Products

IGF-BPs control the distribution, function and activity of IGFs in various cell tissues and body fluids. IGF-BP4 is the major IGF-BP produced by osteoblasts, and is found in the epidermis, ovarian follicles,  and other tissues.  IGF-BP4 inhibits the activity  of IGF-I and IGF-II by binding in a manner that results in the formation of complexes with reduced ability to signal through cell surface IGF receptors. IGF-BP4 can inhibit the growth of chick pelvis cartilage and HT29 colon adenocarcinoma  cells  by  blocking  the mitogenic actions of IGFs, and has also been shown to reduce colony formation by colorectal cancer cells via an IGF-independent pathway. The biological effects of IGF-BP4 can be regulated by Pregnancy Associated Plasma Protein A (PAPP-A), which reduces IGF-BP4/IGF binding affinity by proteolytically cleaving IGF-BP4. The modulation of IGF-BP4 activity by  PAPP-A  is  an important component in the regulation of ovarian folliculogenesis and  in  the  growth  inhibition  of  responding  ovarian  cancer cells. Recombinant Human IGF-BP4 is a 25.7 kDa protein consisting of 237 amino acid residues including, the IGF-BP domain and thyroglobulin type-I domain.   Product Properties Synonyms Insulin-like Growth Factor-Binding Protein 4, IBP-4, HT29-IGF-BP, colon cancer cell growth inhibitor Accession P22692 GeneID 3487 Source Insect Cell-derived Human IGF-BP4 protein,Asp22-Glu258. Molecular Weight Approximately 30 kDa. AA Sequence DEAIHCPPCS EEKLARCRPP VGCEELVREP GCGCCATCAL GLGMPCGVYT PRCGSGLRCY PPRGVEKPLH TLMHGQGVCM ELAEIEAIQE SLQPSDKDEG DHPNNSFSPC SAHDRRCLQK HFAKIRDRST SGGKMKVNGA PREDARPVPQ GSCQSELHRA LERLAASQSR THEDLYIIPI PNCDRNGNFH PKQCHPALDG QRGKCWCVDR KTGVKLPGGL EPKGELDCHQ LADSFRE 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 ED50 as determined by its ability to inhibit IGF-II induced proliferation of MCF-7 cells is less than 0.1 μg/mL, corresponding to a specific  activity  of > 1.0 × 104 IU/mg in the presence of 14 ng/ml of rHuIGF-II. Endotoxin < 0.1 EU per 1μg of the protein by the LAL method. Formulation Lyophilized from a 0.2 μm filtered concentrated solution in 20mM Tris-HCl, pH 8.0, 150mM 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 °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!

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IGF-BPs control the distribution, function and activity of IGFs in various cell tissues and body fluids. Currently, there are seven named IGF-BPs that form high affinity complexes with both IGF-I and IGF-II. IGF-BP5 is a 28.6 kDa,  cysteine-rich, secreted  protein produced by vascular smooth muscle cells. It is the major IGF-binding protein present in bone tissue and helps potentiate the action of IGF-I on smooth muscle cells, fibroblasts, and osteoblasts. Data shows that IGFBP-5 acts as a growth inhibitor and pro-apoptotic agent in breast cancer cells. IGFBP-5-overexpressing mice show an increase in neonatal mortality, reduced female fertility, whole-body growth inhibition, and retarded muscle development. Recombinant Human IGF-BP5 is a 28.6 kDa protein consisting of 253 amino acid residues.   Product Properties Synonyms Human IGF-BP5 Accession P24593 GeneID 3488 Source E.coli-derived HumanIGF-BP5 protein,Leu21-Glu272. Molecular Weight Approximately 28.6 kDa. AA Sequence LGSFVHCEPC DEKALSMCPP SPLGCELVKE PGCGCCMTCA LAEGQSCGVY TERCAQGLRC LPRQDEEKPL HALLHGRGVC LNEKSYREQV KIERDSREHE EPTTSEMAEE TYSPKIFRPK HTRISELKAE AVKKDRRKKL TQSKFVGGAE NTAHPRIISA PEMRQESEQG PCRRHMEASL QELKASPRMV PRAVYLPNCD RKGFYKRKQC KPSRGRKRGI CWCVDKYGMK LPGMEYVDGD FQCHTFDSSN VE 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 its ability to inhibit IGF-II induced proliferation of MCF-7 cells is less than 0.4 μg/mL, corresponding to a specific activity of > 2500 IU/mg in the presence of 15 ng/mL of rHuIGF-II. Endotoxin < 0.1 EU per 1μg of the protein by the LAL method. Formulation Lyophilized from a 0.2 μm filtered concentrated solution in 10 mM Sodium Citrate, pH 3.0. 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!

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IGF-BPs control the distribution, function and activity of IGFs in various cell tissues and body fluids. Currently, there are seven named IGF-BPs that form high affinity complexes with both IGF-I and IGF-II. IGF-BP7 is expressed in a wide range of normal human tissues, and it generally shows reduced expression in cancer cell lines of prostate, breast, colon, and lung origin.  It plays a  role in skeletal myogenesis by binding to IGF in a manner that inhibits IGF-induced differentiation of skeletal myoblasts, without affecting IGF-induced proliferation. Additionally, IGF-BP7 suppresses growth and colony formation of prostate and breast  cancer cell lines through an IGF-independent mechanism, which causes a delay in the G1 phase of the cell cycle and increased apoptosis. Recombinant Human IGF-BP7 is a 26.4 kDa protein consisting of 256 amino acid residues.   Product Properties Synonyms Insulin-like Growth Factor-Binding Protein 7, IBP-7, Mac25, IGF binding protein related protein-1 (IGFBP-rP1) Accession Q16270 GeneID 3490 Source E.coli-derived HumanIGF-BP7 protein,Leu21-Glu282. Molecular Weight Approximately 26.4 kDa. AA Sequence SSSDTCGPCE PASCPPLPPL GCLLGETRDA CGCCPMCARG EGEPCGGGGA GRGYCAPGME CVKSRKRRKG KAGAAAGGPG VSGVCVCKSR YPVCGSDGTT YPSGCQLRAA SQRAESRGEK AITQVSKGTC EQGPSIVTPP KDIWNVTGAQ VYLSCEVIGI PTPVLIWNKV KRGHYGVQRT ELLPGDRDNL AIQTRGGPEK HEVTGWVLVS PLSKEDAGEY ECHASNSQGQ ASASAKITVV DALHEIPVKK GEGAEL Tag None Physical Appearance Sterile Filtered White lyophilized (freeze-dried) powder. Purity > 95 % 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 20 mM Tris-HCl, pH 8.6, 150 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 °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!

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IFNA1, also known as IFN-alpha and IFNA, belongs to the alpha/beta interferon family. Interferons(IFNs) are proteins made and released by host cells in response to the presence of pathogens such as viruses, bacteria, parasites, or tumor cells. They belong to the large class of glycoproteins known as cytokines. Leukocyte interferon is produced predominantly by B lymphocytes. Immune interferon is produced by mitogen- or antigen-stimulated T lymphocytes. IFNA1 is produced by macrophages and has antiviral activities.IFNs stimulate the production of two enzymes: a protein kinase and an oligoadenylate synthetase. They allow for communication between cells to trigger the protective defenses of the immune system that eradicate pathogens or tumors. IFNs can activate immune cells, such as natural killer cells and macrophages; they increase recognition of infection or tumor cells by up-regulating antigen presentation to T lymphocytes, and they also increase the ability of uninfected host cells to resist new infection by the virus.   Product Properties Synonyms IFN-alpha 1a protein Accession P01562 GeneID 3439 Source E.coli-derived Human IFN-α1a protein,Cys24-Glu189. Molecular Weight Approximately 19.5 kDa. AA Sequence MCDLPETHSL DNRRTLMLLA QMSRISPSSC LMDRHDFGFP QEEFDGNQFQ KAPAISVLHE LIQQIFNLFT TKDSSAAWDE DLLDKFCTEL YQQLNDLEAC VMQEERVGET PLMNADSILA VKKYFRRITL YLTEKKYSPC AWEVVRAEIM RSLSLSTNLQ ERLRRKE 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 specific activity determined by an anti-viral assay is no less than 1.0 × 108 IU/mg. Endotoxin < 0.1 EU per 1μg of the protein by the LAL method. Formulation Lyophilized from a 0.2 µm filtered solution in PBS, pH 7.4, containing 3 % Mannitol, 5 % Trehalose, 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 °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!

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Interferons (IFN) are a family of cytokines with potent antiviral, antiproliferative and immunomodulatory properties, classified based on their binding specificity to cell surface receptors . Human IFNA2 was originally cloned in the early ‘80s and now more than a dozen closely related IFN alpha subtypes have been identified in both the human and mouse genome, each sharing about 80% amino acid (aa) sequence homology. Structurally, type I IFNs belong to the class of five helical- bundle cytokines, with the IFNA subtypes containing 2 conserved disulfide bonds. The extracellular domain (ECD) of mature human IFNA1, also known as IFNA13, shares 63% aa sequence identity with mouse IFNA1. Two variants of human IFNA1 are known to exist, IFNA1a and IFNA1b, which only differ by a single residue at position 137. The type I IFNs bind to the interferon alpha receptor (IFNAR), which consists of two subunits: IFNAR1 (alpha - subunit) and IFNAR2 (beta - subunit).   Product Properties Synonyms Human IFN-α1b Accession P01562 GeneID 3439 Source E.coli-derived Human IFN-α1b protein,Cys24-Glu189(A115).with an N-terminal Met. Molecular Weight Approximately 19.5 kDa. AA Sequence MCDLPETHSL DNRRTLMLLA QMSRISPSSC LMDRHDFGFP QEEFDGNQFQ KAPAISVLHE LIQQIFNLFT TKDSSAAWDE DLLDKFCTEL YQQLNDLEAC VMQEERVGET PLMNVDSILA VKKYFRRITL YLTEKKYSPC AWEVVRAEIM RSLSLSTNLQ ERLRRKE 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 specific activity determined by an anti-viral assay is no less than 1.0 × 108 IU/mg. Endotoxin < 0.1 EU per 1μg of the protein by the LAL method. Formulation Lyophilized from a 0.2 µm filtered solution in PBS, pH 7.4, containing 4% mannitol and 1 % HSA. 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!

