CPB2
CPB2 (carboxypeptidase B2, also known as CPU, PCPB and TAFI) is a secreted M14-family carboxypeptidase that removes C-terminal arginine or lysine residues from peptides in the circulation. Through this activity it dampens fibrinolysis and modulates kinins and anaphylatoxins. Browse Assay Genie's current range of CPB2 research reagents below, or read on for the biology behind the target.
CPB2 is a carboxypeptidase that cleaves C-terminal arginine or lysine residues from biologically active peptides such as kinins and anaphylatoxins in the circulation, thereby regulating their activities. It also down-regulates fibrinolysis by removing C-terminal lysine residues from fibrin that has already been partially degraded by plasmin. Removing these residues limits further plasmin generation on the clot, which is why the enzyme is of interest in haemostasis research.
Carboxypeptidases hydrolyse C-terminal peptide bonds, and the family includes metallo-, serine and cysteine enzymes. By substrate specificity they are classed as carboxypeptidase A, which cleaves aliphatic residues, or carboxypeptidase B, which cleaves basic residues. The CPB2 protein acts on carboxypeptidase B substrates and belongs to the peptidase M14 family, the HGNC gene group of M14 carboxypeptidases. It is a secreted protein, and the CPB2 gene has mouse and rat orthologs, both named Cpb2.
The protein is activated by trypsin. After thrombin activation, the mature protein downregulates fibrinolysis. Polymorphisms have been described in the gene and its promoter region, and alternate splicing gives multiple transcript variants. The enzyme has also been called thrombin-activatable fibrinolysis inhibitor (TAFI), plasma carboxypeptidase B (PCPB) and carboxypeptidase U (CPU), and earlier HGNC names were carboxypeptidase B2 (plasma, carboxypeptidase U) and carboxypeptidase B2 (plasma). Researchers studying the CPB2 gene or the CPB2 protein often compare it with the related pancreatic enzyme CPB1.
CPB2 removes C-terminal lysines from partially degraded fibrin, so it is a key enzyme for studying how fibrinolysis is downregulated.
After thrombin activation the mature protein downregulates fibrinolysis, linking CPB2 to the interface between clotting and clot breakdown.
CPB2 cleaves C-terminal basic residues from kinins and anaphylatoxins in the circulation, regulating their activity.
Polymorphisms in the gene and its promoter region make CPB2 relevant to studies of variation and transcript diversity.
CPB2 cleaves C-terminal arginine or lysine residues from peptides such as kinins and anaphylatoxins in the circulation, regulating their activity. It also down-regulates fibrinolysis by removing C-terminal lysines from fibrin already partially degraded by plasmin.
CPB2 is also known as CPU, PCPB and TAFI. Earlier HGNC names were carboxypeptidase B2 (plasma, carboxypeptidase U) and carboxypeptidase B2 (plasma). The gene produces multiple transcript variants through alternate splicing, so check the datasheet of any product for its validated reactivity.
Yes. Mouse and rat both carry an ortholog named Cpb2. The human protein is a secreted M14-family carboxypeptidase, and rodent models are therefore a common route to studying its role in fibrinolysis. Check the datasheet of any product for its validated reactivity.
Related carboxypeptidases with products at Assay Genie.
Gene and protein annotations from HGNC, NCBI Gene and UniProt Q96IY4; product specifications from Assay Genie datasheets.