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Sox2 belongs to a diverse family of structurally-related transcription factors whose primary structure contains a 79-residue DNA-binding domain, called high mobility group (HMG) box. It plays an essential role in maintaining the pluripotency of embryonic stem cells (ESC) and the determination of cell fate. Microarray analysis showed that Sox2 regulates the expression of multiple genes involved in embryonic development, including FGF-4, YES1 and ZFP206. Sox2 acts as a transcriptional activator after forming a ternary complex with Oct3/4 and a conserved non-coding DNA sequence (CNS1) located approximately 2 kb upstream of the RAX promoter. The introduction of Sox2, Oct4, Myc, and Klf4 into human dermal fibroblasts isolated from a skin biopsy of a healthy research fellow was sufficient to confer a pluripotent state upon the fibroblast genome. The reprogrammed cells thus obtained resemble ESC in morphology, gene expression, and in their capacity to form teratomas in immune-deficient mice. Sox2 and other transcription factors have been introduced into cells by DNA transfection, viral infection, or microinjection. Product Properties   Synonyms SOX2-TAT Accession P48431 GeneID 6657 Source E.coli-derived Human SOX2-TAT, Met1-Met317, with an N-terminal Met. Molecular Weight Approximately 36.0kDa. AA Sequence MYNMMETELK PPGPQQTSGG GGGNSTAAAA GGNQKNSPDRVKRPMNAFMVWSRGQRRKMA QENPKMHNSE ISKRLGAEWK LLSETEKRPF IDEAKRLRAL HMKEHPDYKYRPRRKTKTLM KKDKYTLPGG LLAPGGNSMA SGVGVGAGLG AGVNQRMDSY AHMNGWSNGS YSMMQDQLGY PQHPGLNAHG AAQMQPMHRY DVSALQYNSM TSSQTYMNGS PTYSMSYSQQ GTPGMALGSM GSVVKSEASS SPPVVTSSSH SRAPCQAGDL RDMISMYLPG AEVPEPAAPS RLHMSQHYQS GPVPGTAING TLPLSHMGGY GRKKRRQRRR Tag None Physical Appearance Sterile Filtered White lyophilized (freeze-dried) powder. Purity > 95 % by SDS-PAGE and HPLC analyses. Biological Activity Data Not Available. Endotoxin Less than 1.0 EU/μg of the protein as determined by LAL method. Formulation Lyophilized from a 0.2 μm filtered concentrated solution in 2 × PBS, pH 7.4, with 5% Trehalose. Reconstitution We recommend that this vial be briefly centrifuged prior to opening to bring the contents to the bottom.Reconstitute in sterile distilled water or aqueous buffer containing 0.1 % BSA to a concentration of 0.1-1.0 mg/mL. Stock solutions should be apportioned into working aliquots and stored at ≤ -20°C. Further dilutions should be made in appropriate buffered solutions.   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.   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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RANKL and RANK are members of the TNF superfamily of ligands and receptors that play an important role in the regulation of specific immunity and bone turnover. RANK (receptor) was originally identified as a dendritic cell-membrane protein, which, by interacting with RANKL, augments the ability of dendritic cells. These dendritic cells then stimulate naïve T-cell proliferation in a mixed lymphocyte reaction, promote the survival of RANK+ T-cells, and regulate T-cell-dependent immune response. RANKL, which is expressed in a variety of cells, including osteoblasts, fibroblasts, activated T-cells and bone marrow stromal cells, is also capable of interacting with a decoy receptor called OPG. Binding of soluble OPG to sRANKL inhibits osteoclastogenesis by interrupting the signaling between stromal cells and osteoclastic progenitor cells, thereby leading to excess accumulation of bone and cartilage.   Product Properties   Synonyms soluble Receptor Activator of NF-κB Ligand, TNFSF11, TRANCE (TNF-related activation-induced cytokine), OPGL, ODF Accession O14788 Source HEK293 Cells-derived human sRANKL protein, Gly64-Asp24 Molecular Weight Approximately 20.5 kDa. AA Sequence VALFFYF RAQMDPNRIS EDGTHCIYRI LRLHENADFQ DTTLESQDTK LIPDSCRRIK QAFQGAVQKE LQHIVGSQHI RAEKAMVDGS WLDLAKRSKL EAQPFAHLTI NATDIPSGSH KVSLSSWYHD RGWAKISNMT FSNGKLIVNQ DGFYYLYANI CFRHHETSGD LATEYLQLMV YVTKT Tag None Physical Appearance Sterile Filtered White lyophilized (freeze-dried) powder. Purity > 85 % by SDS-PAGE  analyses. Biological Activity 1. Immobilized human TNFSF11 at 2 μg/ml (100 μL/well) can bind human Osteoprotegerin hFc, the EC50 of human Osteoprotegerin hFc is 5-40 ng/mL. 2. The bioactivity of hRANKL was determined by measuring the ability of hRANKL to induce TRAP activity in Raw 264.7 cells. The ED50 for this effect is typically 1.5-7.5 ng/mL. Endotoxin Less than 1.0 EU/μg of the protein as determined by 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.   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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  Name Catalog No. Size Recombinant Human SSR1 Protein-VLP C230753E 20 μg C230753S 100 μg C230753M 100 μg C230753L 1 mg   Product Properties   Synonyms Translocon-associated protein subunit alpha;SSR1; TRAPA; Translocon-associated protein subunit alpha; TRAP-alpha; Signal sequence receptor subunit alpha; SSR-alpha Source HEK293 Cells AA sequence Accession #P30872:Met1 - Leu391 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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TRAIL Receptor-1/DR4 and TRAIL Receptor-2/DR5 belong to the TNFR superfamily of transmembrane proteins, and contain a cytoplasmic "death domain," which can activate the cell's apoptotic machinery. These receptors are activated by binding to either membrane-anchored or soluble TRAIL/Apo2L. The DR4 and DR5 receptors are both produced as type I transmembrane proteins, which contain an extracellular domain, a transmembrane domain, and a cytoplasmic domain. The recombinant soluble forms of DR4 and DR5 consist of the TNFR-homologous, cysteine-rich portion of their respective extracellular domains. Recombinant Human soluble TRAIL Receptor-2/DR5 is a 14.9 kDa protein (133 amino acid residues) consisting of the TNFR-homologous, cysteine-rich portion of the extracellular domain.   Product Properties   Synonyms soluble TRAIL Receptor-2, DR5, TNFRSF10B, KILER, TRICK2A, TRICKB Accession O14763 GeneID 8795 Source E.coli-derived Human soluble TRAIL Receptor-2 protein,Glu52-Ser183. Molecular Weight Approximately 14.8 kDa. AA Sequence ESALITQQDL APQQRAAPQQ KRSSPSEGLC PPGHHISEDG RDCISCKYGQ DYSTHWNDLL FCLRCTRCDS GEVELSPCTT TRNTVCQCEE GTFREEDSPE MCRKCRTGCP RGMVKVGDCT PWSDIECVHK ES 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. rHusTRAIL-R2 reduced the production of LPS-induced TNF by its ability to neutralize endogenous TRAIL in fresh human PBMC. In this assay, endogenous TRAIL is induced during a 24 hour exposure to LPS (10 ng/mL) but in the presence of rHusTRAIL-R2, TRAIL-induced TNF is suppressed. Endotoxin Less than 1.0 EU/μg of the protein as determined by LAL method. Formulation Lyophilized from a 0.2 μm filtered concentrated solution in 20mM PBS, pH 7.0. 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.   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.   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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CXCL12, also known as SDF-1, is a heparin-binding member of the CXC (or alpha-) family of chemokines. SDF-1 alpha and SDF-1 beta are the first cytokines initially identified using the signal sequence trap cloning strategy from a mouse bone-marrow stromal cell line. These proteins were subsequently also cloned from a human stromal cell line. CXCL12β is synthesized as a 93 amino acid (aa) precursor that contains a 21 aa signal sequence and a 72 aa mature region. The mature molecule exhibits a typical three antiparallel beta -strand chemokine-like fold. There are no potential N-linked glycosylation sites.The C-terminus is likely associated with heparin binding . SDF-1 beta circulates and undergoes proteolytic processing. CD26 will remove the first two N-terminal amino acids, possibly creating a reduced-activity chemokine. On the cell surface, the receptor for this chemokine is CXCR4 and syndecan4. Among its many functions, CXCL12 is known to influence lymphopoiesis, regulate patterning and cell number of neural progenitors, and promote angiogenesis. It also enhances the survival of myeloid progenitor cells.   Product Properties   Synonyms hSDF-1 beta, IRH, hIRH, PBSF Accession P48061 GeneID 6387 Source E.coli-derived Human SDF-1β/CXCL12β, Lys22-Met93. Molecular Weight Approximately 8.5 kDa. AA Sequence KPVSLSYRCP CRFFESHVAR ANVKHLKILN TPNCALQIVA RLKNNNRQVC IDPKLKWIQE YLEKALNKRF KM Tag None Physical Appearance Sterile Filtered White lyophilized (freeze-dried) powder. Purity > 97 % by SDS-PAGE and HPLC analyses. Biological Activity The biological activity determined by a chemotaxis bioassay using PHA and rHuIL-2 activated human peripheral blood T-lymphocytes is in a concentration range of 20-80 ng/mL. Fully biologically active when compared to standard. Endotoxin Less than 1.0 EU/μg of the protein as determined by 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.   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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Human CXCL12 is expressed as five isoforms that differ only in the C-terminal tail. The gamma isoform of CXCL12, also known as SDF-1 gamma, is a 12 kDa, heparin-binding member of the CXC (or alpha) family of chemokines ,Mature SDF-1 molecules are not glycosylated and exhibit a typical three antiparallel beta -strand chemokine-like fold. N-terminal aa 1 - 8 form a receptor binding site, while aa 1 and 2 (Lys- Pro) are involved in receptor activation. All SDF-1 isoforms can undergo proteolytic processing of the first two N-terminal amino acids by CD26, which is thought to create a reduced- activity chemokine. Human SDF-1 gamma is synthesized as a 119 amino acid (aa) precursor that contains a 21 aa signal sequence and a 98 aa mature region. Mature human SDF-1 gamma shares 99%, 97% and 98% aa identity with mouse, rat, and equine SDF-1 gamma, respectively. The unique C-terminal 26 aa of SDF-1 gamma are highly charged, including four BBXB (where B = basic and X = any aa) motifs, while the most prevalent form, SDF-1 alpha, has 4 unique C-terminal aa and binds heparin via the shared BBXB site more N-terminally located . The SDF- 1 gamma C-terminus binds heparin in secreted SDF-1 gamma, or targets the isoform to the nucleolus in the absence of a signal sequence. SDF-1 isoforms interact with CXCR4 and CXCR7 receptors on the cell surface, and can also bind syndecan-4.   Product Properties   Synonyms CXCL12γ Accession P48061 GeneID 6387 Source E.coli-derived Human CXCL12γ protein,Gly21-Asn119. Molecular Weight Approximately 11.6 kDa. AA Sequence GKPVSLSYRC PCRFFESHVA RANVKHLKIL NTPNCALQIV ARLKNNNRQV CIDPKLKWIQ EYLEKALNKG RREEKVGKKE KIGKKKRQKK RKAAQKRKN 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 biological activity determined by a chemotaxis bioassay using PHA and rHuIL-2 activated human peripheral blood T-lymphocytes is in a concentration range of 30-100 ng/mL. Endotoxin Less than 0.1 EU/μg of the 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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Syndecan-4, previously known as amphiglycan or ryudocan, is a member of the syndecan family of Type 1 transmembrane proteins capable of carrying heparan sulfate (HS) and chondroitin sulfate glycosaminoglycans. Human Syndecan-4 ECD shares  approximately 79%, 78% and 81% aa identity with mouse, rat and porcine Syndecan-4 ECD, respectively. Syndecans are the best-characterized plasma membrane proteoglycans with two conserved cytoplasmic domains and divergent extracellular portions, except for HS attachment sites. SYND4 is the most similar to SYND2, but is more universally expressed and is found in virtually every cell type. Expression can be upregulated by TGFβ2 and in response to mechanical stress in smooth muscle, wound healing, arterial injury or acute myocardial infarction, probably in response to at least one inflammatory mediator. SYND4 has more widespread distribution than other syndecans and it is the only syndecan that has been found consistently in focal adhesions.   Product Properties Synonyms Amphiglycan, MGC22217, Ryudocan, SDC4, syndecan 4, Syndecan4 Accession P31431 GeneID 6385 Source E.coli-derived human SYND4 protein, Glu19-Glu145 Molecular Weight Approximately 13.9 kDa. AA Sequence ESIRETEVID PQDLLEGRYF SGALPDDEDV VGPGQESDDF ELSGSGDLDD LEDSMIGPEV VHPLVPLDNH IPERAGSGSQ VPTEPKKLEE NEVIPKRISP VEESEDVSNK VSMSSTVQGS NIFERTE Tag None Physical Appearance Sterile Filtered White lyophilized (freeze-dried) powder. Purity > 95 % by SDS-PAGE and HPLC analyses. Biological Activity The specific activity is determined by binding ability in a functional ELISA. Immobilized recombinant human SYND4 at 500 ng/mL (100 μl/well) can bind recombinant human bFGF with a linear range of 0.1-10 ng/mL. Fully biologically active when compared to standard. Endotoxin < 0.1 EU per 1μg of the protein by the LAL method. Formulation Lyophilized from a 0.2 μm filtered concentrated solution in PBS, pH 7.4. 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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Syndecan-4, previously known as amphiglycan or ryudocan, is a member of the syndecan family of Type 1 transmembrane proteins capable of carrying heparan sulfate (HS) and chondroitin sulfate glycosaminoglycans. Human Syndecan-4 ECD shares approximately 79%, 78% and 81% aa identity with mouse, rat and porcine Syndecan-4 ECD, respectively. Syndecans are the best-characterized plasma membrane proteoglycans with two conserved cytoplasmic domains and divergent extracellular portions, except for HS attachment sites. SYND4 is the most similar to SYND2, but is more universally expressed and is found in virtually every cell type. Expression can be upregulated by TGFβ2 and in response to mechanical stress in smooth muscle, wound healing, arterial injury or acute myocardial infarction, probably in response to at least one inflammatory mediator. SYND4 has more widespread distribution than other syndecans and it is the only syndecan that has been found consistently in focal adhesions.   Product Properties   Synonyms Amphiglycan, MGC22217, Ryudocan, SDC4, syndecan 4, Syndecan4 Accession P31431 GeneID 6385 Source E.coli-derived human SYND4 protein,Glu19-Glu145. Molecular Weight Approximately 13.9 kDa. AA Sequence ESIRETEVID PQDLLEGRYF SGALPDDEDV VGPGQESDDF ELSGSGDLDD LEDSMIGPEV VHPLVPLDNH IPERAGSGSQ VPTEPKKLEE NEVIPKRISP VEESEDVSNK VSMSSTVQGS NIFERTE Tag None Physical Appearance Sterile Filtered White lyophilized (freeze-dried) powder. Purity > 95 % by SDS-PAGE and HPLC analyses. Biological Activity The specific activity is determined by binding ability in a functional ELISA. Immobilized recombinant human SYND4 at 500 ng/mL (100 μl/well) can bind recombinant human bFGF with a linear range of 0.1-10 ng/mL. Fully biologically active when compared to standard. Endotoxin Less than 0.1 EU/μg of the protein as determined by 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.   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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CCL17, also known as thymus and activation-related chemokine (TARC), a small cytokine belonging to the C-C chemokine family. Among CC chemokine family members, CCL17 has approximately 24 - 29% amino acid sequence identity with RANTES, MIP-1 alpha, MIP-1 beta, MCP-1, MCP-2, MCP-3 and I-309. CCL17 is constitutively expressed in thymus, and at a lower level in lung, colon, and small intestine. CCL17 is also transiently expressed in phytohemagglutinin-stimulated peripheral blood mononuclear cells. CCL17 has been shown to be chemotactic for T cell lines but not monocytes or neutrophils. CCL17 was identified to be a specific functional ligand for CCR4, a receptor that is selectively expressed on T cells.   Product Properties Synonyms MGC138273, SCYA17, SCYA17MGC138271 Accession Q92583 GeneID 6361 Source E.coli-derived Human TARC/CCL17, Ala24-Ser93. Molecular Weight Approximately 8.1 kDa. AA Sequence ARGTNVGREC CLEYFKGAIP LRKLKTWYQT SEDCSRDAIV FVTVQGRAIC SDPNNKRVKN AVKYLQSLER S Tag None Physical Appearance Sterile Filtered White lyophilized (freeze-dried) powder. Purity > 97% by SDS-PAGE and HPLC analyses. Biological Activity The biological activity determined by a chemotaxis bioassay using human T-lymphocytes is in a concentration range of 1.0-10 ng/mL. Fully biologically active when compared to standard. Endotoxin < 1.0 EU per 1μg of the protein by the LAL method. Formulation Lyophilized from a 0.2 μm filtered concentrated solution in 20 mM PB, 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 0.1-1.0mg/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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Transforming Growth Factor-alpha (TGF-α) , also known as sarcoma growth factor, TGF-type I and ETGF, is a member of the EGF family of cytokines. TGF-α is an EGF-related polypeptide growth factor that signals through the EGF receptor, and stimulates the proliferation of a wide range of epidermal and epithelial cells.Mature TGF-alpha shows approximately 93% amino acid sequence identity with mouse or rat TGF-alpha and is not species specific in its biological effects. Product Properties Synonyms Transforming Growth Factor alpha; TGF-a; TGF-type I; ETGF Accession P01135  Gene ID 7039 Source E.coli-derived Human TGF-a protein, Vla40-Ala89 Molecular Weight Approximately 5.8 kDa, on SDS-PAGE under reducing conditions AA Sequence V VSHFNDCPDS HTQFCFHGTC RFLVQEDKPA CVCHSGYVGA RCEHADLLA Tag None Physical Appearance Sterile Filtered White lyophilized (freeze-dried) powder Purity > 95% as determined by SDS-PAG Biological Activity Measured in a cell proliferation assay using Balb/3T3 mouse embryonic fibroblast cells. The ED50 for this effect is < 0.4 ng/mL. Endotoxin < 1.0 EU per 1μg of the protein by the LAL method Formulation Lyophilized after extensive dialysis against PBS. Reconstitution We recommend that this vial be briefly centrifuged prior to opening to bring the contents to the bottom. Reconstitute the lyophilized powder in ddH₂O or PBS up to 100 μg/ml.For long term storage it is recommended that a carrier protein (example 0.1% BSA) be added. Avoid repeated freeze-thaw cycles.   Shipping and Storage The products are shipped with ice pack and can be stored at -80℃ for 1 year from date of receipt. 1week, 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. For your safety and health, please wear lab coats and disposable gloves for operation. 2. For research use only!