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IFNA2 (Interferon Alpha 2) is a Protein Coding gene. This gene is a member of the alpha interferon gene cluster on chromosome 9. The encoded protein is a cytokine produced in response to viral infection. Type I Interferons (IFNs) are well-known cytokines that exert antiviral activity, antitumor activity, and immunomodulatory effects. Interferon tau (IFNT), a type I IFN similar to alpha IFNs(IFNA), is the pregnancy recognition signal produced by the ruminant conceptus. Among the IFN-α genes, a total of 28 different sequence variants have been described. The three principal subtypes of IFNα-2 are designated α-2a, α-2b, and α-2c. IFNα-2b is being the predominant allele while IFNα-2a is less predominant and IFNα-2c only a minor allelic variant.   Product Properties Synonyms IFN-alpha 2a protein Accession P01563 GeneID 3440 Source Yeast-derived Human IFN-α2a protein,Cys24-Glu188. Molecular Weight Approximately 19.2 kDa. AA Sequence CDLPQTHSLG SRRTLMLLAQ MRKISLFSCL KDRHDFGFPQ EEFGNQFQKA ETIPVLHEMI QQIFNLFSTK DSSAAWDETL LDKFYTELYQ QLNDLEACVI QGVGVTETPL MKEDSILAVR KYFQRITLYL KEKKYSPCAW EVVRAEIMRS FSLSTNLQES LRSKE 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 specific activity determined by an anti-viral assay is no less than 1.0 × 108 IU/mg. Endotoxin < 1 EU per 1μg of the protein by the LAL method. Formulation Lyophilized from a 0.2 µm filtered 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!

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Interferon-alpha (IFN-alpha), also known as leukocyte interferon, represents a group of related but distinct proteins that share over 95% amino acid sequence homology. They are members of the type I interferon family which share a common cell surface receptor composed of two subunits, a 100 kDa ligand-binding subunit (IFN-alpha R2) and a 125 kDa ligand binding and signal transduction subunit (IFN-alpha R1) that is involved both in ligand binding and signal transduction. IFN-alpha has both anti-viral and immunomodulatory activities on target cells.   Product Properties Synonyms IFN-α2c Source Yeast-derived Human IFN-α2c protein,Cys24-Glu188(K23R,H24R. Molecular Weight Approximately 19.3 kDa. AA Sequence CDLPQTHSLG SRRTLMLLAQ MRRISLFSCL KDRRDFGFPQ EEFGNQFQKA ETIPVLHEMI QQIFNLFSTK DSSAAWDETL LDKFYTELYQ QLNDLEACVI QGVGVTETPL MKEDSILAVR KYFQRITLYL KEKKYSPCAW EVVRAEIMRS FSLSTNLQES LRSKE 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 activity is determined by the cytopathic effect inhibition assay. Endotoxin < 0.1 EU per 1μg of the protein by the LAL method. Formulation Lyophilized from a 0.2 µm filtered solution in PBS, pH 7.4, 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 °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!

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IFN λ1, 2, and 3 (also known as IL-29, IL-28A and IL-28B respectively) are distantly related to the  IL-10  family  and  the interferons. All three IFN-lambdas use a distinct receptor system composed of an IFN-λR1 subunit (also called CRF2-12) and IL-10R2 subunit (also called CRF2-14). Signaling through this receptor system induces antiviral defenses similar to, but distinct from, that of type I interferons. Recombinant Human IFN-λ1 is a 19.8 kDa protein containing 178 amino acid residues.   Product Properties Synonyms Cytokine Zcyto21 Accession Q8IU54 GeneID 282618 Source E.coli-derived Human IFN-λ1 protein,Gly20-Thr200. Molecular Weight Approximately 19.8 kDa. AA Sequence GPVPTSKPTT TGKGCHIGRF KSLSPQELAS FKKARDALEE SLKLKNWSCS SPVFPGNWDL RLLQVRERPV ALEAELALTL KVLEAAAGPA LEDVLDQPLH TLHHILSQLQ ACIQPQPTAG PRPRGRLHHW LHRLQEAPKK ESAGCLEASV TFNLFRLLTR DLKYVADGNL CLRTSTHPES T 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 ED50 as determined by an anti-viral assay using human HepG2 cells infected with encephalomyocarditis is less than 5 ng/mL, corresponding to a specific activity of > 2.0 × 105 IU/mg. Endotoxin < 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!

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IL-1ra was originally isolated from the urine of patients with monocytic leukemia and has also been purified from adherent monocytes. The naturally occurring, fully glycosylated form has an apparent molecular weight of about 25,000 Daltons. The protein shows 26% amino acid homology to IL-1 beta and 19% homology to IL-1 alpha. It will compete with either factor for receptor binding, but does not interact with either one. Human IL-1ra will bind to both types of IL-1 receptor (I and II) on human cells, but reportedly will not block binding to the type II receptor on murine pre-B cell lines. The recombinant, non-glycosylated form of IL-1ra blocks binding of IL-1 to its receptor equally as well as the naturally-occurring, glycosylated form. The IL-1ra has been shown to block the inflammatory responses induced by IL-1 both in vitro and in vivo. Currently, pre-clinical and clinical studies are underway to test possible therapeutic applications for IL-1ra in the treatment of sepsis, rheumatoid arthritis and chronic myelogenous leukemia.   Product Properties   Synonyms IL-1RN, IRAP Source E.coli-derived Human IL-1RA, Arg26-Glu177. AA sequence RPSGRKSSKM QAFRIWDVNQ KTFYLRNNQL VAGYLQGPNV NLEEKIDVVP IEPHALFLGI HGGKMCLSCV KSGDETRLQL EAVNITDLSE NRKQDKRFAF IRSDSGPTTS FESAACPGWF LCTAMEADQP VSLTNMPDEG VMVTKFYFQE DE Endotoxin < 1.0 EU per μg by the LAL method. Purity > 96% by SDS-PAGE and HPLC analyses. Formulation Lyophilized from a 0.2 μm filtered concentrated solution in PBS, pH 7.4. Applications ELISA, Kinetics (BLI), Kinetics (SPR), Immunization Dilution Dilute with sterile distilled water or aqueous buffer containing 0.1% BSA.   Storage   The products are shipped with ice pack and can be stored at -20 ℃ for 1 year.  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.  

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Interleukin 11 (IL-11), a member of the IL-6 family of cytokines, exerts pleiotropic activities by stimulating hemopoiesis and thrombopoiesis, regulating macrophage differentiation, and conferring mucosal protection in the intestine. These effects are mediated by a multimeric complex comprising the ligand-binding IL-11R± and the ubiquitously expressed gp130R-subunit, which together, trigger intracellular signaling and engagement of Stat3. Mature human IL-11 shares 88%, 88%, and 96% aa sequence identity with mouse, rat and canine IL-11, respectively. IL-11 is a pleotropic cytokine produced by lung stromal cells in response to respiratory viruses, cytokines, and histamine. The functions of IL-11 are that it directly stimulates the proliferation of hematopoietic stem cells and megakaryocyte progenitor cells, and induces megakaryocyte maturation resulting in increased platelet production.   Product Properties   Synonyms Adipogenesis inhibitory factor, AGIF, IL-11, IL-11Oprelvekin, interleukin 11, interleukin-11, Oprelveki Source E.coli-derived human IL-11, Pro22-Leu199, with an N-terminal Met. AA sequence MPGPPPGPPR VSPDPRAELD STVLLTRSLL ADTRQLAAQL RDKFPADGDH NLDSLPTLAM SAGALGALQL PGVLTRLRAD LLSYLRHVQW LRRAGGSSLK TLEPELGTLQ ARLDRLLRRL QLLMSRLALP QPPPDPPAPP LAPPSSAWGG IRAAHAILGG LHLTLDWAVR GLLLLKTRL Endotoxin < 1.0 EU per μg by the LAL method. Purity > 95% by SDS-PAGE and HPLC analyses. Formulation Lyophilized from a 0.2 μm filtered concentrated solution in PBS, pH 7.4. Applications ELISA, Kinetics (BLI), Kinetics (SPR), Immunization Dilution Dilute with sterile distilled water or aqueous buffer containing 0.1% BSA.   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. Please operate with lab coats and disposable gloves,for your safety.        2. This product is for research use only.  

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The Interleukin 17B (IL-17) family proteins, comprising six members (IL-17, IL-17B through IL-17F), are secreted, structurally related proteins that share a conserved cystine-knot fold near the C-terminus, but have considerable sequence divergence at the N-terminus (1, 2). With the exception of IL-17B, which exists as a non- covalently linked dimer, all IL-17 family members are disulfide-linked dimers (3). IL-17 family proteins are pro-inflammatory cytokines that induce local cytokine production and are involved in the regulation of immune functions (1, 2). Two receptors (IL- 17 R, and IL-17B R), which are activated by IL-17 family members, have been identified. In addition, at least three additional orphan type I transmembrane receptors with homology to IL-17 R, including IL-17 RL (IL-17 RC), IL-17 RD, and IL- 17 RE, have also been reported (1- 4). Human IL-17B cDNA encodes a 180 aa protein with a putative 20 aa signal peptide (5, 6). Human and mouse IL-17B share 88% amino acid sequence identity. Among IL-17 family members, IL-17B is most closely related to IL-17D, sharing 27% aa sequence homology. IL-17B is expressed highly in spinal cord, and at lower levels in brain, kidney, lung, small intestine, prostate, testes, pancreas, adrenal gland and trachea (5- 7). Expression of IL-17B has also been detected in chondrocytes in articular cartilage (2). IL-17B binds the IL-17B receptor but not IL-17 R and exhibits bioactivities distinct from those of IL-17 (5, 6).   Product Properties   Synonyms IL-17B Source E.coli-derived human IL-17B protein, Gln21-Phe180, with an N-terminal Met. AA sequence MQPRSPKSKR KGQGRPGPLA PGPHQVPLDLVSRMKPYARM EEYERNIEEM VAQLRNSSEL AQRKCEVNLQ LWMSNKRSLS PWGYSINHDP SRIPVDLPEA RCLCLGCVNP FTMQEDRSMV SVPVFSQVPV RRRLCPPPPR TGPCRQRAVM ETIAVGCTCI F Endotoxin < 1.0 EU per μg by the LAL method. Purity > 95% by SDS-PAGE and HPLC analyses. Formulation Lyophilized from a 0.2 µm filtered concentrated solution in PBS, pH 7.4, with 0.1% Tween-20 and 3% Trehalose. Applications ELISA, Kinetics (BLI), Kinetics (SPR), Immunization Dilution Dilute in sterile distilled water or aqueous buffer containing 0.1% BSA.   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. Please operate with lab coats and disposable gloves,for your safety.        2. This product is for research use only.  

