Description
Product Characteristics:
This protein belongs to a family of Zn-containing metallocarboxypeptidases specific to C-terminal lysine and arginine residues. It circulates in plasma as a zymogen with molecular weight of 55 kDa (401 amino acid residues, pI 5.0). Being activated by thrombin-thrombomodulin complex during blood coagulation, it exerts carboxypeptidase activity. Activated carboxypeptidase B2 removes C-terminal lysine residues from fibrin, which is necessary for plasminogen binding to fibrin. This prevents plasminogen from activation into plasmin and retards the lysis of a fibrin clot. The concentration in plasma of healthy people is 5-10 µg/mL. High plasma levels were found in patients with stable angina pectoris and angiographically verified coronary artery disease. Elevated concentration in blood is considered as a risk factor for venous thrombosis. A deficiency might contribute to the severity of bleeding disorders in hemophilias A and B, and decreased levels are found in chronic liver disease.
Subcellular location: Secreted
Synonyms: Carboxypeptidase B like protein, Carboxypeptidase U, CarboxypeptidaseB2, Carboxypeptidase B2, CarboxypeptidaseU, CP B2, CPB 2, CPB2, CPU, PCPB, Plasma carboxypeptidase B, Plasma carboxypeptidase B2, Procarboxypeptidase B, Procarboxypeptidase R, Procarboxypeptidase U, TAFI, Thrombin activable fibrinolysis inhibitor, Thrombin activatable fibrinolysis inhibitor.
Target Information: Carboxypeptidases are enzymes that hydrolyze C-terminal peptide bonds. The carboxypeptidase family includes metallo-, serine, and cysteine carboxypeptidases. According to their substrate specificity, these enzymes are referred to as carboxypeptidase A (cleaving aliphatic residues) or carboxypeptidase B (cleaving basic amino residues). The protein encoded by this gene is activated by trypsin and acts on carboxypeptidase B substrates. After thrombin activation, the mature protein downregulates fibrinolysis. Polymorphisms have been described for this gene and its promoter region. [provided by RefSeq, Apr 2012]