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TGFβ3 is a member of the TGF-β superfamily subgroup, defined by its structural and functional similarities. TGF-β3, along with β1 and β2, acts as a cellular switch to regulate immune function, cell proliferation, and epithelial-mesenchymal transition. The human TGF-β3 cDNA encodes a 412 amino acid (aa) precursor, which contains a 20 aa signal peptide and a 392 aa protein. Mature human TGF-β3 shares 100%, 99%, and 98% homology with mouse/dog/horse, rat, and pig TGF-β3, respectively. TGF-β3 has a high affinity for TGF-βRII, a type II serine/threonine kinase receptor. This receptor phosphorylates and activates the type I serine/threonine kinase receptor TGF-βRI or ALK-1 to regulate transcription through Smad phosphorylation. The product is provided in the form of a lyophilized (freeze-dried) powder, characterized by high activity, high purity, and low endotoxin levels. Product Properties Synonyms TGF-β3; ARVD; ARVD1; FLJ16571; LDS5; RNHF; TGFB3; TGFbeta 3; TGF-beta 3; TGF-beta3; TGF-beta-3; transforming growth factor beta-3; transforming growth factor beta 3 Uniprot No. P10600 Expression System and Range CHO-derived Human TGF-β3, Ala 301-Ser 412 Molecular Weight Approximately 13 kDa AA Sequence MALDTNYCFRN LEENCCVRPL YIDFRQDLGW KWVHEPKGYY ANFCSGPCPY LRSADTTHST VLGLYNTLNP EASASPCCVP QDLEPLTILY YVGRTPKVEQ LSNMVVKSCK CS Appearance White powder, Colorless clear liquid after reconstitution Purity ≥95%, by SDS-PAGE (under reducing (R) & Non-reducing conditions, visualized by Coomassie staining. Biological Activity Measured in a cell inhibition assay using TF-1 cells at IL4 presence. The ED50 for this effect is ≤0.2ng/mL. Endotoxin < 10 EU/mg of the protein by the LAL method Formulation Lyophilized from a 0.22 μm-filtered solution containing 100 mM Glycine, 150 mM NaCl, 5% mannitol and 0.01% Tween 80, pH 4.0   Method of Use It is recommended to centrifuge before opening the cap to bring the contents to the bottom, and then resuspend with sterile deionized water. Transportation and Storage Methods Store at -20°C, with a one-year shelf life upon receipt. After resuspension, store at 2~8°C for a shelf life of 7-10 days. After resuspension, store at -85 to -65°C for a shelf life of six months. It is recommended to aliquot and freeze for the first use to avoid repeated freeze-thaw cycles. Cautions 1.For your safety and health, please wear a lab coat and use disposable gloves when operating. 2.This product is intended for scientific research purposes only.