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The Interleukin 17F (IL-17) family proteins, comprising six members (IL-17, IL-17B through IL-17F), are secreted, structurally related proteins that share a conserved cystine-knot fold near the C-terminus, but have considerable sequence divergence at the N-terminus. With the exception of IL-17B, which exists as a non- covalently linked dimer, all IL-17 family members are disulfide-linked dimers. IL-17 family proteins are pro-inflammatory cytokines that induce local cytokine production and are involved in the regulation of immune functions. Two receptors (IL- 17 R, and IL-17B R), which are activated by IL-17 family members, have been identified. In addition, at least three additional orphan type I transmembrane receptors with homology to IL-17 R, including IL-17 RL (IL-17 RC), IL-17 RD, and IL- 17 RE, have also been reported. Human IL-17B cDNA encodes a 180 aa protein with a putative 20 aa signal peptide. Human and mouse IL-17B share 88% amino acid sequence identity. Among IL-17 family members, IL-17B is most closely related to IL-17D, sharing 27% aa sequence homology. IL-17B is expressed highly in spinal cord, and at lower levels in brain, kidney, lung, small intestine, prostate, testes, pancreas, adrenal gland and trachea . Expression of IL-17B has also been detected in chondrocytes in articular cartilage. IL-17B binds the IL-17B receptor but not IL-17 R and exhibits bioactivities distinct from those of IL-17.   Product Properties   Synonyms ML-1, IL-24 Source E.coli-derived human IL-17F protein, Arg31-Gln163, with an N-terminal Met. AA sequence MRKIPKVGHT FFQKPESCPP VPGGSMKLDI GIINENQRVS MSRNIESRST SPWNYTVTWD PNRYPSEVVQ AQCRNLGCIN AQGKEDISMN SVPIQQETLV VRRKHQGCSV SFQLEKVLVT VGCTCVTPVI HHVQ Endotoxin < 1.0 EU per μg by the LAL method. Purity > 95% by SDS-PAGE and HPLC analyses. Formulation Lyophilized from a 0.2 µm filtered concentrated solution in PBS, pH 7.4. Applications ELISA, Kinetics (BLI), Kinetics (SPR), Immunization Dilution Dilute in 6 mM HCl to a concentration of 0.1 mg/ml.   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. Please operate with lab coats and disposable gloves,for your safety.        2. This product is for research use only.  

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Interleukin-18 (IL-18), also known as IL-1F4, is a proinflammatory cytokine that belongs to the IL-1 superfamily and is produced by macrophages and other cells. It is expressed as a 24 kDa precursor by endothelial and epithelial cells, keratinocytes, gamma δ T cells, and phagocytes. Mature human IL-18 shares approximately 63% amino acid sequence identity with mouse and rat IL-18. IL-18 activation is induced by infection or tissue damage and leads to disease pathology in chronic inflammation. In the presence of IL-12 or IL-15, IL-18 enhances anti-viral Th1 immune responses by inducing IFN-gamma production and the cytolytic activity of CD8+ T cells and NK cells. IL-18 induces the antigen-independent production of IL-17 by gamma δ T cells and CD4+ T cells. IL-18 also promotes myeloid dendritic cell maturation and triggers neutrophil respiratory burst. In the absence of IL-12 or IL-15, IL-18 promotes production of the Th2 cytokines IL-4 and IL-13 by CD4+ T cells and basophils. IL-18 induces the antigen-independent production of IL-17 by gamma δ T cells and CD4+ T cells. IL-18 also promotes myeloid dendritic cell maturation and triggers neutrophil respiratory burst. In cancer, IL-18 has shown a variety of activities, including enhancing anti-tumor immunity, inhibiting or promoting angiogenesis, and promoting tumor cell metastasis.   Product Properties Synonyms IL-1F4 Accession Q14116 GeneID 3606 Source E.coli-derived Human IL-11, Tyr37-Asp193. Molecular Weight Approximately 18.2 kDa. AA Sequence YFGKLESKLS VIRNLNDQVL FIDQGNRPLF EDMTDSDCRD NAPRTIFIIS MYKDSQPRGM AVTISVKCEK ISTLSCENKI ISFKEMNPPD NIKDTKSDII FFQRSVPGHD NKMQFESSSY EGYFLACEKE RDLFKLILKK EDELGDRSIM FTVQNED Tag None Physical Appearance Sterile Filtered White lyophilized (freeze-dried) powder. Purity > 95% by SDS-PAGE analyses. Biological Activity Test in processing. Endotoxin Less than 0.1 EU/μg of rHuIL-18 as determined by LAL method. Formulation Lyophilized from a 0.2 μm filtered solution in PBS, pH 7.0. Reconstitution 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!

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IL-20 belongs to the IL-10 family. It is a cytokine structurally related to interleukin 10. Human IL-20 is synthesized as a 176 amino acid (aa) precursor with a 24 aa signal sequence and a 152 aa mature segment. IL-20 production has been found in skin, trachea, and other tissues. In particular, it is produced by activated keratinocytes and monocytes. It has been shown that IL-20 transduces its signal through signal transducer and activator of transcription 3 (STAT3) in keratinocytes. It may be involved in epidermal function and psoriasis. It also regulates the proliferation and differentiation of keratinocytes during inflammation, particularly inflammation associated with the skin. Also, it is reported to induce the proliferation of multipotential hematopoietic progenitor cells, direct the differentiation and expansion of keratinocytes, and promote the release of proinflammatory mediators in keratinocytes and other IL-20 receptor expressing cells.   Product Properties   Synonyms Cytokine Zcyto10 Source E.coli-derived Human IL-20, Leu25-Glu176, with an N-terminal Met. AA sequence MLKTLNLGSC VIATNLQEIR NGFSEIRGSV QAKDGNIDIR ILRRTESLQD TKPANRCCLL RHLLRLYLDR VFKNYQTPDH YTLRKISSLA NSFLTIKKDL RLCHAHMTCH CGEEAMKKYS QILSHFEKLE PQAAVVKALG ELDILLQWME ETE  Endotoxin < 1.0 EU per μg by the LAL method. Purity > 95% by SDS-PAGE and HPLC analyses. Formulation Lyophilized from a 0.2 μm filtered concentrated solution in PBS, pH 7.2, with trehalose. Applications ELISA, Kinetics (BLI), Kinetics (SPR), Immunization Dilution Dilute in sterile distilled water or aqueous buffer containing 0.1% BSA.   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. Please operate with lab coats and disposable gloves,for your safety.        2. This product is for research use only.  

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Human 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- 38 (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- 22 kDa, 158 amino acid (aa) intracellular and secreted protein that contains no signal sequence, no prosegment and no potential from N-linked glycosylation sites. It can be released in response to LPS and the cell ATP-induced activation of the P2X7 receptor. A 120 aa isoform missing aa 1- 38 has been reported. Human IL- 36 alpha (aa 6 - 158) shares 57- 68% aa sequence identity with mouse, 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 IL1RL2 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, and it is highly expressed in intubulointerstitial lesions in mouse models of chronic glomerulonephritis, lupus nephritis and diabetic nephritis. Product Properties   Synonyms FIL1 epsilon, IL-1 epsilon, IL-1F6, IL-1H1 Source E.coli-derived human Interleukin-36 alpha protein, Lys6-Phe158. AA sequence KIDTPQQGSI QDINHRVWVL QDQTLIAVPR KDRMSPVTIA LISCRHVETL EKDRGNPIYL GLNGLNLCLM CAKVGDQPTL QLKEKDIMDL YNQPEPVKSF LFYHSQSGRN STFESVAFPG WFIAVSSEGG CPLILTQELG KANTTDFGLT MLF Endotoxin < 1.0 EU per μg by the LAL method. Purity > 95% by SDS-PAGE and HPLC analyses. Formulation Lyophilized from a 0.2 μm filtered concentrated solution in 20 mM Tris, 300 mM NaCl, pH 8.0, 0.1% Tween 80. Applications ELISA, Kinetics (BLI), Kinetics (SPR), Immunization Dilution Dilute with sterile distilled water or aqueous buffer containing 0.1% BSA.   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. Please operate with lab coats and disposable gloves,for your safety.        2. This product is for research use only.  

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Human 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- 38 (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- 22 kDa, 158 amino acid (aa) intracellular and secreted protein that contains no signal sequence, no prosegment and no potential from N-linked glycosylation sites. It can be released in response to LPS and the cell ATP-induced activation of the P2X7 receptor. A 120 aa isoform missing aa 1- 38 has been reported. Human IL- 36 alpha (aa 6 - 158) shares 57- 68% aa sequence identity with mouse, 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 IL1RL2 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, and it is highly expressed in intubulointerstitial lesions in mouse models of chronic glomerulonephritis, lupus nephritis and diabetic nephritis. Product Properties   Synonyms FIL1 epsilon, IL-1 epsilon, IL-1F6, IL-1H1 Source E.coli-derived human IL-36 alpha protein, Met1-Phe158. AA sequence MEKALKIDTP QQGSIQDINH RVWVLQDQTL IAVPRKDRMS PVTIALISCR HVETLEKDRG NPIYLGLNGL NLCLMCAKVG DQPTLQLKEK DIMDLYNQPE PVKSFLFYHS QSGRNSTFES VAFPGWFIAV SSEGGCPLIL TQELGKANTT DFGLTMLF Endotoxin < 1.0 EU per μg by the LAL method. Purity > 95% by SDS-PAGE and HPLC analyses. Formulation Lyophilized from a 0.2 μm filtered concentrated solution in 2 × PBS, pH 7.4. Applications ELISA, Kinetics (BLI), Kinetics (SPR), Immunization Dilution Dilute with sterile distilled water or aqueous buffer containing 0.1% BSA.   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. Please operate with lab coats and disposable gloves,for your safety.        2. This product is for research use only.  

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Interleukin-36 Beta Human Recombinant Shipping: Synonyms Interleukin 36 beta, interleukin 1 family member 8, Interleukin-1 homolog 2, IL1F8 (Canonical product IL-1F8a), IL-1F8 (FIL1-eta), Interleukin-1 Superfamily, IL1H2, MGC126880, MGC126882. Introduction Human IL-36b belongs to the IL-1 family that includes IL-1b, IL-1a, IL-1ra, IL-18, IL-36ra (IL1F5), IL-36b (IL1F8), IL-36g (IL1F9), IL-37 (IL1F7) and IL-38 (IL-1F10). The IL-1 family members display a 12 b-strand, b-trefoil configuration, and are thought to have ascended from a mutual ancestral gene. IL-36 beta is known to be actively secreted. Cells expressing IL-36 beta include resting and activated monocytes and B cells. The receptor for IL-36 beta is a blend of IL-1 Rrp2 and IL-1 RAcP. Product Properties   Synonyms FIL1 eta, IL-1 eta, IL-1F8, IL-1H2 Source E.coli-derived human Interleukin-36 beta protein, Arg5-Glu157. AA sequence REAAPKSYAI RDSRQMVWVL SGNSLIAAPL SRSIKPVTLH LIACRDTEFS DKEKGNMVYL GIKGKDLCLF CAEIQGKPTL QLKEKNIMDL YVEKKAQKPF LFFHNKEGST SVFQSVSYPG WFIATSTTSG QPIFLTKERG ITNNTNFYLD SVE Endotoxin < 1.0 EU per μg by the LAL method. Purity > 97% by SDS-PAGE and HPLC analyses. Formulation Lyophilized from a 0.2 μm filtered concentrated solution in 2 × PBS, pH 7.4. Applications ELISA, Kinetics (BLI), Kinetics (SPR), Immunization Dilution Dilute with sterile distilled water or aqueous buffer containing 0.1% BSA.   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. Please operate with lab coats and disposable gloves,for your safety.        2. This product is for research use only.  

