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). CPB2 is activated by trypsin and acts on carboxypeptidase B substrates. After thrombin activation, the mature protein downregulates fibrinolysis. Polymorphisms have been described for its gene and its promoter region.
For Research Use Only. Not for use in diagnostic procedures. Not for resale without express authorization.
Protein Aliases: carboxypeptidase B-like protein; Carboxypeptidase B2; carboxypeptidase B2 (plasma); carboxypeptidase B2 (plasma, carboxypeptidase U); Carboxypeptidase R; Carboxypeptidase U; CPR; CPU; pCPB; Plasma carboxypeptidase B; TAFI; Thrombin-activable fibrinolysis inhibitor; thrombin-activatable fibrinolysis inhibitor
Gene Aliases: 1110032P04Rik; 4930405E17Rik; AI255929; CPB2; CPR; CPU; PCPB; TAFI