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TGF-beta 2 (transforming growth factor beta 2) is one of three closely related mammalian members of the large TGF-beta superfamily that share a characteristic cysteine knot structure. TGF-beta 1, -2 and -3 are highly pleiotropic cytokines proposed to act as cellular switches that regulate processes such as immune function, proliferation and epithelial-mesenchymal transition. Each TGF-beta isoform has some non-redundant functions; for TGF-beta 2, mice with targeted deletion show defects in development of cardiac, lung, craniofacial, limb, eye, ear and urogenital systems . Human TGF-beta 2 cDNA encodes a 414 amino acid (aa) precursor that contains a 19 aa signal peptide and a 395 aa proprotein. A furin-like convertase processes the proprotein to generate an N-terminal 232 aa latency-associated peptide (LAP) and a C-terminal 112 aa mature TGF- beta 2. Disulfide-linked homodimers of LAP and TGF-beta 2 remain non-covalently associated after secretion, forming the small latent TGF-beta 1 complex. Covalent linkage of LAP to one of three latent TGF-beta binding proteins (LTBPs) creates a large  latent complex that may interact with the extracellular matrix. Mature human TGF-beta 2 shows 100% aa identity with porcine, canine, equine and bovine TGF-beta 2, and 97% aa identity with mouse and rat TGF-beta 2. It demonstrates cross-species activity. Product Properties Synonyms Transforming Growth Factor beta 2 Accession P61812 Gene ID 7042 Source NS0-derived Human TGF-β2 protein, Ala303-Ser414 Molecular Weight Approximately 24 kDa AA Sequence ALDAAYCF RNVQDNCCLR PLYIDFKRDL GWKWIHEPKG YNANFCAGAC PYLWSSDTQH SRVLSLYNTI NPEASASPCC VSQDLEPLTI LYYIGKTPKI EQLSNMIVKS CKCS Tag None Physical Appearance Sterile Filtered White lyophilized (freeze-dried) powder Purity > 97% as determined by SDS-PAGE. Biological Activity Measured by its ability to inhibit the IL-4-dependent proliferation of HT‑ 2 mouse T cells. The ED50 for this effect is 0.025-0.25 ng/mL. Endotoxin < 0.1 EU per 1μg of the protein by the LAL method Formulation Lyophilized from 0.2 µm filtered concentrated solution in 35 % Acetonitrile and 0.1 % TFA Reconstitution We recommend that this vial be briefly centrifuged prior to opening to bring the contents to the bottom. Reconstitute in sterile 4 mM HCl to a concentration of 0.1 mg/ml. Stock solutions should be apportioned into working aliquots and stored at ≤ -20 °C. Further dilutions should be made in appropriately buffered solutions.   Shipping and Storage The products are shipped with ice pack and can be stored at -20℃ to -70 °C 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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Thymic stromal lymphopoietin (TSLP) is an interleukin 7 (IL-7)-like cytokine originally characterized by its ability to promote the activation of B cells and dendritic cells (DCs). Both mouse TSLP and IL-7 can co-stimulate growth of thymocytes and mature T cells, and support B lymphopoiesis in long-term cultures of fetal liver cells and bone-marrow cells. Whereas mouse IL-7 facilitates the development of B220+/IgM- pre-B cells, mouse TSLP promotes the development B220+/IgM+ B cells. Human TSLP was reported   to preferentially stimulate myeloid cells; inducing the release of T cell-attracting chemokines from monocytes and enhancing the maturation of CD11c+ dendritic cells. Thymic stromal lymphopoietin (TSLP) is a cytokine expressed by epithelial cells, including keratinocytes, and is important in allergic inflammation. Subsequent studies have shown that TSLP promotes T helper type 2 (TH2) cell responses associated with immunity to some helminth parasites and the pathogenesis of many inflammatory diseases, including atopic dermatitis and asthma. TSLP can promote TH2 cytokine-associated inflammation by directly promoting the effector functions of CD4+ TH2 cells, basophils and other granulocyte populations while simultaneously limiting the expression of DC-derived proinflammatory cytokines and promoting regulatory T cell responses in peripheral tissues.   Product Properties Synonyms thymic stromal lymphopoietin Accession Q969D9 GeneID 85480 Source E.coli-derived Human TSLP, Tys29-Gln159, with an N-terminal Met Molecular Weight Approximately 15.1 kDa. AA Sequence MYDFTNCDFE KIKAAYLSTI SKDLITYMSG    TKSTEFNNTV SCSNRPHCLT EIQSLTFNPT AGCASLAKEM FAMKTKAALA IWCPGYSETQ INATQAMKKR RKRKVTTNKC LEQVSQLQGL WRRFNRPLLK QQ 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 IL-7Rα and human TSLP R co-transfected murine BaF3 pro-B cells is less than 0.3 ng/mL, corresponding to a specific activity of > 3.3× 106 IU/mg. Fully biologically active when compared to standard. Endotoxin < 1.0 EU per 1μg of the protein by the LAL method. Formulation Lyophilized from a 0.2 μm filtered concentrated solution in 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 0.1-1.0mg/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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Thymosin Beta 4 is a naturally occurring peptide encoded by the TMSB4X gene located on Chr. X in humans. It is found in high concentrations in blood platelets, wound fluid and other tissues in the body. Tβ-4 is a major actin regulating peptide and the primary function is to stimulate the productions of T cells, which plays important part of the immune system. The thymosin beta-4 peptide, if used after a heart attack, might reactivate cardiac progenitor cells to repair damaged heart tissue.   Product Properties Synonyms Fx Accession P62328 GeneID 7114 Source E.coli-derived human Tβ-4 protein, Ser2-Ser44.  Molecular Weight Approximately 4.9 kDa. AA Sequence SDKPDMAEIE KFDKSKLKKT ETQEKNPLPS KETIEQEKQA GES Tag None Physical Appearance Sterile Filtered White lyophilized (freeze-dried) powder. Purity > 97% by SDS-PAGE and HPLC analyses. Biological Activity The biological activity determined by its ability to produce a protective effect against hydrogen peroxide in primary lung fibroblasts is in a concentration range of 0.5 - 10 μg/mL. Fully biologically active when compared to standard. Endotoxin < 1.0 EU per 1μg of the protein by the LAL method. Formulation Lyophilized from a 0.2 μm filtered concentrated solution in 20 mM PB, pH 7.4. Reconstitution We recommend that this vial be briefly centrifuged prior to opening to bring the contents to the bottom. Reconstitute in sterile distilled water or aqueous buffer containing 0.1% BSA to a concentration of 0.1-1.0mg/mL. Stock solutions should be apportioned into working aliquots and stored at ≤ -20℃. Further dilutions should be made in appropriate buffered solutions.   Shipping and Storage The products are shipped with ice pack and can be stored at -20℃ to -80℃ for 1 year. Recommend to aliquot the protein into smaller quantities when first used and avoid repeated freeze-thaw cycles.   Cautions 1. Avoid repeated freeze-thaw cycles. 2. For your safety and health, please wear lab coats and disposable gloves for operation. 3. For research use only!