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Interleukin-36 Beta Human Recombinant Shipping: Synonyms Interleukin 36 beta, interleukin 1 family member 8 (eta), Interleukin-1 homolog 2, IL1F8 (Canonical product IL-1F8a), IL-1F8 (FIL1-eta), Interleukin-1 Superfamily e, IL1H2, MGC126880, MGC126882. Introduction Human IL-36b belongs to the IL-1 family that includes IL-1b, IL-1a, IL-1ra, IL-18, IL-36ra (IL1F5), IL-36b (IL1F8), IL-36g (IL1F9), IL-37 (IL1F7) and IL-38 (IL-1F10). The IL-1 family members display a 12 b-strand, b-trefoil configuration, and are thought to have ascended from a mutual ancestral gene. IL-36 beta is known to be actively secreted. Cells expressing IL-36 beta include resting and activated monocytes and B cells. The receptor for IL-36 beta is a blend of IL-1 Rrp2 and IL-1 RAcP. Recombinant IL-36 beta stimulates processes involving NF-kB and MAPK in an IL-1 Rrp2-dependent manner. Description IL36B Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 157 amino acids and having a molecular mass of 17.7kDa. Product Properties   Synonyms FIL1 eta, IL-1 eta, IL-1F8, IL-1H2 Source E.coli-derived human Interleukin-36 beta protein, Met1-Glu157, with an N-terminal Met. AA sequence MNPQREAAPK SYAIRDSRQM VWVLSGNSLI AAPLSRSIKP VTLHLIACRD TEFSDKEKGN MVYLGIKGKD LCLFCAEIQG KPTLQLKEKN IMDLYVEKKA QKPFLFFHNK EGSTSVFQSV SYPGWFIATS TTSGQPIFLT KERGITNNTN FYLDSVE Endotoxin < 1.0 EU per μg by the LAL method. Purity > 95% by SDS-PAGE and HPLC analyses. Formulation Lyophilized from a 0.2 μm filtered concentrated solution in PBS, pH 7.4. Applications ELISA, Kinetics (BLI), Kinetics (SPR), Immunization Dilution Dilute with sterile distilled water or aqueous buffer containing 0.1% BSA.   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. Please operate with lab coats and disposable gloves,for your safety.        2. This product is for research use only.  

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IL-36 gamma [previously called IL-1F9, IL-1 epsilon (epsilon), and IL-1H1] is a member of the IL-1 family which includes IL- 1 beta, IL- 1 alpha, IL- 1ra, IL- 18, IL- 36 Ra (IL- 1F5), IL-36 alpha (IL- 1F6), IL- 36 beta (IL- 1F8), 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 gamma is an 18- 22 kDa, 169 amino acid intracellular and secreted protein that contains no signal sequence, no prosegment and no potential N-linked glycosylation sites. Human IL- 36 gamma (aa 18- 169) shares 58%, 59%, 68% and 69% aa sequence identity with mouse, rat, bovine and equine IL- 36 gamma, respectively, and 23- 57% aa sequence identity with other family members. 134 aa isoform missing aa 19- 53 has been reported. Highest levels of IL- 36 gamma are produced by Langerhans cells, keratinocytes, and stomach Chief cells and parietal cells; these cells contribute to first-line defense against pathogens in the skin, lungs and  digestive tract. Its expression is induced by LPS treatment of monocytes, and by IL- alpha / beta, IL- 17 or TNF- alpha treatment of keratinocytes and bronchial epithelia. Skin IL-36 gamma expression is increased in contact hypersensitivity and psoriasis. It is elevated in inflammatory disorders of the lung (such as asthma) and viral infections. Lung IL- 36 gamma and other IL- 36 proteins contribute to neutrophil influx. The receptor for IL-36 gamma is a combination of IL- 1 Rrp2, 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 IL- 36 gamma induces production of inflammatory cytokines and chemokines such as CXCL8/IL- 8. Product Properties   Synonyms IL-1RP2, IL-1 epsilon, IL-1F9, IL-1H1 Source E.coli-derived human Interleukin-36 gamma protein, Ser18-Asp169. AA sequence SMCKPITGTI NDLNQQVWTL QGQNLVAVPR SDSVTPVTVA VITCKYPEAL EQGRGDPIYL GIQNPEMCLY CEKVGEQPTL QLKEQKIMDL YGQPEPVKPF LFYRAKTGRT STLESVAFPD WFIASSKRDQ PIILTSELGK SYNTAFELNI ND Endotoxin < 1.0 EU per μg by the LAL method. Purity > 95% by SDS-PAGE and HPLC analyses. Formulation Lyophilized from a 0.2 μm filtered concentrated solution in PBS, pH 7.4. Applications ELISA, Kinetics (BLI), Kinetics (SPR), Immunization Dilution Dilute with sterile distilled water or aqueous buffer containing 0.1% BSA.   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. Please operate with lab coats and disposable gloves,for your safety.        2. This product is for research use only.  

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IL-36 gamma [previously called IL-1F9, IL-1 epsilon (epsilon), and IL-1H1] is a member of the IL-1 family which includes IL- 1 beta, IL- 1 alpha, IL- 1ra, IL- 18, IL- 36 Ra (IL- 1F5), IL-36 alpha (IL- 1F6), IL- 36 beta (IL- 1F8), 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 gamma is an 18- 22 kDa, 169 amino acid intracellular and secreted protein that contains no signal sequence, no prosegment and no potential N-linked glycosylation sites. Human IL- 36 gamma (aa 18- 169) shares 58%, 59%, 68% and 69% aa sequence identity with mouse, rat, bovine and equine IL- 36 gamma, respectively, and 23- 57% aa sequence identity with other family members. 134 aa isoform missing aa 19- 53 has been reported. Highest levels of IL- 36 gamma are produced by Langerhans cells, keratinocytes, and stomach Chief cells and parietal cells; these cells contribute to first-line defense against pathogens in the skin, lungs and  digestive tract. Its expression is induced by LPS treatment of monocytes, and by IL- alpha / beta, IL- 17 or TNF- alpha treatment of keratinocytes and bronchial epithelia. Skin IL-36 gamma expression is increased in contact hypersensitivity and psoriasis. It is elevated in inflammatory disorders of the lung (such as asthma) and viral infections. Lung IL- 36 gamma and other IL- 36 proteins contribute to neutrophil influx. The receptor for IL-36 gamma is a combination of IL- 1 Rrp2, 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 IL- 36 gamma induces production of inflammatory cytokines and chemokines such as CXCL8/IL- 8. Product Properties   Synonyms IL-1RP2, IL-1 epsilon, IL-1F9, IL-1H1 Source E.coli-derived human Interleukin-36 gamma protein, Met1-Asp169, with an N-terminal Met. AA sequence MRGTPGDADG GGRAVYQSMC KPITGTINDL NQQVWTLQGQ NLVAVPRSDS VTPVTVAVIT CKYPEALEQG RGDPIYLGIQ NPEMCLYCEK VGEQPTLQLK EQKIMDLYGQ PEPVKPFLFY RAKTGRTSTL ESVAFPDWFI ASSKRDQPII LTSELGKSYN TAFELNIND Endotoxin < 1.0 EU per μg by the LAL method. Purity > 95% by SDS-PAGE and HPLC analyses. Formulation Lyophilized from a 0.2 μm filtered concentrated solution in PBS, pH 7.4. Applications ELISA, Kinetics (BLI), Kinetics (SPR), Immunization Dilution Dilute with sterile distilled water or aqueous buffer containing 0.1% BSA.   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. Please operate with lab coats and disposable gloves,for your safety.        2. This product is for research use only.  

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Human interleukin-36 receptor antagonist IL-36Ra; previously IL-1F5 and also named FIL-1δ (delta), IL- 1HY1, IL- 1H3, and IL-1L1 is a member of the IL- 1 family of proteins. IL- 1 family members include IL-1 beta, IL-1 alpha, IL-1ra, IL- 18 and IL-1F5-F10. All family members show a 12 beta -strand, beta -trefoil configuration, and all family members are believed to have arisen from a common ancestral gene that underwent multiple duplications . The human IL- 36Ra/IL- 1F5 gene is in closest proximity to the gene for IL-1ra and is likely a relatively recent duplication of the IL-1ra gene. IL-36Ra/IL-1F5 is synthesized as a 155 amino acid (aa) protein that contains no signal sequence, no prosegment and no potential N-linked glycosylation site(s). Nevertheless, it appears to be secreted as a 17 kDa monomer. There is an alternate start site that potentially gives rise to an alternate splice form. The translated product, however, has a premature stop codon, resulting in a truncated 16 aa peptide. Human to mouse, full length IL-1F5 has 90% aa identity. Within the family, IL-36Ra/IL-1F5 is 50% aa identical to IL-1ra, and 32%, 31%, 35%, 37%, 32% and 42% aa identical to IL-1 beta, IL-36 alpha /IL- 1F6, IL- 37/IL- 1F7, IL- 36 beta /IL- 1F8, IL- 36 gamma /IL- 1F9 and IL- 1F10, respectively. Cells reported to expressIL- 36Ra/IL- 1F5 include monocytes, B cells, dendritic cells/Langerhans cells, keratinocytes, and gastric fundus Parietal and Chief cells. The receptor for IL-36Ra/IL-1F5 has not been positively identified. Indirect evidence suggests it is IL-1 Rrp2 and/or IL-1 RAcP. In either case, activity association with receptor binding is also unclear. It was initially reported to be an antagonist of IL- 36 gamma /IL- 1F9 activity. This would be consistent with its hypothesized relationship to IL- 1ra. Studies, however, find IL-36Ra/IL-1F5 antagonist activity difficult to demonstrate. Product Properties   Synonyms IL-1RP3, IL-1HY1, IL-1 delta, IL-1F5, IL-1ra homolog 1, IL-1L1 Source E.coli-derived human Interleukin-36 Receptor Antagonist protein, Val2-Asp155. AA sequence VLSGALCFRM KDSALKVLYL HNNQLLAGGL HAGKVIKGEE ISVVPNRWLD ASLSPVILGV QGGSQCLSCG VGQEPTLTLE PVNIMELYLG AKESKSFTFY RRDMGLTSSF ESAAYPGWFL CTVPEADQPV RLTQLPENGG WNAPITDFYF QQCD Endotoxin < 1.0 EU per μg by the LAL method. Purity > 95% by SDS-PAGE and HPLC analyses. Formulation Lyophilized from a 0.2 μm filtered concentrated solution in PBS, pH 7.4. Applications ELISA, Kinetics (BLI), Kinetics (SPR), Immunization Dilution Dilute with sterile distilled water or aqueous buffer containing 0.1% BSA.   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. Please operate with lab coats and disposable gloves,for your safety.        2. This product is for research use only.  

