Protein C Protein | PROC protein

Protein C, Human

Cat. Num. AAA634709

• Gene Names: PROC; PC; APC; PROC1; THPH3; THPH4
• Purity: Affinity Purified; Human protein C is prepared from fresh frozen citrated human 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
• Synonyms: Protein C; Human; PROC protein

• Host: Human plasma
• Purity/Purification: Affinity Purified; Human protein C is prepared from fresh frozen citrated human 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
• Form/Format: Supplied as a liquid in 50% glycerol/H2O.

• Extinction Coefficient: E1%1cm, 280nm=14.5 (7)
• Isoelectric Point: 4.4-4.8 (8)
• Mode of Action: Zymogen; precursor to the serine protease activated protein C (APC)
• Structure: Two chains, Mr=41,000 and 21,000, disulfide linked, NH2-terminal gla domain two EGF domains; ; Percent Carbohydrate: 23%(7)
• Post-translational Modifications: Nine gla residues, one b-hydroxyaspartate
• Preparation and Storage: May be stored at 4 degree C for short-term only. For long-term storage, store at -20 degree C. Aliquots are stable for at least 6 months at -20 degree C. For maximum recovery of product, centrifuge the original vial after thawing and prior to removing the cap. Further dilutions can be made in assay buffer.

Related Product Information for PROC protein

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 (Mr=3000) from the COOH-terminal end of the heavy chain, yielding an altered form referred to as b-protein C. No functional distinction between a- and b-protein C has been observed. A single cleavage at Arg-12 (Arg-14 in bovine) of the heavy chain of human protein C converts the zymogen into the serine protease, activated protein C. This cleavage is catalyzed by a complex between a-thrombin and the endothelial cell surface protein thrombomodulin. In contrast to the other vitamin K dependent coagulation factors, activated protein C functions as an anticoagulant by catalyzing the proteolytic inactivation of factors Va and VIIIa. APC also contributes to the fibrinolytic response by complex formation with plasminogen activator inhibitors.

Product Categories/Family for PROC protein

Molecular Biology; MB-Coagulation Factors

NCBI and Uniprot Product Information

• NCBI GI #: 265668
• NCBI GeneID: 5624
• UniProt Accession #: P04070; Q15189; Q15190; Q16001; Q53S74; Q9UC55
• Molecular Weight: 62,000
• NCBI Official Full Name: protein C
• NCBI Official Synonym Full Names: protein C (inactivator of coagulation factors Va and VIIIa)
• NCBI Official Symbol: PROC
• NCBI Official Synonym Symbols: PC; APC; PROC1; THPH3; THPH4
• NCBI Protein Information: vitamin K-dependent protein C; autoprothrombin IIA; anticoagulant protein C; blood coagulation factor XIV
• UniProt Protein Name: Vitamin K-dependent protein C
• Protein Family: Protein
• UniProt Gene Name: PROC
• UniProt Entry Name: PROC_HUMAN

NCBI Description

This gene encodes a vitamin K-dependent plasma glycoprotein. The encoded protein is cleaved to its activated form by the thrombin-thrombomodulin complex. This activated form contains a serine protease domain and functions in degradation of the activated forms of coagulation factors V and VIII. Mutations in this gene have been associated with thrombophilia due to protein C deficiency, neonatal purpura fulminans, and recurrent venous thrombosis.[provided by RefSeq, Dec 2009]

Uniprot Description

PROC: 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. Defects in PROC are the cause of thrombophilia due to protein C deficiency, autosomal dominant (THPH3). A hemostatic disorder characterized by impaired regulation of blood coagulation and a tendency to recurrent venous thrombosis. However, many adults with heterozygous disease may be asymptomatic. Individuals with decreased amounts of protein C are classically referred to as having type I protein C deficiency and those with normal amounts of a functionally defective protein as having type II deficiency. Defects in PROC are the cause of thrombophilia due to protein C deficiency, autosomal recessive (THPH4). A hemostatic disorder characterized by impaired regulation of blood coagulation and a tendency to recurrent venous thrombosis. It results in a thrombotic condition that can manifest as a severe neonatal disorder or as a milder disorder with late-onset thrombophilia. The severe form leads to neonatal death through massive neonatal venous thrombosis. Often associated with ecchymotic skin lesions which can turn necrotic called purpura fulminans, this disorder is very rare. Belongs to the peptidase S1 family.

Protein type: Apoptosis; EC 3.4.21.69; Protease

Chromosomal Location of Human Ortholog: 2q13-q14

Cellular Component: Golgi lumen; endoplasmic reticulum lumen; extracellular region

Molecular Function: protein binding; serine-type endopeptidase activity; calcium ion binding

Biological Process: cellular protein metabolic process; negative regulation of blood coagulation; post-translational protein modification; blood coagulation; proteolysis; peptidyl-glutamic acid carboxylation; leukocyte migration; negative regulation of apoptosis

Disease: Thrombophilia Due To Protein C Deficiency, Autosomal Recessive; Thrombophilia Due To Protein C Deficiency, Autosomal Dominant