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TECK is a CC chemokine, specifically expressed by thymic stromal cells, and signals through the CCR9 receptor. TECK is chemotactic towards activated macrophages, thymocytes and dendritic cells. Recombinant Human TECK is a 14.3 kDa protein containing 127 amino acid residues, including the four conserved cysteine residues present in CC chemokines.   Product Properties Synonyms TECK, CCL25, SCYA25, Ckb15 Accession O15444 GeneID 6370 Source E.coli-derived Human CCL25 protein,Glu24-Leu150. Molecular Weight Approximately 14.3 kDa. AA Sequence MQGVFEDCCL AYHYPIGWAV LRRAWTYRIQ EVSGSCNLPA AIFYLPKRHR KVCGNPKSRE VQRAMKLLDA RNKVFAKLHH NTQTFQAGPH AVKKLSSGNS KLSSSKFSNP ISSSKRNVSL LISANSGL 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 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 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 0.1-1.0mg/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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TL-1A belongs to the TNF superfamily of ligands. It is expressed predominantly in endothelial cells, and to a lesser extent in the placenta, lung, kidney, skeletal muscle, pancreas, small intestine and colon. TL-1A inhibits endothelial cell proliferation and angiogenesis.   Product Properties Synonyms TL1A; TNF-like 1 Accession O95150 Source E.coli-derived Human TL-1A protein,Leu72-Leu251. Molecular Weight Approximately 20.5 kDa Purity > 97% by SDS-PAGE. 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, with 1% BSA. Reconstitution 1. We recommend that this vial be briefly centrifuged prior to opening to bring the contents to the bottom. Reconstitute in sterile PBS, pH 7.4, with 0.1% BSA to a concentration of 0.1-1.0 mg/mL. 2. Stock solutions should be apportioned into working aliquots and stored at ≤ -20 °C. 3.Further dilutions should be made in PBS, which must contain carrier proteins, such as 0.1% BSA, 10% FBS, 5% HSA, 5% trehalose, one of four options.   Shipping and Storage The product should be stored at -25~-15℃ for 1 year date of receipt. 1 month, 2 ~8 °C under sterile conditions after reconstitution. 3 months, -25~-15℃ °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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Human TNF-alpha is a cytokine that plays a crucial role in the inflammatory response. It is produced by various immune cells such as macrophages and T-cells and is involved in the regulation of immune cell proliferation, differentiation, and apoptosis.   Product Properties Synonyms Tumor Necrosis Factor, TNFA, TNFSF2, Cachectin, Cytotoxin, Differentiation-inducing factor, DIF Uniprot No. P01375 Source E.coli-derived human TNF-α/TNFSF2 protein, Val77-Leu233, with C-terminal His tag. Molecular Weight Approximately 18.5 kDa. Purity > 95% as determined by SDS-PAGE. Endotoxin < 0.01 EU per 1μg of the protein by the LAL method. Formulation Lyophilized from a 0.2 μm filtered concentrated solution in PBS. Reconstitution Centrifuge tubes before opening. Dissolve lyophilized protein with PBS. Recommend to aliquot the protein into smaller quantities when first used and avoid repeated freeze-thaw cycles.   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.   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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TWEAKR belongs to the TNF family of transmembrane proteins, and contains a cytoplasmic "death domain", which can activate a cell's apoptotic machinery. It is expressed in the spleen, thymus, peripheral blood lymphocytes, colon, and small intestine. Signal transduction by TWEAKR can be activated by either membrane-anchored or soluble TWEAK. Recombinant Human soluble TWEAKR is a 53 amino acid polypeptide (5.6 kDa) comprising the entire extracellular domain of the full-length TWEAKR protein.   Product Properties Synonyms TNFRSF12A, FGF-inducible 14, CD266 Accession Q9NP84  GeneID  51330 Source E.coli-derived Human TWEAK Receptor/TNFRSF12A protein,Glu28-Pro80. Molecular Weight Approximately 5.6 kDa Sequence EQAPGTAPCS RGSSWSADLD KCMDCASCRA RPHSDFCLGC AAAPPAPFRL LWP Physical Appearance Sterile Filtered White lyophilized (freeze-dried) powder. Purity > 95% by SDS-PAGE and HPLC analyses Biological Activity Fully biologically active when compared to standard. The ED50 as determined by inhibiting TWEAK-dependent proliferation of human umbilical vein endothelial cells (HUVEC) is less than 30ng/ml, corresponding to a specific activity of > 3.3 × 104 IU/mg, in the presence of 15 ng/mL of rHuTWEAK. 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 0.1-1.0mg/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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Thrombopoietin (TPO), is a key regulator of megakaryocytopoiesis and thrombopoiesis. The 353 amino acid (aa) human TPO precursor is cleaved to yield the 332 aa mature protein. Mature human TPO shares approximately 70% aa sequence homology with mouse and rat TPO. TPO and its receptor (c-Mpl) are the major regulators of megakaryocyte and platelet production and serve a critical and non-redundant role in hematopoietic stem cell (HSC) biology. TPO signals through the Jak-STAT, Ras-Raf-MAPK, and PI3K pathways, and promotes survival, proliferation, and polyploidization in megakaryocytes. The proto-oncogene c- also plays an important role in many of these same processes.   Product Properties Synonyms MGDF, MGDFC-mpl ligand, MKCSF, MK-CSF, ML, MPL ligand, MPLLG, THCYT1, THPO Accession NP_000451.1 Source HEK293 Cells-derived human TPO protein, Ser 22-Gly 353 with His tag at the N-terminus. Molecular Weight Approximately 37.6 kDa. As a result of glycosylation, TPO migrates as an approximately 78.2 kDa band in SDS-PAGE under reducing conditions. AA Sequence SPAPPACDL RVLSKLLRDS HVLHSRLSQC PEVHPLPTPV LLPAVDFSLG EWKTQMEETK AQDILGAVTL LLEGVMAARG QLGPTCLSSL LGQLSGQVRL LLGALQSLLG TQLPPQGRTT AHKDPNAIFL SFQHLLRGKV RFLMLVGGST LCVRRAPPTT AVPSRTSLVL TLNELPNRTS GLLETNFTAS ARTTGSGLLK WQQGFRAKIP GLLNQTSRSL DQIPGYLNRI HELLNGTRGL FPGPSRRTLG APDISSGTSD TGSLPPNLQP GYSPSPTHPP TGQYTLFPLP PTLPTPVVQL HPLLPDPSAP TPTPTSPLLN TSYTHSQNLS QEG Tag His Physical Appearance Sterile Filtered White lyophilized (freeze-dried) powder. Purity > 90 % by SDS-PAGE Biological Activity Measured in a cell proliferation assay using MO7e human megakaryocytic leukemic cells. The ED50 for this effect is typically 10-60 ng/mL. Endotoxin < 1.0 EU per 1μg of the protein by the LAL method. Formulation Lyophilized from a 0.2 μm filtered concentrated solution in PBS, pH 7.4. Reconstitution We recommend that this vial be briefly centrifuged prior to opening to bring the contents to the bottom. Reconstitute in sterile distilled water (400 μL) to a concentration of 0.25 mg/mL. Stock solutions should be apportioned into working aliquots and stored at ≤ -20°C. Stock solutions should be apportioned into working aliquots and stored at ≤ -20°C. Further dilutions should be made in appropriate buffered solutions.   Shipping and Storage The products are shipped with ice pack and can be stored at -20℃ for 1 year. 1 month, 2 to 8 °C under sterile conditions after reconstitution. 3 months, -20 °C under sterile conditions after reconstitution. Recommend to aliquot the protein into smaller quantities when first used and avoid repeated freeze-thaw cycles.   Cautions 1. Avoid repeated freeze-thaw cycles. 2. For your safety and health, please wear lab coats and disposable gloves for operation. 3. For research use only!

