Recombinant Human Protein C is a Human Full Length protein, in the 1 to 461 aa range, expressed in Wheat germ, suitable for ELISA, WB.
View Alternative Names
Vitamin K-dependent protein C, Anticoagulant protein C, Autoprothrombin IIA, Blood coagulation factor XIV, PROC
- SDS-PAGE
Unknown
SDS-PAGE - Recombinant Human Protein C (AB159228)
ab159228 on a 12.5% SDS-PAGE stained with Coomassie Blue.
Reactivity data
Sequence info
Properties and storage information
Shipped at conditions
Appropriate short-term storage conditions
Appropriate long-term storage conditions
Aliquoting information
Storage information
Supplementary information
This supplementary information is collated from multiple sources and compiled automatically.
Biological function summary
Protein C serves as an important regulator in the coagulation pathway. Upon activation it joins with a cofactor known as Protein S to form the activated Protein C complex which inactivates clotting factors Va and VIIIa. This inactivation leads to a reduction in thrombin formation thereby preventing excessive blood clotting. The activated C complex works efficiently on phospholipid surfaces such as those found on cellular membranes.
Pathways
Protein C activation is an important step in the anticoagulant pathway and works to balance the procoagulant actions of other factors. Protein C functions in tandem with proteins such as thrombin which transforms it into its active form when bound to thrombomodulin on the endothelial cell surface. The activated Protein C pathway ensures proper blood flow by preventing unchecked clot propagation and is intricately tied with pathways involving thrombin and factors Va and VIIIa.
Specifications
Form
Liquid
General info
Function
Protein C is a vitamin K-dependent serine protease that regulates blood coagulation by inactivating factors Va and VIIIa in the presence of calcium ions and phospholipids (PubMed : 25618265). Exerts a protective effect on the endothelial cell barrier function (PubMed : 25651845).
Sequence similarities
Belongs to the peptidase S1 family.
Post-translational modifications
The vitamin K-dependent, enzymatic carboxylation of some Glu residues allows the modified protein to bind calcium.. N- and O-glycosylated. Partial (70%) N-glycosylation of Asn-371 with an atypical N-X-C site produces a higher molecular weight form referred to as alpha. The lower molecular weight form, not N-glycosylated at Asn-371, is beta. O-glycosylated with core 1 or possibly core 8 glycans.. The iron and 2-oxoglutarate dependent 3-hydroxylation of aspartate and asparagine is (R) stereospecific within EGF domains.. May be phosphorylated on a Ser or Thr in a region (AA 25-30) of the propeptide.
Target data
Product promise
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