anti-Protein C antibody [HLW-C]
anti-Protein C antibody [HLW-C] for ELISA and Human
Cell Biology and Cellular Response antibody
|Product Description||Mouse Monoclonal antibody [HLW-C] recognizes Protein C|
|Target Name||Protein C|
|Immunogen||Purified human Protein C derived from human blood|
|Full Name||protein C (inactivator of coagulation factors Va and VIIIa)|
|Alternate Names||EC 184.108.40.206; Blood coagulation factor XIV; PC; THPH3; Vitamin K-dependent protein C; THPH4; APC; Autoprothrombin IIA; PROC1; Anticoagulant protein C|
|Application Note||* The dilutions indicate recommended starting dilutions and the optimal dilutions or concentrations should be determined by the scientist.|
|Calculated MW||52 kDa|
|Purification||Protein G affinity purified|
|Buffer||0.01M PBS (pH 7.2)|
|Storage instruction||For continuous use, store undiluted antibody at 2-8°C for up to a week. For long-term storage, aliquot and store at -20°C or below. Storage in frost free freezers is not recommended. Avoid repeated freeze/thaw cycles. Suggest spin the vial prior to opening. The antibody solution should be gently mixed before use.|
|Note||For laboratory research only, not for drug, diagnostic or other use.|
|Gene Full Name||protein C (inactivator of coagulation factors Va and VIIIa)|
|Background||Protein C is a vitamin K dependant glycoprotein in blood. Activated Protein C (APC) functions as an anti-coagulation factor in blood by proteolyzing pro-coagulation factors including Factor V and Factor VIII. When bound with endothelial protein C receptor (EPCR) on vascular endothelial cells, APC acts on protease activated receptor I (PAR-1) to up-regulate the expression of genes involved with anti-inflammatory and anti- apoptotic pathways, thus it also possesses a cell protective function. Protein C is activated by binding with thrombin. The activation is enhanced by thrombomodulin and EPCR.|
|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. [UniProt]|
|Research Area||Cell Biology and Cellular Response antibody|
|PTM||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.