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TACI, a member of the TNF Receptor superfamily, is expressed in the small intestine, spleen, thymus, peripheral blood leukocytes, activated T cells, and resting B cells. TACI can bind to both APRIL and BAFF, stimulate the activation of transcription factors NF-κB and AP-1, and can mediate the calcineurin-dependent activation of NF-AT (nuclear-factor of activated T cells). TACI also plays a key role in the stimulation of B and T cell function. Soluble TACI inhibits APRIL-stimulated proliferation of primary B cells by blocking the binding of APRIL to the membrane-anchored TACI receptor. Recombinant Human TACI is a soluble 159 amino acid polypeptide (17.8 kDa) comprising the TNFR homologous, cysteine-rich extracellular domain of the TACI protein.   Product Properties Synonyms TACI,TNFRSF13B Accession O14836 GeneID 23495 Source E.coli-derived Human Endostatin protein,Met1-Val160,with an N-terminal Met. Molecular Weight Approximately 18.0 kDa. AA Sequence MSGLGRSRRG GRSRVDQEER FPQGLWTGVA MRSCPEEQYW DPLLGTCMSC KTICNHQSQR TCAAFCRSLS CRKEQGKFYD HLLRDCISCA SICGQHPKQC AYFCENKLRS PVNLPPELRR QRSGEVENNS DNSGRYQGLE HRGSEASPAL PGLKLSADQV Tag None Physical Appearance Sterile Filtered White lyophilized (freeze-dried) powder. Purity > 95 % by SDS-PAGE and HPLC analyses. Biological Activity Fully biologically active when compared to standard. The biological activity is determined by its ability to block human BAFF induced T2B cell survival using a concentration range of 1.0-3.0 µg/mL. Endotoxin < 1.0 EU per 1μg of the protein by the LAL method. Formulation Lyophilized from a 0.2 μm filtered concentrated solution in PBS, pH 7.4. Reconstitution We recommend that this vial be briefly centrifuged prior to opening to bring the contents to the bottom. Reconstitute in sterile distilled water or aqueous buffer containing 0.1% BSA to a concentration of 0.1-1.0mg/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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Trefoil factor 1 belongs to the trefoil factor family that consists of three members named TFF1, TFF2 and TFF3. They are characterized by having at least one copy of the trefoil motif, a 40-amino acid domain that contains three conserved disulfides.  Mature human TFF1 shares 67% amino acid sequence identity with mouse and rat TFF1. The TFFs are stable secretory proteins expressed highly in the gastrointestinal tract (gastric mucosa). TFF1 is an essential protein for normal differentiation of the antral and pyloric gastric mucosa and functions as a stabilizer of the mucous gel overlying the gastrointestinal mucosa that provides a physical barrier against various noxious agents. TFF1 is down-regulated during the progression from gastritis to gastric dysplasia to gastric cancer, although it is up-regulated in breast and prostate cancers. TFF1 inhibits the formation of calcium oxalate crystals, and its excretion in the urine is reduced in patients with kidney stones.   Product Properties Synonyms Breast Cancer Estrogen-inducible Protein, PNR-2, Polypeptide P1.A (hP1.A), Protein pS2 Accession P04155 GeneID 7031 Source E.coli-derived human TFF1 protein, Glu25-Phe84. Molecular Weight Approximately 13.2 kDa. AA Sequence EAQTETCTVA PRERQNCGFP GVTPSQCANK GCCFDDTVRG VPWCFYPNTI DVPPEEECEF Tag None Physical Appearance Sterile Filtered White lyophilized (freeze-dried) powder. Purity > 97 % by SDS-PAGE and HPLC analyses. Biological Activity The ED50 as determined by a chemotaxis bioassay using human MCF-7 cells is less than 10 μg/mL, corresponding to a specific activity of > 100 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, 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 0.1-1.0mg/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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Trefoil Factor 2 (TFF2), also known as spasmolytic peptide (SP), is one of three structurally related secreted proteins that contain trefoil domains. Trefoil factor 2 belongs to the trefoil factor family that consists of three members named TFF1, TFF2 and TFF3. They are characterized by having at least one copy of the trefoil motif, a 40-amino acid domain that contains three conserved disulfides. Mature human TFF2 shares 87% and 83% amino acid sequence identity with mouse and rat TFF2. The TFFs are stable secretory proteins expressed highly in the gastrointestinal tract (gastric mucosa). TFF2 can inhibit gastrointestinal motility and gastric acid secretion. Additionally, it functions as a structural component of gastric mucus, possibly by stabilizing glycoproteins in the mucus gel through interactions with carbohydrate side chains. Administration of TFF2 can reduce the severity of experimental colitis. TFF2 is down-regulated in many gastric cancers, although it is up-regulated in some breast cancers.   Product Properties Synonyms Spasmolysin, Spasmolytic polypeptide, SP Accession Q03403 GeneID 7032 Source E.coli-derived human TFF2 protein, Glu24-Tyr129. Molecular Weight Approximately 12.0 kDa. AA Sequence EKPSPCQCSR LSPHNRTNCG FPGITSDQCF DNGCCFDSSV TGVPWCFHPL PKQESDQCVM EVSDRRNCGY PGISPEECAS RKCCFSNFIF EVPWCFFPKS VEDCHY Tag None Physical Appearance Sterile Filtered White lyophilized (freeze-dried) powder. Purity > 97 % by SDS-PAGE and HPLC analyses. Biological Activity The ED50 as determined by a chemotaxis bioassay using human MCF-7 cells is less than 10 ng/mL, corresponding to a specific activity of > 1.0 × 105 IU/mg. Fully biologically active when compared to standard. Endotoxin < 1.0 EU per 1μg of the protein by the LAL method. Formulation Lyophilized from a 0.2 μm filtered concentrated solution in 20 mM PB, pH 7.4, 130 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℃. 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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Trefoil Factor 3 (TFF3), also known as Intestinal Trefoil Factor (ITF) and P1.B, is one of three structurally related secreted proteins that contain trefoil domains. Trefoil factor 2 belongs to the trefoil factor family that consists of three members named TFF1, TFF2 and TFF3. They are characterized by having at least one copy of the trefoil motif, a 40-amino acid domain that contains three conserved disulfides. TFF-3 is expressed by goblet cells and in the uterus, and has also been shown to express in certain cancers, including colorectal, hepatocellular, and in biliary tumors. It involves in the maintenance and repair of the intestinal mucosa, also promotes the mobility of epithelial cells in healing processes. TFF3 up-regulation is associated with and enhances tumor cell invasion and metastasis. It supports hypoxia-induced VEGF up-regulation in tumor cells and also promotes angiogenesis in non-tumor environments. Over-expression of TFF3 in type 2 diabetic mouse liver has been shown to improve glucose tolerance and insulin sensitivity.   Product Properties Synonyms Intestinal Trefoil Factor, hITF, Polypeptide P1.B, hP1.B Accession Q07654 GeneID 7033 Source E.coli-derived human TFF3 protein, Glu36-Phe94. Molecular Weight Approximately 13.2 kDa. AA Sequence EEYVGLSANQ CAVPAKDRVD CGYPHVTPKE CNNRGCCFDS RIPGVPWCFK PLQEAECTF Tag None Physical Appearance Sterile Filtered White lyophilized (freeze-dried) powder. Purity > 97 % by SDS-PAGE and HPLC analyses. Biological Activity The ED50 as determined by a chemotaxis bioassay using human MCF-7 cells is less than 10 μg/mL, corresponding to a specific activity of > 100 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 0.1-1.0mg/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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  Name Catalog No. Size Recombinant Human TSHR Protein-VLP C230754E 20 μg C230754S 100 μg C230754M 100 μg C230754L 1 mg   Product Properties   Synonyms TSHR;LGR3 Source HEK293 Cells AA sequence Accession #P16473: Met1 - Leu764 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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TNF-β is a potent mediator of inflammatory and immune responses. It belongs to the TNF family of ligands, and signals through TNFR1 and TNFR2. TNF-β is produced by activated T and B lymphocytes, and has similar activities to TNF-α. Like TNF-α, TNF-β is involved in the regulation of various biological processes, including cell proliferation, differentiation, apoptosis, lipid metabolism, coagulation, and neurotransmission. TNF-β forms heterotrimers with lymphotoxin-beta, which anchors TNF-β to the cell surface. TNF-β mediates the inflammatory, immunostimulatory, and antiviral response, involves in the formation of second lymphoid organs during development, has a role in apoptosis. TNF-β is produced by lymphocytes and cytotoxic for a variety of tumor cells in vitro.   Product Properties Synonyms TNFB, TNFSF1 Uniprot No. P01374 GeneID 4049 Source E.coli-derived Human Tumor Necrosis Factor-beta protein, Leu35-Leu205. Molecular Weight Approximately 18.7 kDa. AA Sequence LPGVGLTPSA AQTARQHPKM HLAHSTLKPA AHLIGDPSKQ NSLLWRANTD RAFLQDGFSL SNNSLLVPTS GIYFVYSQVV FSGKAYSPKA TSSPLYLAHE VQLFSSQYPF HVPLLSSQKM VYPGLQEPWL HSMYHGAAFQ LTQGDQLSTH TDGIPHLVLS PSTVFFGAFA L Tag None Physical Appearance Sterile Filtered White lyophilized (freeze-dried) powder. Purity > 96% as determined by SDS-PAGE. Biological Activity The ED50 as determined by a cytotoxicity assay using murine L929 cells is less than 5 pg/ml, corresponding to a specific activity of > 2.0 × 108 IU/mg in the presence of actinomycin D. Fully biologically active when compared to standard. Endotoxin < 0.1 EU per 1μg of the protein by the LAL method. Formulation Lyophilized from a 0.2 µm filtered concentrated solution in PBS, pH7.4, with 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 0.1-1.0mg/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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Uteroglobin, also called Clara cell secretory, phospholipid binding, 10 kDa or 16 kDa protein (CCSP, CCPBP, CC10 or CC16, respectively) is a small, non-glycosylated secreted protein of the secretoglobin superfamily, (designated 1A, member 1). Its name is derived from its very high expression in the pre-implantation uterus. It is produced by the non-ciliated, non-mucous secretory cells that predominate in lung bronchioles (Clara cells), and other non-ciliated epithelia that communicate with the external environment. Expression is induced by steroid hormones such as estrogen, and enhanced by the non-steroid hormone prolactin. Uteroglobin is found in blood, urine and other body fluids. Human Uteroglobin cDNA encodes a 21 amino acid (aa) signal sequence and a 70 aa mature protein. It shares 53 - 56% aa identity with mouse, rat, bovine, canine, equine or rabbit Uteroglobin, and is active in mice. The mature protein forms a disulfide-linked head-to-tail homodimer of 16 kDa. This homodimer is thought to form a binding pocket that binds hydrophobic ligands such as phospholipids, progesterone and retinols. Sequestering of prostaglandins and leukotrienes is anti-inflammatory, while sequestering of carcinogens such as polychlorinated bisphenols is anti-tumorigenic. Other immunoregulatory activities of Uteroglobin include cell migration inhibition (by binding the chemotaxis-related formyl peptide receptor FPR2 on dendritic cells), and the inhibition of T cell differentiation to a Th2 phenotype. A single nucleotide polymorphism of Uteroglobin, A38G, confers increased risk of asthma. Transglutaminase can crosslink Uteroglobin, either to itself or to other proteins such as the adhesion molecule fibronectin. Binding of fibronectin to Uteroglobin in the kidney is thought to protect against nephropathy, while binding of the lipocalin-1 receptor has been reported to suppress cancer cell motility and invasion.   Product Properties Synonyms CC10, CCSP, UGB Uniprot No. P11684 GeneID 7356 Source E.coli-derived Human Uteroglobin, Glu22-Asn91. Molecular Weight Approximately 15.8 kDa. AA Sequence EICPSFQRVI ETLLMDTPSS YEAAMELFSP DQDMREAGAQ LKKLVDTLPQ KPRESIIKLM EKIAQSSLCN Tag None Physical Appearance Sterile Filtered White lyophilized (freeze-dried) powder. Purity > 98% as determined by SDS-PAGE. Biological Activity The ED50 as determined by the ability of the immobilized protein to support the adhesion of the A549 human lung carcinoma cells is less than 5.0 μg/ml, corresponding to a specific activity of > 200 IU/mg. Fully biologically active when compared to standard. Endotoxin < 0.1 EU per 1μg of the protein by the LAL method. Formulation Lyophilized from a 0.2 µm filtered concentrated solution in PBS, 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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CXCL17 also named dendritic cell and monocyte chemokine-like protein (DMC) and VEGF co-regulated chemokine 1 (VCC-1), is a small cytokine belonging to the CXC chemokine family. CXCL17 was the last chemokine ligand to be described and is the 17th member of the CXC chemokine family. Its strategic expression in mucosal tissues suggests that it is involved in innate immunity and/or sterility of the mucosa. Mature human DMC shares 73%, 71% and 64% amino acid sequence identity with bovine, mouse and rat DMC, respectively. It may be a housekeeping chemokine regulating recruitment of nonactivated blood monocytes and immature dendritic cells into tissues and may play a role in the innate defense against infections. CXCL17 also has a role in angiogenesis of importance for tumour develop   Product Properties Synonyms C-X-C Motif Chemokine 17, CXCL17, Dcip1, DMC, UNQ473, VCC-1, VEGF Coregulated Chemokine 1, VEGF Co-Regulated Chemokine 1 Accession Q6UXB2 GeneID 284340 Source E.coli-derived human VCC-1/CXCL17 protein, Ser22-Leu119. Molecular Weight Approximately 11.5 kDa. AA Sequence SSLNPGVARG HRDRGQASRR WLQEGGQECE CKDWFLRAPR RKFMTVSGLP KKQCPCDHFK GNVKKTRHQR HHRKPNKHSR ACQQFLKQCQ LRSFALPL Tag None Physical Appearance Sterile Filtered White lyophilized (freeze-dried) powder. Purity >96% by SDS-PAGE and HPLC analyses. Biological Activity than 5.0 μg/ml, corresponding to a specific activity of > 200 IU/mg. Fully biologically active when compared to standard. Endotoxin < 0.1 EU per 1μg of the protein by the LAL method. Formulation Lyophilized from a 0.2 μm filtered concentrated solution in PBS, pH 7.4, with 3 % Trehalose. Reconstitution We recommend that this vial be briefly centrifuged prior to opening to bring the contents to the bottom. Reconstitute in sterile distilled water or aqueous buffer containing 0.1% BSA to a concentration of 0.1-1.0 mg/mL. Stock solutions should be apportioned into working aliquots and stored at ≤ -20℃. Further dilutions should be made in appropriate buffered solutions.   Shipping and Storage The products are shipped with ice pack and can be stored at -20℃ to -80℃ for 1 year. Recommend to aliquot the protein into smaller quantities when first used and avoid repeated freeze-thaw cycles.   Cautions 1. Avoid repeated freeze-thaw cycles. 2. For your safety and health, please wear lab coats and disposable gloves for operation. 3. For research use only!

