeze-dried) powder. Purity >97% by SDS-PAGE and HPLC analyses. Biological Activity The ED50 as determined by a cell proliferation assay using murine Balb/c 3T3 cells is less than 0.1 ng/mL, corresponding to a specific activity of > 1.0×107 IU/mg. Fully biologically active when compared tostandard. Endotoxin < 1.0 EU per 1μg of the protein by the LAL method. Formulation Lyophilized from a 0.2 μm filtered concentrated solution in PBS, pH 7.4. Reconstitution We recommend that this vial be briefly centrifuged prior to opening to bring the contents to the bottom. Reconstitute in sterile distilled water or aqueous buffer containing 0.1% BSA to a concentration of 0.1-1.0 mg/mL. Stock solutions should be apportioned into working aliquots and stored at ≤ -20℃. Further dilutions should be made in appropriate buffered solutions.   Shipping and Storage The products are shipped with ice pack and can be stored at -20 ℃ for 1 year. 1 month, 2 to 8 °C under sterile conditions after reconstitution. 3 months, -20 °C under sterile conditions after reconstitution. Recommend to aliquot the protein into smaller quantities when first used and avoid repeated freeze-thaw cycles. Cautions 1. Avoid repeated freeze-thaw cycles. 2. For your safety and health, please wear lab coats and disposable gloves for operation. 3. For research use only!

Read more less

Interferon-gamma (IFN-γ), also known as Type II interferon or immune interferon, is a pleiotropic cytokine which is now recognised as an important modulator of the immune response. Mature human IFN-γ exists as a non-covalently linked homodimer of 20-25 kDa variably glycosylated subunits.    Product Properties Synonyms Interferon-gamma, IFN-γ, IFG, IFI, IFNG, IFNgamma, IFN-gamma. Accession P01580 GeneID 15978 Source E.coli-derived mouse IFN-γ protein, His23-Cys155. Molecular Weight Approximately 15.5 kDa. AA Sequence HGTVIESLES LNNYFNSSGI DVEEKSLFLD IWRNWQKDGD MKILQSQIIS FYLRLFEVLK DNQAISNNIS VIESHLITTF FSNSKAKKDA FMSIAKFEVN NPQVQRQAFN ELIRVVHQLL PESSLRKRKR SRC Tag None Physical Appearance Sterile Filtered White lyophilized (freeze-dried) powder. Purity >96% by SDS-PAGE  analyses. Biological Activity The ED50 as determined by an anti-viral assay using murine L929 cells infected with encephalomyocarditis (EMC) virus is less than 0.8 ng/ml, corresponding to a specific activity of > 1.3×106 IU/mg. Fully biologically active when compared tostandard. Endotoxin < 1.0 EU per 1μg of the protein by the LAL method. Formulation Lyophilized from a 0.2 μm filtered concentrated solution in PBS, pH 7.4. Reconstitution We recommend that this vial be briefly centrifuged prior to opening to bring the contents to the bottom. Reconstitute in sterile distilled water or aqueous buffer containing 0.1% BSA to a concentration of 0.1-1.0 mg/mL. Stock solutions should be apportioned into working aliquots and stored at ≤ -20℃. Further dilutions should be made in appropriate buffered solutions.   Shipping and Storage The products are shipped with ice pack and can be stored at -25~-15℃ for 1 year. 1 month, 2 to 8 °C under sterile conditions after reconstitution. 3 months, -25~-15℃ under sterile conditions after reconstitution. Recommend to aliquot the protein into smaller quantities when first used and avoid repeated freeze-thaw cycles. Cautions 1. Avoid repeated freeze-thaw cycles. 2. For your safety and health, please wear lab coats and disposable gloves for operation. 3. For research use only!

