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| Product Name | Protein C, Bovine |
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| Description | Purity ≥95% by SDS-PAGE. Bovine protein C is prepared from fresh frozen citrated plasma using a combination of immunoaffinity chromatography (5), and conventional techniques (4,9). Purity is determined by SDS-PAGE analysis and activity is measured using a chromogenic substrate based assay. The vitamin K-dependent zymogen, protein C, is synthesized in the liver as a single chain polypeptide and is subsequently converted to a disulfide linked heterodimer, by removal of a dipeptide (Lys-146 and Arg-147) from the precursor molecule (1,2). Trace quantities of the single chain form have been observed in plasma. The light chain, which is responsible for the calcium dependent binding of protein C to phospholipid vesicles, contains 11 g-carboxyglutamic acid (gla) residues, 1 b-hydroxyaspartic acid residue, and 2 epidermal growth factor (EGF) homology domains. The serine protease catalytic triad is located in the heavy chain. Human protein C is susceptible to proteolytic cleavage of a peptide (M |
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| Size | 100ug |
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| Concentration | n/a |
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| Applications | n/a |
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| Other Names | n/a |
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| Gene, Accession, CAS # | n/a |
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| Catalog # | P9079 |
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| Order / More Info | Protein C, Bovine from UNITED STATES BIOLOGICAL |
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| Product Specific References | n/a |
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