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Vascular endothelial growth factor C (VEGF-C) and VEGF-D constitute a subfamily of the angiogenic VEGF angiogenic factors. VEGF-C is synthesized as a 58 kDa molecule that consists of a VEGF homolgy domain (VHD) flanked by N- and C-terminal propeptides. The proprotein undergoes covalent homodimerization and stepwise proteolytic processing to generate ligands with increasing affinity for VEGF R3/Flt-4. Fully processed VEGF-C containing just the 21 kDa VHD can additionally bind and activate VEGF R2/KDR/Flk-1. Fully processed human VEGF-C shares 98% amino acid sequence identity with mouse and rat VEGF-C. VEGF-C interactions with VEGF R3 are critical for lymphangiogenesis. VEGF-C and VEGF R3 are usually co-expressed at sites with lymphatic vessel sprouting, in the embryo, and in various pathological conditions. Over-expression of VEGF-C in tumor cells induces tumoral lymphatic hyperplasia, resulting in enhanced lymph flow and metastasis to regional lymph nodes. Product Properties Synonyms Flt4 ligand; Flt4-L; vascular endothelial growth factor C; Vascular endothelial growth factor-related protein; VEGFC; VEGF-C; VRPFLT4 ligand DHM Accession P49767 Source HEK293 Cells-derived human VEGF-C, Thr103-Arg227 with a C-terminal polyhistidine tag.  Molecular Weight The recombinant mature form of human VEGFC consists of 136 amino acids and has a predicted molecular mass of 15.5 kDa. In SDS-PAGE under reducing conditions, it migrates with an apparent molecular mass of 22.5 kDa due to glycosylation. Tag His Purity > 95% by SDS-PAGE. Biological Activity 1. Measured by its binding ability in a functional ELISA. Immobilized VEGF C-his at2μg/mL(100 μL/well) can bind VEGFR3 hFc, the EC50 of VEGFR3 hFc is 2-15 ng/mL. 2. Scatchard analysis showed the affinity constant (Kd) of recombinant human VEGF-C bound to recombinant human VEGFR3 was 1.4 nM. 3. Measured in a cell proliferation assay using human umbilical vein endothelial cells (HUVEC). The ED50 for this effect is typically 0.1-0.5 μg/mL. Endotoxin < 1.0 EU per 1μg of the protein by the LAL method. Concentration 0.95 mg/mL Formulation Lyophilized from a 0.2 μm filtered concentrated solution in PBS, pH 7.4. Normally 5% - 8% trehalose, mannitol and 0.01% Tween80 are added as protectants before lyophilization. Reconstitution We recommend that this vial be briefly centrifuged prior to opening to bring the contents to the bottom. Reconstitute in sterile distilled water to a concentration of 0.1-1.0 mg/mL. Stock solutions should be apportioned into working aliquots and stored at ≤ -20°C. Further dilutions should be made in  appropriate buffered solutions.   Shipping and Storage The products are shipped with ice pack and can be stored at -20 ℃ for 1 year. 1 month, 2 to 8 °C under sterile conditions after reconstitution. 3 months, -20 °C under sterile conditions after reconstitution. Recommend to aliquot the protein into smaller quantities when first used and avoid repeated freeze-thaw cycles. Cautions 1. Avoid repeated freeze-thaw cycles. 2. For your safety and health, please wear lab coats and disposable gloves for operation. 3. For research use only.

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Vascular endothelial growth factor D (VEGF-D), also known as c-fos-induced growth factor (FIGF), is a secreted glycoprotein of the VEGF/PDGF family. VEGFs regulate angiogenesis and lymphangiogenesis during development and tumor growth, and are  characterized by eight conserved cysteine residues that form a cystine knot structure. VEGF-C and VEGF-D, which share 23% amino acid (aa) sequence identity, are uniquely expressed as preproproteins that contain long N- and C-terminal propeptide extensions around the VEGF homology domain (VHD). Proteolytic processing of the 354 aa VEGF-D preproprotein creates a secreted proprotein. Further processing by extracellular serine proteases, such as plasmin or furin-like proprotein convertases, forms mature VEGF-D consisting of non- covalently linked 42 kDa homodimers of the 117 aa VHD. Mature human VEGF-D shares 94%, 95%, 99%, 97% and 93% aa identity with mouse, rat, equine, canine and bovine VEGF-D, respectively. It is expressed in adult lung, heart,  muscle, and small intestine, and is most abundantly expressed in fetal lungs and skin. Mouse and human VEGF-D are ligands for VEGF Receptor 3 (VEGF R3, also called Flt-4) that are active across species and show enhanced affinity when processed. Processed human VEGF-D is also a ligand for VEGF R2, also called Flk-1 or KDR. VEGF R3 is strongly expressed in lymphatic endothelial cells and is essential for regulation of the growth and differentiation of lymphatic endothelium. While VEGF-C is the critical ligand for VEGF R3 during embryonic lymphatic development, VEGF-D is most active in neonatal lymphatic maturation and bone growth. Both promote tumor lymphangiogenesis .  Product Properties Synonyms c-fos induced growth factor (vascular endothelial growth factor D); FIGF; vascular endothelial growth factor D; VEGFD; VEGF-D; VEGF-DVEGFDc-Fos-induced growth factor Accession O43915 Source HEK293 Cells-derived human VEGFD, Phe 93-Ser 201 with His tag at the C-terminu Molecular Weight The recombinant mature form of human VEGFD consists of 120 amino acids and has a predicted molecular mass of 13.6 kDa. In SDS-PAGE under reducing conditions, it migrates with an apparent molecular mass of 20-22 kDa due to glycosylation. Tag His Purity > 95% by SDS-PAGE. Biological Activity Measured in a cell proliferation assay using human umbilical vein endothelial cells (HUVEC). The ED50 for this effect is 0.3- 1.6 μg/mL Endotoxin < 1.0 EU per 1μg of the protein by the LAL method. Concentration 0.95 mg/mL Formulation Lyophilized from a 0.2 μm filtered concentrated solution in PBS, pH 7.4. Reconstitution We recommend that this vial be briefly centrifuged prior to opening to bring the contents to the bottom. Reconstitute in sterile distilled water or aqueous buffer containing 0.1% BSA to a concentration of 0.1-1.0 mg/mL. Stock solutions should be apportioned into working aliquots and stored at ≤ -20°C. Further dilutions should be made in appropriate buffered solutions.   Shipping and Storage The products are shipped with ice pack and can be stored at -20 ℃ for 1 year. 1 month, 2 to 8 °C under sterile conditions after reconstitution. 3 months, -20 °C under sterile conditions after reconstitution. Recommend to aliquot the protein into smaller quantities when first used and avoid repeated freeze-thaw cycles. Cautions 1. Avoid repeated freeze-thaw cycles. 2. For your safety and health, please wear lab coats and disposable gloves for operation. 3. For research use only