Read more less

CX3CL1, also named neurotactin, is a novel chemokine identified through bioinformatics. CX3CL1 has a unique C-X3-C cysteine motif near the amino-terminus and is the first member of a fourth branch of the chemokine superfamily. Unlike other known chemokines, CX3CL1 is a type 1 membrane protein containing a chemokine domain tethered on a long mucin-like stalk. The extracellular domain of human CX3CL1 can be released, possibly by proteolysis at the dibasic cleavage site proximal to the membrane, to generate soluble CX3CL1. CX3CL1 mRNA has been detected in various tissues including the brain and heart. The expression of CX3CL1 was also reported to be up-regulated in endothelial cells and microglia by inflammatory signals. Membrane-bound CX3CL1 has been shown to promote adhesion of leukocytes. The soluble chemokine domain of human CX3CL1 was reported to be chemotactic for T cells and monocytes while the soluble chemokine domain of mouse CX3CL1 was reported to chemoattract neutrophils and T-lymphocytes but not monocytes. The gene for human CX3CL1 has been mapped to chromosome 16q.   Product Properties Synonyms C-X3-C motif chemokine 1, CX3C membrane-anchored chemokine, Neurotactin, Small-inducible cytokine D1 Accession cytokine D1 GeneID 20312 Source E.coli-derived Mouse Fractalkine/CX3CL1, Gln25-Gly100. Molecular Weight Approximately 8.7 kDa. AA Sequence QHLGMTKCEI MCGKMTSRIP VALLIRYQLN QESCGKRAIV LETTQHRRFC ADPKEKWVQD AMKHLDHQAA ALTKNG Tag None Physical Appearance Sterile Filtered White lyophilized (freeze-dried) powder. Purity > 97% by SDS-PAGE and HPLC analyses. Biological Activity The ED50 as determined by a cell proliferation assay using human peripheral blood lymphocytes (PBL) is less than 0.5 μg/mL, corresponding to a specific activity of > 2000 IU/mg. Fully biologically active when compared to standard. Endotoxin < 1.0 EU per 1μg of the protein by the LAL method. Formulation Lyophilized from a 0.2 μm filtered concentrated solution in PBS, pH 7.4. Reconstitution We recommend that this vial be briefly centrifuged prior to opening to bring the contents to the bottom. Reconstitute in sterile distilled water or aqueous buffer containing 0.1% BSA to a concentration of 0.1-1.0 mg/mL. Stock solutions should be apportioned into working aliquots and stored at ≤ -20℃. Further dilutions should be made in appropriate buffered solutions.   Shipping and Storage The products are shipped with ice pack and can be stored at -20℃ to -80℃ for 1 year. Recommend to aliquot the protein into smaller quantities when first used and avoid repeated freeze-thaw cycles Cautions 1. Avoid repeated freeze-thaw cycles. 2. For your safety and health, please wear lab coats and disposable gloves for operation. 3. For research use only!

Read more less

Heparin-binding epidermal growth factor (HB-EGF)-like growth factor (EGF) is found in cerebral neurons. Human HB-EGF- shares 76% and 73% aa sequence identity with rat and mouse HB-EGF. Its expression is increased after hypoxic or ischemic injury, which also stimulates neurogenesis. HB-EGF has been implicated as a participant in a variety of normal physiological processes such as blastocyst implantation and wound healing, and in pathological processes such as tumor growth, SMC hyperplasia and atherosclerosis. The protein is an 86 amino acid mitogenic and chemotactic glycoprotein containing an EGF-like domain with six conserved cysteine residues.   Product Properties Synonyms HBEGF, DT-R Accession Q06186 GeneID 15200 Source E.coli-derived mouse HB-EGF protein, Asp63-Leu148. Molecular Weight Approximately 9.8 kDa. AA Sequence DLEGTDLNLF KVAFSSKPQG LATPSKERNG KKKKKGKGLG KKRDPCLRKY KDYCIHGECR YLQEFRTPSC KCLPGYHGHR CHGLTL Tag None Physical Appearance Sterile Filtered White lyophilized (freeze-dried) powder. Purity > 97% by SDS-PAGE and HPLC analyses. Biological Activity The ED50 as determined by a cell proliferation assay using mouse Balb/c 3T3 cells is less than 1 ng/mL, corresponding to a specific activity of > 1.0 × 106 IU/mg. Fully biologically active when compared tostandard. Endotoxin < 1.0 EU per 1μg of the protein by the LAL method. Formulation Lyophilized from a 0.2 μm filtered concentrated solution in 10 mM PBS, 500 mM NaCl, pH7.4. Reconstitution We recommend that this vial be briefly centrifuged prior to opening to bring the contents to the bottom. Reconstitute in sterile distilled water or aqueous buffer containing 0.1% BSA to a concentration of 0.1-1.0 mg/mL. Stock solutions should be apportioned into working aliquots and stored at ≤ -20℃. Further dilutions should be made in appropriate buffered solutions.   Shipping and Storage The products are shipped with ice pack and can be stored at -20℃ to -80℃ for 1 year. Recommend to aliquot the protein into smaller quantities when first used and avoid repeated freeze-thaw cycles. Cautions 1. Avoid repeated freeze-thaw cycles. 2. For your safety and health, please wear lab coats and disposable gloves for operation. 3. For research use only!

Read more less