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Interleukin-5 (IL-5) is a secreted glycoprotein that belongs to the alpha -helical group of cytokines. Unlike other family members, it is present as a covalently linked antiparallel dimer. The cDNA for human IL-5 encodes a signal peptide and a 115 amino acid (aa) mature protein. Mature human IL-5 shares 70%, 70%, 62%, 71%, 70% and 66%, aa sequence identity with mouse, rat, canine, equine, feline and porcine IL-5, respectively and shows cross-reactivity with mouse IL-5. IL-5 is primarily produced by CD4+ Th2 cells, but also by activated eosinophils, mast cells, EBV-transformed B cells, Reed-Sternberg cells in Hodgkin’s disease, and IL- 2-stimulated invariant natural killer T cells (iNKT). IL-5 increases production and mobilization of eosinophils and CD34+ progenitors from the bone marrow and causes maturation of eosinophil precursors outside the bone marrow. The receptor for human IL-5, mainly expressed by eosinophils, but also found on basophils and mast cells, consists of a unique ligand-binding subunit (IL-5 R alpha ) and a shared signal-transducing subunit, beta. IL-5 R alpha first binds IL-5 at low affinity, then associates with preformed beta c dimers, forming a high-affinity receptor.   Product Properties   Synonyms B-cell differentiation factor I, Eosinophil differentiation factor, TRF Source E.coli-derived human IL-5 protein, Ile20-Ser134,with an N-terminal Met. AA sequence MIPTEIPTSA LVKETLALLS THRTLLIANE TLRIPVPVHK NHQLCTEEIF QGIGTLESQT VQGGTVERLF KNLSLIKKYI DGQKKKCGEE RRRVNQFLDY LQEFLGVMNT EWIIES Endotoxin < 1.0 EU per μg by the LAL method. Purity > 98% by SDS-PAGE and HPLC analyses. Formulation Lyophilized from a 0.2 µm filtered concentrated solution in 20mM PB, pH 7.5, 3% trehalose, 0.1% Tween-80. Applications ELISA, Kinetics (BLI), Kinetics (SPR), Immunization Dilution Dilute with sterile distilled water or aqueous buffer containing 0.1% BSA.   Storage   The products are shipped with ice pack and can be stored at -20℃ to -80℃. 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.  

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Interleukin-8 (IL-8), also known as CXCL8, GCP-1, and NAP-1, is a widely expressed proinflammatory member of the CXC family of chemokines. This chemokine is secreted by a variety of cell types including monocyte/macrophages, T cells, neutrophils, fibroblasts, endothelial cells, and various tumor cell lines in response to inflammatory stimuli (IL1, TNF, LPS, etc). IL-8/CXCL8 can associate into a homodimer or a heterodimer with CXCL4/PF4 (2), and it can interact with matrix and cell surface glycosaminoglycans. Near its N-terminus, this 8-9 kDa chemokine contains an ELR motif which is important for its angiogenic properties. Numerous observations have established IL-8/CXCL8 as a key mediator in neutrophil-mediated acute inflammation due to its potent actions on neutrophils. In addition, IL-8/CXCL8 has crucial roles in various pathological conditions such as chronic inflammation and cancer. It induces VEGF expression, vascular endothelial cell proliferation, angiogenesis, and tumor cell invasiveness.   Product Properties Synonyms (Ser-IL-8)72, GCP/IL-8 protein I, IL8/NAP1 form III, LYNAP, MDNCF-c, NA Accession P10145 GeneID 3576 Source E.coli-derived Human IL-8,72aa/CXCL8, Ser28-Ser99 AA Sequence SAKELRCQCI KTYSKPFHPK FIKELRVIES GPHCANTEII VKLSDGRELC LDPKENWVQR VVEKFLKRAE NS Tag  None Physical Appearance Sterile Filtered White lyophilized (freeze-dried) powder. Purity > 97% by SDS-PAGE and HPLC analyses. Biological Activity less than 2 ng/mL, corresponding to a specific activity of > 5.0 × 10 5 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.

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Interleukin-8 (IL-8) is encoded by the IL8 gene and produced by macrophages and other cell types such as epithelial cells. It is also synthesized by endothelial cells, which store IL-8 in their storage vesicles. There are many receptors capable to bind IL-8, the most affinity to IL-8 are receptors CXCR1, and CXCR2. As a member of the CXC chemokine family, function of IL-8 is the induction of chemotaxis in its target cells, like neutrophil granulocytes, basophils, and T-cells. IL-8 (77a.a.) has a 5-10 fold higher activity on neutrophil activation, compared to IL-8 (77a.a.). IL-8 is often associated with inflammation, it has been cited as a proinflammatory mediator in gingivitis and psoriasis.   Product Properties Synonyms CXCL 8, Emoctakin, GCP-1, MDNCF, MONAP, NAP-1, Protein 3-10C, T-cell chemotactic factor Accession P10145 GeneID 3576 Source E.coli-derived human IL-8 protein, Ala23-Ser99 Molecular Weight Approximately 8.9 kDa. AA Sequence AVLPRSAKEL RCQCIKTYSK PFHPKFIKEL RVIESGPHCA NTEIIVKLSD GRELCLDPKE NWVQRVVEKF LKRAEN 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 chemotaxis bioassay using human CXCR2 transfected mouse BaF3 cells is less than 2 ng/ml, corresponding to a specific activity of > 5.0 × 10^5 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 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.

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Interleukin 9, also known as IL-9, is a cytokine (cell signaling molecule) belonging to the group of interleukins. IL-9 is a cytokine that acts as a regulator of a variety of hematopoietic cells. This cytokine stimulates cell proliferation and prevents apoptosis. It functions through the interleukin 9 receptor (IL-9R), which activates different signal transducer and activator (STAT) proteins and thus connects this cytokine to various biological processes. Genetic studies on a mouse model of asthma demonstrated that this cytokine is a determining factor in the pathogenesis of bronchial hyperresponsiveness.   Product Properties   Synonyms Cytokine P40, T-cell Growth Factor P40 Source E.coli-derived human IL-1alpha protein, Gln19-Ile144. AA sequence QGCPTLAGIL DINFLINKMQ EDPASKCHCS ANVTSCLCLG IPSDNCTRPC FSERLSQMTN TTMQTRYPLI FSRVKKSVEV LKNNKCPYFS CEQPCNQTTA GNALTFLKSL LEIFQKEKMR GMRGKI Endotoxin < 1.0 EU per μg by the LAL method. Purity > 95% by SDS-PAGE and HPLC analyses. Formulation Lyophilized from a 0.2 μm filtered concentrated solution in PBS, pH 7.4. Applications ELISA, Kinetics (BLI), Kinetics (SPR), Immunization Dilution Dilute with sterile distilled water or aqueous buffer containing 0.1% BSA.   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. Please operate with lab coats and disposable gloves,for your safety.        2. This product is for research use only.  

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Fibroblast growth factor 7 (FGF-7), also known as Keratinocyte Growth Factor (KGF), is a member of the fibroblast growth factor (FGF) family. It plays an important role in the regulation of embryonic development, cell proliferation, and cell differentiation. It is essential for normal branching morphogenesis and is an active growth factor for keratinocytes. It may be the main paracrine factor for the proliferation of normal epithelial cells. The activity of recombinant KGF overexpressed in E. coli is about 10 times that of the natural protein, which may be related to the lack of glycosylation of recombinant KGF. The 122-132AA segment of KGF is the specific binding site for the KGF receptor. KGF is secreted by various sources of mesenchymal cells and has a strong affinity for heparin. Its receptor, KGFR, belongs to the family of protein tyrosine kinase receptors and is mainly distributed in epithelial cells. After KGF specifically binds to the receptor KGFR on the target cell membrane, it promotes the autophosphorylation of the receptor, thereby initiating a series of intracellular signaling cascades and playing various biological functions: participating in the development of tissues and organs, promoting cell proliferation, and tissue damage repair. This product is a recombinant protein prepared by the E. coli prokaryotic expression system, and is made through steps such as separation and purification, filtration sterilization, and freeze-drying. It has the characteristics of high purity, high activity, tag-free, and low endotoxin. Product Properties Synonyms FGF7, FGF-7, HBGF7, HBGF-7, Heparin-binding growth factor 7, keratinocyte growth factor, KGF Expression System and Expression Range Human FGF-7 is expressed from E.coli with no tag . It contains Cys32-Thr194. Accession P21781 Molecular Weight Approximately 18.9 kDa Biological Activity Fully biologically active when compared to standard. The ED50 as determined by thymidine uptake assay using FGF-receptors transfected BaF3 cells is less than 10 ng/ml, corresponding to a specific activity of > 1.0 × 10 5 IU/mg. Appearance Sterile-filtered white lyophilized powder. Purity Greater than 96%, detected by SDS-PAGE and HPLC. Endotoxin <1.0 EU/μ Formulation Lyophilized from a 0.2 μm filtered concentrated solution in 20 mM PB, 0.5 M NaCl, pH 8.0 Reconstitution Before opening, it is recommended to briefly centrifuge to bring the contents to the bottom. Reconstitute in sterile distilled water or an aqueous buffer solution containing 0.1% BSA to a concentration of 0.1-1.0 mg/mL. The stock solution should be divided into aliquots and stored at ≤-20°C.   Shipping and Storage Store at -25 to -15°C, with a shelf life of 1 year after receipt of goods. After reconstitution, store at 2 to 8°C for a shelf life of 30 days. After reconstitution, store at -25 to -15°C for a shelf life of 3 months. It is recommended to aliquot the protein at the first use to avoid repeated freeze-thaw cycles.   Cautions 1. This product is for research use only.2. For your safety and health, please wear a lab coat and use disposable gloves when handling.

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Laminin 521 is a defined matrix for feeder-free culture of human embryonic (hES) and induced pluripotent (hiPS) stem cells. When used in combination with defined maintenance media, Laminin 521 reliably facilitates self-renewal of human hES and hiPS cells without spontaneous differentiation.   Product Properties Synonyms   LN521，LAMB2,LN-11   Source Mammalian cells Purity > 95% Endotoxin <1 EU/ ml TSE/BSE Animal-Free Mycoplasma Negative Concentration 0.1 mg/ml Formulation Clear colorless, buffered solution with a pH of 7.4 with PBS. Form Liquid   Shipping and Storage This product should be stored at -85~-65℃ for 2 years from date of receipt. 3 months at 2-8°C after thaw. Cautions 1. This product is for research use only.  2. Please operate with lab coats and disposable gloves，for your safety.

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  Name Catalog No. Size Recombinant Human LGR6 Protein-VLP C230751E 20 μg C230751S 100 μg C230751M 100 μg C230751L 1 mg   Product Properties   Synonyms Leucine-rich repeat-containing G-protein coupled receptor 6; Source HEK293 Cells AA sequence Accession #Q9HBX8: Met1 - Val967 Endotoxin < 1EU per μg by the LAL method. Purity > 85% as determined by DLS. Formulation 115mM Gly 4% trehalose Applications ELISA, Kinetics (BLI), Kinetics (SPR), Immunization Dilution Dilute with PBS.   Storage   The product should be stored at -85~-65℃ for 1 year from date of receipt. 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.        This product is for research use only.    

