| Description | Native carboxypeptidase B catalyzes the release of C-terminal from basic amino acids, arginine, lysine, or ornithine from polypeptides. Inhibited by EDTA and other Zn2+ chelators.Native carboxypeptidase B catalyzes the release of C-terminal from basic amino acids, arginine, lysine, or ornithine fromNative carboxypeptidase B catalyzes the release of C-terminal from basic amino acids, arginine, lysine, or ornithine from polypeptides. Inhibited by EDTA and other Zn2+ chelators.Native carboxypeptidase B catalyzes the release of C-terminal from basic amino acids, arginine, lysine, or ornithine from polypeptides. Inhibited by EDTA and other Zn2+ chelators. Has an optimal pH of 7.0-9.0 and a pI of 6.0... Read More | Human CCL18 is encoded by the CCL18 gene located on the chromosome 17. As also named MIP-4, it shares 61 % sequence identity to human MIP-1α. CCL18 is mainly expressed by lung and some lymphoid tissues like lymph nodes express CCL18 at low level. It is chemotactic for both activated (CD3+) T Human CCL18 is encoded by the CCL18 gene located on the chromosome 17. As also named MIP-4, it shares 61 % sequence identity to human MIP-1α. CCL18 is mainly expressed by lung and some lymphoid tissues like lymph nodes express CCL18 at low level. It is chemotactic for both activated (CD3+) T cells and nonactivated (CD14-) lymphocytes, but not for monocytes or granulocytes. Involved in B-cell migration into B-cell follicles in lymph nodes. CCL18 plays a role in both humoral and cell mediated immunity responses. Recombinant Human MIP-4/CCL18 is a 7.9kDa protein containing 69 amino acid residues, including the four highly conserved cysteine residues present in CC chemokines.Purity>96% SDS-PAGEFunctionChemotactic factor that attracts lymphocytes but not monocytes or granulocytes. May be involved in B-cell migration into B-cell follicles in lymph nodes. Attracts naive T-lymphocytes toward dendritic cells and activated macrophages in lymph nodes, has chemotactic activity for naive T-cells, CD4+ and CD8+ T-cells and thus may play a role in both humoral and cell-mediated immunity responses... Read More | Purity>95% by SDS-PAGE and HPLC analyses.FunctionLigand for IL17RA and IL17RC (PubMed:17911633). The heterodimer formed by IL17A and IL17F is a ligand for the heterodimeric complex formed by IL17RA and IL17RC (PubMed:18684971). Involved in stimulating the production of other cytokines such as IL6Purity>95% by SDS-PAGE and HPLC analyses.FunctionLigand for IL17RA and IL17RC (PubMed:17911633). The heterodimer formed by IL17A and IL17F is a ligand for the heterodimeric complex formed by IL17RA and IL17RC (PubMed:18684971). Involved in stimulating the production of other cytokines such as IL6, IL8 and CSF2, and in regulation of cartilage matrix turnover (PubMed:11591732, PubMed:11591768, PubMed:11574464). Also involved in stimulating the proliferation of peripheral blood mononuclear cells and T-cells and in inhibition of angiogenesis (PubMed:11591732). Plays a role in the induction of neutrophilia in the lungs and in the exacerbation of antigen-induced pulmonary allergic inflammation... Read More | Inquire | Trypsin is a member of the serine protease family. Trypsin cleaves peptides on the C-terminal end of lysine and arginine amino acid residues. The pH optimum of trypsin is pH 7 - 10. The enzyme is inhibited by serine protease inhibitors, e.g. PMSF, and by metal chelating agents, e.g., EDTA. Trypsin is a member of the serine protease family. Trypsin cleaves peptides on the C-terminal end of lysine and arginine amino acid residues. The pH optimum of trypsin is pH 7 - 10. The enzyme is inhibited by serine protease inhibitors, e.g. PMSF, and by metal chelating agents, e.g., EDTA. Recombinant Human Trypsin is a genetically engineered protein expressed in E.coli and purified by high pressure liquid chromatography. There are no contaminating enzyme activities such as carboxypeptidase A and chymotrypsin. No protease inhibitors such as PMSF are contained in the preparation.Animal origin free:The use of recombinant Human Trypsin eliminates the risk of virus presence, and of any other potential adventitious agents found in animal pancreas-derived trypsin. Recombinant human trypsin:The amino acid sequence is the same as the Human Trypsin 2.Stable:A sterile recombinant human trypsin lyophilized eliminates the contamination risks and decreases the chance of activity loss in the process of transport and storage.High purity:(1) Recombinant human trypsin provides increased specificity and eliminates contaminating activities found in lower purity enzymes.(2) No other contaminating proteases such as chymotrypsin or carboxypeptidase A... Read More |