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Vascular endothelial growth factor 121 (VEGF121) is a protein that plays a crucial role in the growth and survival of blood vessels. It stimulates the formation of new blood vessels, a process known as angiogenesis, which is essential for normal development and tissue repair. VEGF121 has therapeutic applications for conditions such as ischemic heart disease and cancer.   Product Properties Synonyms VEGFA; vascular permeability factor; vasculotropin;V EGF-A Uniprot No. P15692-9 Source Recombinant Human VEGF121 Protein is expressed from HEK293 Cells with His tag at the C-terminal. It contains Ala27-Arg147. Molecular Weight The protein has a predicted MW of 16 kDa. And it migrates as 17-25 kDa under reducing (R) condition (SDS-PAGE) due to glycosylation. Purity > 95% as determined by SDS-PAGE. Endotoxin <0.1 EU per 1μg of the protein by the LAL method. Formulation Lyophilized from 0.22 μm filtered solution in PBS (pH 7.4). Reconstitution Centrifuge tubes before opening. Dissolve lyophilized protein with sterile PBS to ensure the concentration is greater than 100 ug/mL.   Shipping and Storage The product should be stored at -25~-15℃ for 1 year from date of receipt. 2-7 days, 2 ~8 °C under sterile conditions after reconstitution. 3 months, -25~-15℃ under sterile conditions after reconstitution. Recommend to aliquot the protein into smaller quantities when first used and avoid repeated freeze-thaw cycles.   Cautions 1. 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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VEGF 165, also known as Vascular Endothelial Growth Factor 165, is a protein that plays a critical role in angiogenesis, the process of forming new blood vessels from pre-existing ones. It belongs to the vascular endothelial growth factor family and is one of the most well-studied isoforms of VEGF.    Product Properties Synonyms   VEGF-165；VEGF; VEGFA; MVCD1;  VPF; RP1-261G23.1;   Uniprot No. P15692-4 Source Recombinant Human VEGF165 Protein is expressed from HEK293 without tag. It contains Ala27-Arg191 Molecular Weight The protein has a predicted MW of 19.2 kDa. Due to glycosylation, the protein migrates to 20-30 kDa based on Tris-Bis PAGE result. Biological Activity ED50 < 3 ng/ml, measured in a cell proliferation assay using HUVEC cells. Purity > 95% by SDS-PAGE and HPLC Endotoxin <1.0 EU per 1μg of the protein by the LAL method. Formulation Lyophilized from 0.22μm filtered solution in PBS (pH 7.4). Reconstitution It is recommended that this vial be briefly centrifuged prior to opening to bring the contents to the bottom. Reconstituting to a concentration more than 100 μg/ml is recommended. Dissolve the lyophilized protein in distilled water.   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 -6 months, -85~-65℃ 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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Vimentins are class-III intermediate filaments found in various non-epithelial cells, especially mesenchymal cells.Human Vimentin shares 97-98% aa identity with mouse, rat, ovine, bovine and canine Vimentin. Vimentin is involved in positioning autophagosomes, lysosomes and the Golgi complex within the cell. Vimentin helps maintain the lipid composition of cellular membranes, and caspase cleavage of Vimentin is a key event in apoptosis.   Product Properties Synonyms FLJ36605, VIM Accession P08670 GeneID 7431 Source E.coli-derived Human Vimentin, Ser2-Glu466. Molecular Weight Approximately 53.5 kDa. AA Sequence STRSVSSSSY RRMFGGPGTA SRPSSSRSYV TTSTRTYSLG SALRPSTSRS LYASSPGGVY ATRSSAVRLR SSVPGVRLLQ DSVDFSLADA INTEFKNTRT NEKVELQELN DRFANYIDKV RFLEQQNKIL LAELEQLKGQ GKSRLGDLYE EEMRELRRQV DQLTNDKARV EVERDNLAED IMRLREKLQE EMLQREEAEN TLQSFRQDVD NASLARLDLE RKVESLQEEI AFLKKLHEEE IQELQAQIQE QHVQIDVDVS KPDLTAALRD VRQQYESVAA KNLQEAEEWY KSKFADLSEA ANRNNDALRQ AKQESTEYRR QVQSLTCEVD ALKGTNESLE RQMREMEENF AVEAANYQDT IGRLQDEIQN MKEEMARHLR EYQDLLNVKM ALDIEIATYR KLLEGEESRI SLPLPNFSSL NLRETNLDSL PLVDTHSKRT LLIKTVETRD GQVINETSQH HDDLE Tag None Physical Appearance Sterile Filtered White lyophilized (freeze-dried) powder. Purity > 95% by SDS-PAGE and HPLC analyses. Endotoxin < 0.1 EU per 1μg of the protein by the LAL method. Formulation Lyophilized from a 0.2 µm filtered solution in 30 % Acetonitrile and 0.1 % TFA. Reconstitution We recommend that this vial be briefly centrifuged prior to opening to bring the contents to the bottom. Reconstitute in 4 mM HCl to a concentration of 0.1-1.0 mg/mL. Stock solutions should be apportioned into working aliquots and stored at ≤ -20℃. Further dilutions should be made in appropriate buffered solutions.   Shipping and Storage The products are shipped with ice pack and can be stored at -20℃ for 1 year. 1 month, 2 to 8 °C under sterile conditions after reconstitution. 3 months, -20 °C under sterile conditions after reconstitution. Recommend to aliquot the protein into smaller quantities when first used and avoid repeated freeze-thaw cycles.   Cautions 1. Avoid repeated freeze-thaw cycles. 2. For your safety and health, please wear lab coats and disposable gloves for operation. 3. For research use only.

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

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Human Wnt-3a protein is a signaling protein that belongs to the Wnt family. It plays a crucial role in various developmental processes, including cell fate determination, tissue patterning, and organogenesis. Wnt-3a protein is secreted by cells and acts as a ligand, binding to specific receptors on the surface of target cells to activate intracellular signaling pathways.   Product Properties Synonyms   Wingless-type MMTV Integration Site Family, Member 3a   Uniprot No.  P56704 Source HEK293 cells-derived human Wnt-3a protein, Ser19-Lys352, with C-terminal His tag. Molecular Weight The protein has a predicted MW of 39.4 kDa. And it migrates as 43 kDa under reducing (R) condition (SDS-PAGE) due to glycosylation. Purity > 50% as determined by SDS-PAGE. Endotoxin < 1 EU per 1μg of the protein by the LAL method. Formulation Liquid in PBS，the concentration is 0.015 mg/ml.   Shipping and Storage The product should be stored at -25~-15℃ 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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Wnt3a, one of Wnt family members, plays key roles in regulating pleiotropic cellular functions, including self-renewal, proliferation, differentiation, and motility. The Wnt family comprises 19 human proteins, including Wnt1, Wnt2, Wnt2b (Wnt13), Wnt3, Wnt3a, Wnt4, Wnt5a, Wnt5b, Wnt6, Wnt7a, Wnt7b, Wnt8a, Wnt8b, Wnt9a (Wnt14), Wnt9b (Wnt14b), Wnt10a, Wnt10b, Wnt11, and Wnt16. These genes encode secreted glycoproteins that are rich in cysteine. Wnts can combine with cell membrane receptors that play a critical role in autocrine regulation and/or participate in paracrine modification by binding to adjacent cell membrane receptors. The signal transduction pathway mediated by Wnt genes is called the Wnt signaling pathway. Accumulating evidence has suggested that Wnt3a promotes or suppresses tumor progression via the canonical Wnt signaling pathway depending on cancer type. In addition, the roles of Wnt3a signaling can be inhibited by multiple proteins or chemicals. Human Wnt-3a shares 96% aa identity with mouse mouse, bovine and canine Wnt-3a, and 89%, 86% and 84% aa identity with chicken, Xenopus and zebrafish Wnt-3a, respectively. It also shares 87% aa identity with Wnt3. During embryonic development, Wnt-3a is necessary for proper development of the hippocampus, anterior-posterior patterning, somite development, and tailbud formation. Wnt-3a also promotes self-renewal of  hematopoietic stem cells, neural stem cells, and embryonic stem cells. Product Properties Synonyms Wingless-type MMTV Integration Site Family, Member 3 Uniprot No. P56704 GeneID 8978 Source HEK293 cells-derived Human wnt-3a, Ser19-Lys352 Molecular Weight Approximately 63.3 kDa AA Sequence SY PIWWSLAVGP QYSSLGSQPI LCASIPGLVP KQLRFCRNYV EIMPSVAEGI KIGIQECQHQ  FRGRRWNCTT VHDSLAIFGP VLDKATRESA FVHAIASAGV AFAVTRSCAE GTAAICGCSS RHQGSPGKGW KWGGCSEDIE FGGMVSREFA DARENRPDAR SAMNRHNNEA GRQAIASHMH LKCKCHGLSG SCEVKTCWWS QPDFRAIGDF LKDKYDSASE MVVEKHRESR GWVETLRPRY TYFKVPTERD LVYYEASPNF CEPNPETGSF GTRDRTCNVS SHGIDGCDLL CCGRGHNARA ERRREKCRCV FHWCCYVSCQ ECTRVYDVHT CK Tag Fc Purity > 75% as determined by SDS-PAGE. Activity Measured by its binding ability in a ELISA method. Immobilized Human Wnt-3a at 10 μg/ml (100 μl/well) can bind bind Wnt-3a mouse monoclonal antibody. Endotoxin < 1.0 EU per 1μg of the protein by the LAL method. Formulation Lyophilized from a 0.2 µm filtered concentrated solution in PBS. Reconstitution We recommend that this vial be briefly centrifuged prior to opening to bring the contents to the bottom. Reconstitute in sterile distilled water or aqueous buffer containing 0.1% BSA to a concentration of 0.1-1.0 mg/mL. Stock solutions should be apportioned into working aliquots and stored at ≤ -20°C. Further dilutions should be made in appropriate buffered solutions. Transportation and Storage Methods Transport with ice packs. Store at -20°C to -80°C with a one-year shelf life. It is recommended to aliquot and freeze for the first use to avoid repeated freeze-thaw cycles. Cautions 1.Avoid repeated freezing and thawing. 2.For your safety and health, please wear a lab coat and use disposable gloves during operations. 3.This product is for research use only!

