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CAS Number: 60202-16-6
MDL number: MFCD00165567
| Related Categories | Application Index, Bioactive Small Molecules, Cell Biology, Coagulation Proteins and Reagents, Enzymes, Inhibitors, and Substrates, |
| description | Zymogen |
| form | lyophilized powder |
| shipped in | dry ice |
| storage temp. | −20°C |
| Gene Information | Research your gene in Your Favorite Gene powered by Ingenuity human ... F5(2153), F8(2157), PROC(5624) |
Protein C is purified from a concentrate of pooled normal human plasma using an Anti-Protein C-Agarose column (Product No. A 0435) followed by gel filtration.
1 vial = 100 μg protein.
Reconstitute with 1 ml deionized water.
Purified Protein C forms a closely spaced doublet at a molecular weight of 62 kDa using SDS gel electrophoresis under non-reduced conditions.
Lyophilized from 20 mM Tris buffered saline, pH 7.4, containing 0.02% sodium azide
Protein C is a plasma, vitamin K-dependent zymogen of a serine protease that can inhibit blood coagulation by inhibiting thrombin formation, selectively inactivating factors Va and VIIIa. The Protein C anticoagulant pathway is triggered when thrombin binds to the endothelial cell proteoglycan, thrombomodulin. This complex, which cannot clot blood, is a potent activator of the protein C zymogen. Activation involves the release of a dodecapeptide from the N-terminal domain of the heavy chain. The activated Protein C (APC) then binds to protein S on cell surfaces and inactivates the coagulation factors Va and VIIIa by proteolysis. APC has also been shown to bind to receptors on the endothelium of large blood vessels.
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Activated, lyophilized powder, ≥90% (SDS-PAGE)
| Hazard Codes | B |
| WGK Germany | 3 |
Despite their complexity, blood and plasma are abundant biological resources for the discovery of drug targets and biomarkers for human disease. It is estimated that plasma may contain as many as 40,...
BioFiles 2006, 1.5, 2.
Keywords: Gas chromatography
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Heeb, M.J., et al., Importance of individual activated protein C cleavage site regions in coagulation factor V for factor Va inactivation and for factor Xa activation. Eur. J. Biochem. 260, 64-75, (1999)
Esmon, C.T., et al., Regulation and functions of the protein C anticoagulant pathway. Haematologica 84, 363-368, (1999)
Laszik, Z., et al., Human protein C receptor is present primarily on endothelium of large blood vessels: implications for the control of the protein C pathway. Circulation 96, 3633-3640, (1997)
Merck 14,7884
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