Recombinant Human Carboxypeptidase B2 (CPB2)

Uniprot Id

Q96IY4

Target Species

Human

Target Name

CPB2

Target Full Name

Carboxypeptidase B2

Target Function

Cleaves C-terminal arginine or lysine residues from biologically active peptides such as kinins or anaphylatoxins in the circulation thereby regulating their activities. Down-regulates fibrinolysis by removing C-terminal lysine residues from fibrin that has already been partially degraded by plasmin.

Target Subcellular Location

Secreted.

Target Protein Families

Peptidase M14 family

Target Tissue Specificity

Plasma; synthesized in the liver.

Target Synonyms

CPB2; Carboxypeptidase B2; EC 3.4.17.20; Carboxypeptidase U; CPU; Plasma carboxypeptidase B; pCPB; Thrombin-activable fibrinolysis inhibitor; TAFI

Target Background

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. Alternate splicing results in multiple transcript variants.