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  Name Catalog No. Size Recombinant Human XCR1 Protein-VLP C230755E 20 μg C230755S 100 μg C230755M 100 μg C230755L 1 mg   Product Properties   Synonyms XCR1 / CCXCR1 / GPR5 Source HEK293 Cells AA sequence Accession #P46094:Met1 - Tyr333 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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Activin A, a homodimer of activin βA subunits, is a member of the transforming growth factor (TGF)-β super-family. Activin A is produced by the placenta during human pregnancy, has been recognized as a multifunctional cytokine expressed in a wide range of tissues and cells with roles in regulation of wound repair, cell differentiation, apoptosis, embryogenesis, and inflammation. The 14 kDa mature human beta A chain shares 100% amino acid sequence identity with bovine, feline, mouse, porcine, and rat beta A. Activin A has been proposed in several pathological processes such as carcinogenesis and fibrosis, and this cytokine may also be involved in the pathogenesis of various inflammatory disorders such as inflammatory bowel disease and rheumatoid arthritis.   Product Properties Synonyms Activin A, activin AB alpha polypeptide, erythroid differentiation factor, Erythroid differentiation protein, FSH-releasing protein, inhibin beta A chain Accession P08476 GeneID 3624 Source Insect Cell-derived Human/Mouse/Rat Activin A/Inhibin beta A protein, Gly311 - Ser426. Molecular Weight Approximately 26 kDa. AA Sequence GLECDGKVNI CCKKQFFVSF KDIGWNDWII APSGYHANYC EGECPSHIAG TSGSS LSFHS TVINHYRMRG HSPFANLKSC CVPTKLRPMS MLYYDDGQNI IKKDIQNMIV EECGCS Tag None Physical Appearance Sterile Filtered White lyophilized (freeze-dried) powder. Purity > 95% by SDS-PAGE analyses. Biological Activity Test in processing. Endotoxin < 0.1 EU per 1μg of the protein by the LAL method. Formulation Lyophilized from a 0.2 μm filtered concentrated solution in 20 mM Tris-HCl, pH 8.0, 300 mM NaCl, with 5% Trehalose, 0.02% Tween-20. Reconstitution We recommend that this vial be briefly centrifuged prior to opening to bring the contents to the bottom. Reconstitute in sterile 10mM HCl to a concentration of 0.1-0.3 mg/mL. Stock solutions should be apportioned into working aliquots and stored at ≤ -20℃. Further dilutions should be made in appropriate buffered solutions.   Shipping and Storage The products are shipped with ice pack and can be stored at -20 ℃ for 1 year. 1 month, 2 to 8 °C under sterile conditions after reconstitution. 3 months, -20 °C under sterile conditions after reconstitution. Recommend to aliquot the protein into smaller quantities when first used and avoid repeated freeze-thaw cycles.   Cautions 1. Avoid repeated freeze-thaw cycles. 2. For your safety and health, please wear lab coats and disposable gloves for operation. 3. For research use only!

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Bone morphogenetic protein 2 (BMP-2) is a member of the BMP subgroup, where BMP2-7 belong to the TGF-β superfamily. It plays a leading role in embryonic dorsal-ventral patterning, organogenesis, limb bud formation, and bone formation and regeneration. Mature human BMP-2 has 100% amino acid sequence identity with mouse and rat BMP-2. It shares 85% sequence identity with human BMP-4 and less than 51% sequence identity with other BMPs. Normal bone formation is a carefully regulated long-term process involving the continuous expression of growth regulatory factors by osteoblasts during proliferation and eventual differentiation. This orderly sequence of osteoblast gene expression indicates a cascade effect, which BMP-2 can initiate and maintain. BMP-2 also promotes the maintenance and repair of colonic epithelium, inhibits the synthesis and release of neuronal dopamine, induces apoptosis in medulloblastoma cells, and is necessary for myocardial contractility.   Product Properties   Synonyms BDA2, BMP2, BMP-2, BMP-2A, SSFSC Source E.coli-derived human BMP-2, Gln283-Arg396, with an N-terminal Met Endotoxin < 0.1 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 10 mM sodium citrate, pH 3.5. Applications ELISA, Kinetics (BLI), Kinetics (SPR), Immunization Dilution Dilute in sterile distilled water.   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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Transforming growth factor-beta 1 (TGF-β1) is a major pluripotential cytokine with a pronounced immunosuppressive effect. TGF-β1 is a key regulator of diverse biological processes in many tissues and cell types, its can be tumorsuppressive through the activation of the Smadmediated signaling pathway.   Product Properties Synonyms CEDLAP, DPD1, latency-associated peptide, TGF beta, TGF beta1 Uniprot No. P01137 Source HEK293-derived Human TGF-β1, Ala279-Ser390. Molecular Weight The protein has a predicted 12.8 kDa Purity > 95% as determined by SDS-PAGE. Biological Activity Measured by the (CAGA)12—luciferase reporter assay. The EC50 for this effect is 1.092 ng/mL. Endotoxin < 0.01 EU per 1μg of the protein by the LAL method. Formulation Dissolved in sterile PBS buffer. Concentration 0.5 mg/ml   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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Activin A, a homodimer of activin βA subunits, is a member of the transforming growth factor (TGF)-β super-family. Activin A is produced by the placenta during human pregnancy, has been recognized as a multifunctional cytokine expressed in a wide range of tissues and cells with roles in regulation of wound repair, cell differentiation, apoptosis, embryogenesis, and inflammation.   Product Properties   Synonyms Activin A, activin AB alpha polypeptide, inhibin beta A chain Source Human/Murine/Rat Activin A Protein is expressed from CHO cell.It contains Gly311 - Ser426. Endotoxin < 0.01 EU per μg by the LAL method. Purity > 95% by SDS-PAGE analyses. Formulation Lyophilized from 0.2 μm filtered concentrated solution in 30% acetonitrile and 0.1 % TFA. Applications ELISA, Kinetics (BLI), Kinetics (SPR), Immunization Dilution Dilute with sterile 4 mM HCl to a concentration of 0.1-0.5 mg/ml.   Storage    The products are shipped with ice pack and can be stored at -25~-15℃ for 1 year. 1 month, 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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Mouse aFGF, encoded by the FGF1 gene, is a member of the fibroblast growth factor (FGF) family. Fibroblast growth factor was found in pituitary extracts in 1973 and then tested in a bioassay that caused fibroblasts to proliferate. After further fractionating the extract using acidic and basic pH, two different forms have isolated that named "acidic fibroblast growth factor" (FGF-1) and "basic fibroblast growth factor" (FGF-2). Murine aFGF shares 52 % amino acid sequence identity with bFGF. Murine aFGF shares 96 % amino acid sequence identity with human aFGF, so it exhibits considerable species crossreactivity between murine and human aFGF. In mammalian FGF receptor family has 4 members, FGFR1, FGFR2, FGFR3, and FGFR4, and 1, 2, 3 have 2 sub-types “b”, “c” . aFGF can bind and activate all 7 different FGFRs. Affinity between aFGF and its receptors can be increased by heparin or heparan sulfate proteoglycan. aFGF plays an important role in the regulation of cell survival, cell division, angiogenesis, cell differentiation and cell migration.   Product Properties Synonyms Fibroblast growth factor 1；FGF-1；Acidic fibroblast growth factor；HBGF-1 Accession P61148 GeneID 14164 Source E.coli-derived mouse Acidic Fibroblast Growth Factor protein, Phe16-Asp155 Molecular Weight Approximately 15.8 kDa. AA Sequence FNLPLGNYKK PKLLYCSNGG HFLRILPDGT VDGTRDRSDQ HIQLQLSAES AGEVYIKGTE TGQYLAMDTE GLLYGSQTPN EECLFLERLE ENHYNTYTSK KHAEKNWFVG LKKNGSCKRG PRTHYGQKAI LFLPLPVSSD Tag None Physical Appearance Sterile Filtered White lyophilized (freeze-dried) powder. Purity > 96 % by SDS-PAGE and HPLC analyses. Biological Activity Fully biologically active when compared to standard. The ED50 as determined by a cell proliferation assay using murine balb/c 3T3 cells is less than 0.2 ng/ml, corresponding to a specific activity of > 5.0 × 106 IU/mg in the presence of 10 μg/ml of heparin. Endotoxin < 1.0 EU per 1μg of the protein by the LAL method. Formulation Lyophilized from a 0.2 µm filtered concentrated solution in PBS, pH 7.4. Reconstitution We recommend that this vial be briefly centrifuged prior to opening to bring the contents to the bottom. Reconstitute in sterile distilled water or aqueous buffer containing 0.1 % BSA to a concentration of 0.1-1.0 mg/mL. Stock solutions should be apportioned into working aliquots and stored at ≤ -20 °C. Further dilutions should be made in appropriate buffered solutions.   Shipping and Storage The products are shipped with ice pack and can be stored at -20℃ to -80℃ for 1 year. Recommend to aliquot the protein into smaller quantities when first used and avoid repeated freeze-thaw cycles.   Cautions 1. Avoid repeated freeze-thaw cycles. 2. For your safety and health, please wear lab coats and disposable gloves for operation. 3. For research use only!

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

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

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

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

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

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

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

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