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Leukemia Inhibitory Factor (LIF) is a pleiotropic cytokine produced by a variety of cell types, including T cells, bone marrow mononuclear lineage, fibroblasts, liver, heart, and melanoma. LIF promotes the long-term maintenance of embryonic stem cells by inhibiting spontaneous differentiation. Other activities include stimulating the acute-phase protein synthesis in hepatocytes, stimulating the differentiation of cholinergic neurons, and inhibiting lipogenesis in adipocytes by inhibiting lipoprotein lipase. Although human LIF is active on mouse cells and is widely used to maintain mouse ESCs to prevent spontaneous differentiation, mouse LIF is not active on human cells because it cannot bind to the human LIF receptor. This recombinant human LIF is provided in the form of a lyophilized powder, with high activity, high purity, low endotoxin, and without any additional tags. Product Properties Synonyms CDF, DIA, Differentiation-stimulating Factor, D Factor, Emfilermin, HILDA, Melanoma-derived LPL Inhibitor, MLPLI Source E.coli-derived human LIF, Ser23-Phe202. Accession P15018 Tag None Molecular Weight Approximately 19.7 kDa. AA Sequence SPLPITPVNA TCAIRHPCHN NLMNQIRSQL AQLNGSANAL FILYYTAQGE PFPNNLDKLC GPNVTDFPPF HANGTEKAKL VELYRIVVYL GTSLGNITRD QKILNPSALS LHSKLNATAD ILRGLLSNVL CRLCSKYHVG HVDVTYGPDT SGKDVFQKKK LGCQLLGKYK QIIAVLAQAF Endotoxin < 1.0 EU/μg by the LAL method. Purity ＞ 98%, as determined by SDS-PAGE and HPLC analysis. Biological Activity The ED50 as determined by the dose-dependent proliferation of human TF-1 cells is less than 0.1 ng/mL, corresponding to a specific activity of > 1.0 × 10 ^7  IU/mg. Fully biologically active when compared to standard. Formulation Lyophilized from a 0.2 μm filtered concentrated solution in PBS, pH 7.4. Physical Appearance White lyophilized powder   Shipping and Storage Store at -25 to -15°C, with a shelf life of 1 year from the date of receipt of goods.After reconstitution, store at 2 to 8°C, with a shelf life of 7 days.After reconstitution, store at -85 to -65°C, with a shelf life of 3 months.   Reconstitution Method Before opening, centrifuge briefly to bring the contents to the bottom. Reconstitute with sterile deionized water to a concentration of 0.1-1.0 mg/mL, which can be further diluted according to subsequent experimental needs; for long-term storage, it is recommended to include a carrier protein (0.1% BSA) in the dilution buffer; aliquot for a single experimental use and store at -80°C to avoid repeated freeze-thaw cycles. Cautions 1. For your safety and health, please wear a lab coat and use disposable gloves when handling.2. This product is for research purposes only.

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Members of Lipocalin family share a highly conserved fold with an eight-stranded antiparallel beta barrel, and act as a transporters, carrying small molecules to specific cells. Lipocalin-2, also known as Neutrophil Gelatinase-Associated Lipocalin (NGAL), was originally identified as a component of neutrophil granules. It is a 25 kDa protein existing in monomeric and homo- and heterodimeric forms, the latter as a dimer with human neutrophil gelatinases (MMP-9). Its expression has been observed in most tissues normally exposed to microorganism, and its synthesis is induced in epithelial cells during inflammation. Lipocalin-2 has been implicated in a variety of processes including cell differentiation, tumorigenesis, and apoptosis. Studies indicate that Lipocalin-2 binds a bacterial catecholate sidropore bound to ferric ion such as enterobactin with a subnanomolar dissociation constant (Kd = 0.41 nM). The bound ferric enterobactin complex breaks down slowly in a month into dihydroxybenzoyl serine and dihydroxybenzoic acid (DHBA). It also binds to a ferric DHBA complex with much less Kd values. Secretion of Lipocalin- 2 in immune cells increases by stimulation of Toll-like receptor as an acute phase response to infection. As a result, it acts as a potent bacteriostatic reagent by sequestering iron. Moreover, Lipocalin-2 can alter the invasive and metastatic behavior of Ras-transformed breast cancer cells in vitro and in vivo by reversing epithelial to mesenchymal transition inducing activity of Ras, through restoration of E-cadherin expression, via effects on the Ras-MAPK signaling pathway. Product Properties Synonyms NGAL, p25 Accession P80188 GeneID 3934 Source E.coli-derived Human LCN2, Gln21-Gly198. Molecular Weight Approximately 41.0 kDa. AA Sequence QDSTSDLIPA PPLSKVPLQQ NFQDNQFQGK WYVVGLAGNA ILREDKDPQK MYATIYELKE DKSYNVTSVL FRKKKCDYWI RTFVPGCQPG EFTLGNIKSY PGLTSYLVRV VSTNYNQHAM VFFKKVSQNR EYFKITLYGR TKELTSELKE NFIRFSKSLG LPENHIVFPV PIDQCIDG 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 < 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!

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Human CCL16, also called Liver-expressed chemokine (LEC), Monotactin-1 (MTN-1), IL-10-inducible chemokine and so on, is expressed by the CCL16 gene located on the chromosome 17 in humans. The gene encodes a 120 a.a. residue precursor protein with a 23 a.a. residue predicted signal peptide that is cleaved to generate a 97 a.a. residue mature protein. The protein is secreted by the liver, thymus, spleen cells and showing chemotactic activity for lymphocytes and monocytes but it is distantly related to other CC chemokines, exhibiting less than 30 % sequence identity. CCL16 is highly induced by IL-10, IFN- γ and bacterial lipopolysaccharide in monmcytes and signal through CCR1, CCR2, CCR5, and CCR8. Product Properties Synonyms C-C motif chemokine 16, HCC-4, IL-10-inducible chemokine, LCC-1 Accession O15467 GeneID 6360 Source E.coli-derived human Liver-Expressed Chemokine Protein, Gln24-Gln2 Molecular Weight Approximately 11.2 kDa. AA Sequence QPKVPEWVNT PSTCCLKYYE KVLPRRLVVG YRKALNCHLP AIIFVTKRNR EVCTNPNDDW VQEYIKDPNL PLLPTRNLST VKIITAKNGQ PQLLNSQ 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 biological activity determined by a chemotaxis bioassay using human monocytes is in a concentration range 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 20 mM PB, pH 7.4, 150 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°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.

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  Name Catalog No. Size Recombinant Human LSHR Protein-VLP C230756E 20 μg C230756S 100 μg C230756M 100 μg C230756L 1 mg   Product Properties   Synonyms LSHR / LHCGR / LCGR / LGR2 / LHRHR Source HEK293 Cells AA sequence Accession #P22888:Met1 - Cys699 Endotoxin < 1EU per μg by the LAL method. Purity > 85% as determined by DLS. Formulation 115mM Gly 4% trehalose Applications ELISA, Kinetics (BLI), Kinetics (SPR), Immunization Dilution Dilute with PBS.   Storage   The product should be stored at -85~-65℃ for 1 year from date of receipt. 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.  

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LAG-1 is CC chemokine that signals through the CCR5 receptor. LAG-1 is identical to MIP-1β (ACT II isotype) except for two amino acid substitutions; arginine for histidine at position 22 and serine for glycine at position 47 of the mature protein. LAG-1 chemoattracts monocytes, and exhibits activity as an HIV-suppressive factor. Product Properties Synonyms CCL4L1 Accession Q8NHW4 GeneID 388372 Source E.coli-derived Human CCL4L1protein,Ala24-Asn92. Molecular Weight Approximately 7.8 kDa. AA Sequence APMGSDPPTA CCFSYTARKL PRNFVVDYYE TSSLCSQPAV VFQTKRGKQV CADPSESWVQ EYVYDLELN 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 ED50 as determined by a cell proliferation assay using human CCR5 transfected murine BaF3 cells is less than 2.0 ng/ml, corresponding to a specific activity of > 5.0 × 10 5 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 PSB. 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.

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Human lymphotactin (Lptn)/XCL1 (also named human SCM-1 alpha and ATAC) and its mouse homologue belong to the C or gamma subfamily of chemokines. The C chemokines lack two (the 1st and 3rd ) of the four invariant cysteine residues normally found in the CC and CXC chemokines and have an extended carboxy terminus. Human lymphotactin encodes a 114 amino acid residue precursor protein with a 21 amino acid residue predicted signal peptide. The expression of lymphotactin is abundant in some activated T cells such as activated CD8+ T cells and other class I MHC restricted T cells. Lptn expression is absent in CD4+ T cells. Human and mouse Lptn share approximately 60% amino acid sequence homology. The gene for lymphotactin has been mapped to chromosome 1 in both human and mouse. Recombinant human lymphotactin has been shown to have chemotactic activity for lymphocytes and NK cells. The orphan receptor GPR5 has been reported to be the specific receptor for Lptn. Product Properties Synonyms ATAC, C motif chemokine 1, Cytokine SCM-1, Lymphotaxin, SCM-1-alpha, Small-inducible cytokine C1, XC chemokine ligand 1 Accession P47992 GeneID 6375 Source E.coli-derived Human Lymphotactin/XCL1, Gly23-Gly114. Molecular Weight Approximately 10.2 kDa. AA Sequence GSEVSDKRTC VSLTTQRLPV SRIKTYTITE GSLRAVIFIT KRGLKVCADP QATWVRDVVR SMDRKSNTRN NMIQTKPTGT QQSTNTAVTL TG 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 T-lymphocytes is in a concentration 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 20 mM PB, pH 7.4, 150 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°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.

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Macrophage colony stimulating factor 1, also known as CSF-1 and M-CSF, is a one-way membrane protein that forms homodimers or heterodimers via disulfide bonds. M-CSF is a major regulator of macrophage survival, proliferation and differentiation. M-CSF can promote monocyte survival, monocyte transformation to macrophage and macrophage proliferation. Product Properties Synonyms CSF-1,Lanimostim Source Recombinant Human M-CSF Protein is expressed from HEK293 Cells with His tag at the C-terminal. It contains Glu33-Arg255. Molecular Weight Approximately 27.08 kDa. Tag None Physical Appearance Sterile Filtered White lyophilized (freeze-dried) powder. Purity > 95 % by SDS-PAGE and HPLC analyses. Endotoxin < 0.01 EU per 1μg of the protein by the LAL method. Formulation Lyophilized from a 0.22 μm filtered concentrated 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. 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.

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CCL23 is a member of CC chemokine family and is encoded by CCL23 gene located on Chr.17 in humans, where near several other CC chemokines. Highly expressed in adult lung, liver, skeletal muscle and pancreas, this protein shows strong chemotactic activity for monocytes, resting T-lymphocytes, and neutrophils, but not for activated lymphocytes. It elicits the effects by binding to CCR1. CCL23 is reported that it can be cleaved into four forms: CCL23 (19-99), CCL23 (22-99), CCL23 (27-99), CCL23 (30-99). Product Properties Synonyms CK-BETA-8; Ckb-8; Ckb-8-1; hmrp-2a; MIP-3; MIP3 ; MPIF-1; MPIF1; SCYA23 Accession P55773 GeneID 6368 Source E.coli-derived Human Macrophage Inflammatory Protein-3, Arg22-Asn120 Molecular Weight Approximately 11.4 kDa. AA Sequence RVTKDAETEF MMSKLPLENP VLLDRFHATS ADCCISYTPR SIPCSLLESY FETNSECSKP GVIFLTKKGR RFCANPSDKQ VQVCMRMLKL DTRIKTRKN 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 biological activity determined by a chemotaxis bioassay using human T-lymphocytes is in a concentration of 10-50 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 20 mM PBS, pH 7.4, 150 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°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.

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Human CCL15 is belonging to the CC chemokine family and shares 35 % amino acid homology with human HCC1 (CCL14). CCL15 is most abundant in heart, skeletal muscle and adrenal gland, and low expressed in liver, small intestine, colon, and in certain leukocytes and macrophages of the lung. It is chemotactic for neutrophils, monocytes, and lymphocytes and elicits its effects by binding to cell surface chemokine receptors like CCR1 and CCR3. CCL15 has several cleaved chains. All of them are more potent chemoattractants than CCL15. Product Properties Synonyms HCC-2;HMRP-2B; LKN-1; LKN1; MIP-1 delta; MIP-1D; MIP-5; MRP-2Bn; NCC-3; NCC3; Accession Q16663 GeneID 6359 Source E.coli-derived Human Macrophage Inflammatory Protein-5, Ser46-Ile113 Molecular Weight Approximately 7.4 kDa. AA Sequence SFHFAADCCT SYISQSIPCS LMKSYFETSS ECSKPGVIFL TKKGRQVCAK PSGPGVQDCM  KKLKPYSI 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 T-lymphocytes is in a concentration of 1.0-10 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 1×PBS, pH 7.2. 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.

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Migration Inhibitory Factor (MIF) is a secreted protein without a cleavable signal sequence and is secreted via a specialized, non-classical pathway. It is secreted by macrophages upon stimulation by bacterial lipopolysaccharide (LPS), or by M.tuberculosis antigens. MIF consists of two α-helices and six β-strands, four of which form a β-sheet. The two remaining β-strands interact with other MIF molecules, creating a trimer. Structure-function studies suggest MIF is bifunctional with segregated topology. The N- and C-termini mediate enzyme activity (in theory). Phenylpyruvate tautomerase activity (enol-to-keto) has been demonstrated and is dependent upon Pro at position 1. Amino acids 50-65(a.a.) have also been suggested to contain thiol-protein oxidoreductase activity. MIF has proinflammatory cytokine activity centered around (a.a.) 49 - 65. On fibroblasts, MIF induces, IL-1, IL-8 and MMP expression; on macrophages, MIF stimulates NO production and TNF-α release folllowing IFN-γ activation. MIF apparently acts through CD74 and CD44, likely in some form of trimeric interaction. Human MIF is active on mouse cells. Human MIF is 90 %, 94 %, 95 %, and 90 % aa identical to mouse, bovine, porcine and rat MIF, respectively. Product Properties Synonyms GIF Protein, Human; GLIF Protein, Human; MMIF Protein, Human Accession P14174 GeneID 4282 Source E.coli-derived Human Macrophage Migration Inhibitory Factor protein, Met-Ala115 Molecular Weight Approximately 12.5 kDa. AA Sequence MPMFIVNTNVPRASVPDGFLSELTQQLAQATGKPPQYIAVHVVPDQLMAFGGSSEPCALCSLHSI GKIGGAQNRSYSKLLCGLLAERLRISPDRVYINYYDMNAANVGWNNSTFA 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 specific activity is determined by binding rhCD74 in a functional ELISA. 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.

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CCL22 is a protein that in humans is encoded by the CCL22 gene, which locates on the Chr. 16. The protein is highly expressed in macrophage, monocyte-derived dendritic cell and thymus, additionally, also detected in the tissues of thymus, lymph node and appendix. CCL22 can bind to CCR4, and is a chemoattractant for monocytes, monocyte-derived dendritic cells, and natural killer cells, but not for neutrophils, eosinophils, and resting T-lymphocytes. After secreted from monocyte-derived dendritic cells, the protein can be proteolytic cleaved into three forms: MDC (3-69), MDC (5-69), MDC (7-69). Product Properties Synonyms A-152E5.1n ABCD-1; DC/B-CK; MDC ; SCYA22 ; STCP-1 Accession O00626 GeneID 6367 Source E.coli-derived human Macrophage-Derived Chemokine Protein, Gly25-Gln93 Molecular Weight Approximately 8.1 kDa. AA Sequence GPYGANMEDS VCCRDYVRYR LPLRVVKHFY WTSDSCPRPG VVLLTFRDKE ICADPRVPWV KMILNKLSQ Tag None Physical Appearance Sterile Filtered White lyophilized (freeze-dried) powder. Purity > 97 % by SDS-PAGE and HPLC analyses. Endotoxin < 1.0 EU per 1μg of the protein by the LAL method. Formulation Lyophilized from a 0.22 μm filtered concentrated solution in 20 mM PB, pH7.4, 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 °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.

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Melanoma Inhibitor Activity Protein 2 (MIA-2) encoded by MIA2 gene in humans, is a secreted cytokine that is highly expressed in liver and weakly in testis. The patients with severe fibrosis or inflammation and chronic hepatitis have higher level of MIA2 than other. Levels of MIA2 may severe as a clinically utility marker for diagnosis of hepatic disease activity and severity. The MIA2 is a member of the MIA/OTOR family, which also includes MIA, OTOR, and TANGO, and they share a Src homology-3 (SH3)-like domain. Product Properties Synonyms Melanoma inhibitory activity protein 2, MIA2 Accession Q96PC5 GeneID 117153 Source E.coli-derived HumanMIA-2 protein, Leu20-Leu119. Molecular Weight Approximately 11.4 kDa. AA Sequence LESTKLLADL KKCGDLECEA LINRVSAMRD YRGPDCRYLN FTKGEEISVY VKLAGEREDL WAGSKGKEFG YFPRDAVQIE EVFISEEIQM STKESDFLCL Tag None Physical Appearance Sterile Filtered White lyophilized (freeze-dried) powder. Purity > 97 % by SDS-PAGE and HPLC analyses. Biological Activity Testing in progress. 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, pH 7.4, 150 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°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.

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Melanoma Inhibiting Activity (MIA), also known as cartilage-derived retinoic acid-sensitive protein (CD-RAP), is an approximately 11-15 kDa protein that is secreted as a noncovalent homodimer and is structurally related to OTOR/Otoraplin and MIA-2. Mature human MIA contains a SH3 domain and shares 90% and 92% amino acid sequence identity with mouse and rat MIA, respectively. Alternative splicing generates a short isoform that lacks the SH3 domain. MIA is widely expressed in developing and regenerating cartilage and in the endothelium and parenchyma of developing lungs. MIA disrupts cellular interactions with the extracellular matrix by binding to Integrins alpha 4 beta 1 and alpha 5 beta 1. It competes with Fibronectin fragments for Integrin binding and interferes with Integrin signaling. It also functions as a chemoattractant for mesenchymal stem cells and enhances their BMP-2 and TGF-beta 3 induced differentiation into chondrocytes [tscheud]. MIA-deficient mice exhibit delayed chondrocyte differentiation but enhanced chondrocyte proliferation and cartilage repair. MIA is up-regulated in several cancers including malignant melanoma, lung adenoma, metastatic oral squamous cell carcinoma, neurofibromatosis type 1 (NF-1)-related tumors, and pancreatic cancer. It is selectively secreted and internalized from the trailing pole of migrating cells. This polarization reduces cellular attachment to the matrix at the trailing pole and contributes to directional tumor cell migration. Product Properties Synonyms CD-RAP Accession Q16674 GeneID 8190 Source E.coli-derived Human MIA, Gly25-Gln31. Molecular Weight Approximately 12.1 kDa. AA Sequence GPMPKLADRK LCADQECSHP ISMAVALQDY MAPDCRFLTI HRGQVVYVFS KLKGRGRLFW GGSVQGDYYG DLAARLGYFP SSIVREDQTL KPGKVDVKTD KWDFYCQ 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 A375 cell line is less than 5 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 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 0.1-1.0mg/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!

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Mesencephalic astrocyte-derived neurotrophic factor (MANF), also known as arginine-rich, mutated in early stage tumors (ARMET) and arginine-rich protein (ARP), is a 20 kDa member of the ARMET family of proteins. The name ARMET comes from the fact that the protein was initially thought to be 50 aa longer at the N-terminus and to contain an arginine-rich region. The presence of a  specific mutation changing the previously numbered codon 50 from ATG to AGG, or deletion of that codon, has been reported in a variety of solid tumors. Human MANF is synthesized as a 179 amino acid (aa) precursor that contains a 21 aa signal sequence and a 158 aa mature chain. Mature human MANF is 99%, 98% and 96% aa identical to mature rat, mouse and  bovine  MANF,  respectively. MANF is localized to the endoplasmic reticulum (ER) and Golgi apparatus, and is also secreted. In the CNS, MANF selectively protects nigral dopaminergic neurons, versus GABAergic or serotonergic neurons, which suggests that MANF may be indicated for the treatment of Parkinson’s disease. MANF is also one of the 12 commonly unfolded protein response (UPR)-up-regulated genes. One study showed that MANF plays an important role in protecting cells against tunicamycin and thapsigargin-induced cell death. Loss of MANF renders cells more susceptible to those drugs, but also increases cell proliferation and decreases cell size. Another study showed that MANF is an endoplasmic reticulum stress response (ERSR) gene in the heart that can be induced and secreted in response to ER stresses, including ischemia, and that extracellular MANF may protect cardiac myocytes  in an autocrine and paracrine manner. Product Properties Synonyms ARMET Accession P5514 Source E.coli-derived Human MANF, Leu25-Leu182. GeneID 7873 Tag None Molecular Weight Approximately 18.2 kDa. AA Sequence LRPGDCEVCI SYLGRFYQDL KDRDVTFSPA TIENELIKFC REARGKENRL CYYIGATDDA ATKIINEVSK PLAHHIPVEK    ICEKLKKKDS QICELKYDKQ IDLSTVDLKK LRVKELKKIL DDWGETCKGC AEKSDYIRKI NELMPKYAPK AASARTDL Endotoxin < 1.0 EU/μg by the LAL method. Purity ＞ 98%, as determined by SDS-PAGE and HPLC analysis. Biological Activity The ED50 as determined by a cell proliferation assay using rat C6 cells is less than 20 μg/mL, corresponding to a specific activity of > 50 IU/mg. Fully biologically active when compared to standard. 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!

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MIC-B (MHC class I chain-related gene B) is a single-pass type I member protein. A closely related protein, MICA, shares 85% amino acid identity with MICB. It is widely expressed in many, but not all, epithelial tumors of lung, breast, kidney, ovary, prostate and colon. In addition to this, it is produced by hepatocellular carcinomas, which is only in tumor cells but not in surrounding non-cancerous tissue and can be induced by bacterial and viral infections. MICA/B are ligands for NKG2D, an activating receptor expressed on NK cells, NKT cells, gamma δ T cells, and CD8+ alpha beta T cells. Recognition of MICA/B by NKG2D results in the activation of cytolytic activity and/or cytokine production by these effector cells. MICA/B recognition is involved in tumor surveillance, viral infections, and autoimmune diseases. The release of soluble forms of MICA/B from tumors down-regulates NKG2D surface expression on effector cells resulting in the impairment of anti-tumor immune response. Product Properties Synonyms MHC class I chain-related protein B, MICB, stress inducible class I homolog Accession NP_005922 Source E.coli-derived human MIC-B protein, Ala23-Asp309. GeneID 4277 Tag None Molecular Weight Approximately 32.8 kDa. AA Sequence AEPHSLRYNL MVLSQDESVQ SGFLAEGHLD GQPFLRYDRQ KRRAKPQGQW AEDVLGAKTW DTETEDLTEN GQDLRRTLTH IKDQKGGLHS LQEIRVCEIH EDSSTRGSRH FYYDGELFLS QNLETQESTV PQSSRAQTLA MNVTNFWKED AMKTKTHYRA MQADCLQKLQ RYLKSGVAIR RTVPPMVNVT CSEVSEGNIT VTCRASSFYP RNITLTWRQD GVSLSHNTQQ WGDVLPDGNG TYQTWVATRI RQGEEQRFTC YMEHSGNHGT HPVPSGKVLV LQSQRTD Endotoxin < 1 EU/μg of protein as determined by LAL method Purity ＞ 95%, as determined by SDS-PAGE and HPLC analysis. Biological Activity The specific activity is determined by binding MICB antibody in ELISA. Fully biologically active when compared to standard. Formulation Lyophilized from a 0.2 μm filtered concentrated solution in 20 mM Tris, 150 mM NaCl, pH 8.0. 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℃ 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!

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Midkine (MK) is a 15 kDa heparin-binding molecule originally cloned during a search for genes preferentially transcribed during retinoic acid (RA)-induced differentiation. Midkine belongs to a family of neurotrophic and developmentally-regulated heparin-binding molecules consisting of midkine, pleiotrophin (PTN/HBNF/OSF-1/HNGF-8) and the avian midkine  homolog, RI-HB (for retinoic acid-inducible heparin-binding protein). Midkine is a highly basic, nonglycosylated polypeptide that contains  five intrachain disulfide bonds. The predicted molecular weight is approximately 13.3 kDa, based on a mature peptide length of 118 amino acid residues in the mouse and 121 amino acid residues in the human. Across species, MK shows 87% identity between the human and murine proteins. Between family members, human MK is approximately 50% identical to human PTN, with conservation of all 10 cysteines. Initial structure-function studies indicate that the C-terminal half of MK contains the principal heparin-binding  site plus the molecule’s antigenicity and neurite-promoting sequences; while both the C- and N-termini are necessary for the molecule’s neurotrophic effects. Product Properties Synonyms ARAP, Midgestation and Kidney Protein, Neurite Outgrowth-promoting Factor 2, Neurite Outgrowth-promoting Protein Accession P21741 Source E.coli-derived Human Midkine, Val21-Asp143. GeneID 4192 Tag None Molecular Weight Approximately 13.4 kDa. AA Sequence VAKKKDKVKK GGPGSECAEW AWGPCTPSSK DCGVGFREGT CGAQTQRIRC RVPCNWKKEF GADCKYKFEN WGACDGGTGT KVRQGTLKKA RYNAQCQETI RVTKPCTPKT KAKAKAKKGK GKD Endotoxin < 1 EU/μg of protein as determined by LAL method Purity ＞ 97%, as determined by SDS-PAGE and HPLC analysis. Biological Activity The biological activity determined by a chemotaxis bioassay using human neutrophils is in a concentration range of 0.1-10 ng/mL. Fully biologically active when compared to standard. Formulation Lyophilized from a 0.2 μm filtered concentrated solution in PBS, 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!

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As the first member of membrane type (MT) MMPs, MMP-14, also known as MT1-MMP, plays an important role in extracellular matrix (ECM) remodeling by being able to degrade type I collagen, activate pro-MMP-2 and process cell adhesion molecules such as CD44 and integrin alpha V. MMP-14 is therefore a key enzyme in many physiological and pathological processes such as angiogenesis and tumor invasion. Structurally, MMP-14 consists of the following domains: a pro domain containing the furin cleavage site, a catalytic domain containing the zinc-binding site, a hinge region, a hemopexin-like domain, a transmembrane domain, and a cytoplamasic tail. Product Properties Synonyms MMP-X1, MT-MMP 1, MT1-MMP Accession P50281 GeneID 4323 Source E.coli-derived Human MMP-14 protein, Ala21-Gly284. Molecular Weight Approximately 29.6 kDa. AA Sequence ALASLGSAQS SSFSPEAWLQ QYGYLPPGDL RTHTQRSPQS LSAAIAAMQK FYGLQVTGKA DADTMKAMRR PRCGVPDKFG AEIKANVRRK RYAIQGLKWQ HNEITFCIQN YTPKVGEYAT YEAIRKAFRV WESATPLRFR EVPYAYIREG HEKQADIMIF FAEGFHGDST PFDGEGGFLA HAYFPGPNIG GDTHFDSAEP WTVRNEDLNG NDIFLVAVHE LGHALGLEHS SDPSAIMAPF YQWMDTENFV LPDDDRRGIQ QLYG Tag None Physical Appearance Sterile Filtered White lyophilized (freeze-dried) powder. Purity > 95 % by SDS-PAGE and HPLC analyses. Biological Activity Test in Process. 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-HCl, pH 7.4, 300 mM NaCl, 3 mM CaCl2, 10 μM ZnCl2, with 30% 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°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 -15℃ to -25℃ 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.

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Matrix metalloproteinases are a family of zinc and calcium dependent endopeptidases with the combined ability to degrade all the components of the extracellular matrix. MMP-3 (stromelysin-1), can degrade a broad range of substrates including collagen alpha chains, aggrecan, laminin, fibronectin, elastin, casein, alpha -1 antitrypsin, myelin basic protein, IL-1 beta, IGFBP-3, pro MMP-1, pro MMP-7, pro MMP-8, pro MMP-9 and pro MMP-13. The MMP-3 substrate repertoire extends beyond extracellular matrix proteins and implicates MMP-3 in roles other than direct tissue remodelling, for instance, enzyme cascades and cytokine regulation   Product Properties   Synonyms Matrix Metalloproteinase-3, Stromelysin-1, SL-1, Transin-1 Source Recombinant Human MMP-3 Protein is expressed from E.coli with His tag at the C-terminal. It contains Arg101-Cys477. Endotoxin < 1.0 EU per μg by the LAL method. Purity > 95% by SDS-PAGE and HPLC analyses. Formulation Lyophilized from 0.22 μm filtered solution in PBS (pH 7.4). Applications ELISA, Kinetics (BLI), Kinetics (SPR), Immunization Dilution Dilute with PBS.   Storage    The products are shipped with ice pack and can be stored at -25~-15℃ for 1 year. 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.  

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CCL2, also called monocyte chemotactic protein- 1 (MCP- 1) or JE, is a member of the C- C or beta chemokine family that is best known as a chemotactic agent for mononuclear  cells . Human CCL2 cDNA encodes a 99 amino acid (aa) precursor protein with a   23 aa signal peptide and a 76 aa mature protein . Removal of the first 5 aa of the mature protein, including the N-terminal pyrrolidone carboxylic acid- modified glutamine, occurs naturally by metalloproteinase cleavage and down- regulates activity but not receptor binding. CCL2 may form multiple bands from 8.7- 13.5 kDa on SDS- PAGE due to non- covalent dimerization and variable carbohydrate content. Mature human CCL2 shares 78- 79% aa identity with canine, porcine and equine CCL2, while mouse and rat express a form of CCL2 that is extended by 49 aa and shares only 56% aa identity within the common region. Human CCL2 can, however, induce a response in murine cells. Product Properties Synonyms HC11, Monocyte chemoattractant protein 1, MCAF, MCP-1, Monocyte secretory protein JE, Small-inducible cytokine A2 Accession P13500 Source E.coli-derived Human CCL2 ,Gln23-Thr99. GeneID 6347 Tag None Molecular Weight Approximately 8.7 kDa. AA Sequence QPDAINAPVT CCYNFTNRKI SVQRLASYRR ITSSKCPKEA VIFKTIVAKE ICADPKQKWV QDSMDHLDKQ TQTPKT Endotoxin < 1 EU/μg of protein as determined by LAL method Purity ＞ 96%, as determined by SDS-PAGE and HPLC analysis. Biological Activity Fully biologically active when compared to standard. The biological activity determined by a chemotaxis bioassay using human monocytes is in a concentration range of 10-100 ng/mL. Formulation Lyophilized from a 0.2 μm filtered concentrated solution in 20 mM PB, pH 7.4, 100 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 0.1-1.0mg/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!

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The MCP proteins are members of the CC chemokine family that signal through CCR2 and, with the exception of MCP-1, other CCR receptors. The MCP proteins chemoattract and activate monocytes, activated Tcells, basophils, NK cells, and immature dendritic cells. The MCP family cross-reacts across species. Recombinant Human MCP-3 is a 9.0 kDa protein containing 76 amino acid residues including the four highly conserved cysteine residues present in the CC chemokines.   Product Properties   Synonyms Interleukin-6,BSF2,HSF,IFNB2 Accession P80098 GeneID 6354 Source E.coli-derived Human CCL7 protein,Gln24-Leu99. Molecular Weight Approximately 9.0 kDa AA Sequence QPVGINTSTT CCYRFINKKI PKQRLESYRR TTSSHCPREA VIFKTKLDKE ICADPTQKWV QDFMKHLDKK TQTPKL 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 human monocytes 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 20 mM PB, pH 7.4, 150 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 °C. Further dilutions should be made in appropriate buffered solutions.   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.   Caution   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.

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