TAFI Protein | Cpb2 protein

TAFI, Human (Thrombin Activatable Fibrinolysis Inhibitor)

Cat. Num. AAA634885

• Gene Names: Cpb2; CPR; Cpu; TAFI; AI255929; 1110032P04Rik; 4930405E17Rik
• Purity: Purified; TAFI is prepared from fresh frozen human plasma by a modification of the method of Bajzar, et al. (10).
• Synonyms: TAFI; Human (Thrombin Activatable Fibrinolysis Inhibitor); Cpb2 protein

• Host: Human plasma
• Purity/Purification: Purified; TAFI is prepared from fresh frozen human plasma by a modification of the method of Bajzar, et al. (10).
• Form/Format: Supplied as a liquid in HEPES buffered saline.

• Extinction Coefficient: E1%1cm, 280nm=14.9 (calculated form cDNA)
• Isoelectric Point: 5.0
• Mode of Action: Basic carboxypeptidase, cleaves C-terminal lysine and arginine residues. Inhibition of fibrinolysis by removal of plasminogen binding sites on fibrin.
• Structure: Single chain glycoprotein. 92 a.a. N-terminal activation peptide, 309 a.a. catalytic domain, 1 mol zinc
• Percent Carbohydrate: 19%
• Post-translational Modifications: 4 N-linked glycosylation sites located at residues N22, N51, N63, and N86 of the activation peptide.
• Preparation and Storage: -70 degree C

Related Product Information for Cpb2 protein

Thrombin Activatable Fibrinolysis Inhibitor (TAFI, Plasma pro-carboxypeptidase B, carboxypeptidase U) is a single chain glycoprotein zymogen (Mr=60,000) synthesized in the liver and circulating at a plasma concentration of 50nM (1-4). Thrombin (plasmin, trypsin) cleavage of the zymogen releases a 92 amino acid N-terminal activation peptide containing 4 N-linked glycosylation sites (N22, N51, N63, N86) and the proposed plasminogen recognition site. The rate of thrombin catalyzed activation of TAFI is increased 1250 fold by formation of a ternary complex with thrombomodulin (5). The 309 amino acid C-terminal (Mr=35,783) catalytic domain (TAFIa, pCPB) displays the properties of a basic carboxypeptidase, hydrolyzing lysine and arginine from the C-terminal position of polypeptides. This portion of the molecule is homologous to tissue carboxypeptidase B and contains 7 conserved cystine residues (64,77,136,151,160,165,291), the active site Zn2+ coordination site (H67, E69, H196) and the basic C-terminal amino acid substrate binding pocket (D257, G244, S207).

TAFI is proposed to play a key role in the interaction between procoagulant, anticoagulant and fibrinolytic systems (5-9). Effective fibrinolysis results from the formation of a ternary complex between tPA, plasminogen and C-terminal lysine residues on fibrin. Plasminogen bound to fibrin is more effectively converted to plasmin, thereby localizing the lytic activity to the area of the clot. Plasmin degradation of fibrin generates additional C-terminal lysine residues thereby amplifying the system locally. The ability of TAFI to bind specifically to plasminogen and to cleave C-terminal lysines on fibrin (and cell surfaces) results in down-regulation of fibrinolysis by reducing the number of plasminogen and tPA binding sites on fibrin. The activation of TAFI by the thrombin/thrombomodulin complex couples both the phenomenon of coagulation induced inhibition of fibrinolysis and the profibrinolytic effect of activated protein C.

Product Categories/Family for Cpb2 protein

Molecular Biology; MB-Coagulation Factors

NCBI and Uniprot Product Information

• NCBI GI #: 7416967
• NCBI GeneID: 56373
• UniProt Accession #: Q9JHH6; Q5EBI3; Q9QZF0
• Molecular Weight: 60,000
• NCBI Official Full Name: thrombin-activatable fibrinolysis inhibitor
• NCBI Official Synonym Full Names: carboxypeptidase B2 (plasma)
• NCBI Official Symbol: Cpb2
• NCBI Official Synonym Symbols: CPR; Cpu; TAFI; AI255929; 1110032P04Rik; 4930405E17Rik
• NCBI Protein Information: carboxypeptidase B2; carboxypeptidase R; carboxypeptidase U; thrombin-activable fibrinolysis inhibitor; thrombin-activatable fibrinolysis inhibitor
• UniProt Protein Name: Carboxypeptidase B2
• Protein Family: Carboxypeptidase
• UniProt Gene Name: Cpb2
• UniProt Synonym Gene Names: Tafi; CPR; CPU; TAFI
• UniProt Entry Name: CBPB2_MOUSE

Uniprot Description

CPB2: 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. Belongs to the peptidase M14 family. 2 isoforms of the human protein are produced by alternative splicing.

Protein type: Secreted; Protease; Secreted, signal peptide; EC 3.4.17.20

Cellular Component: extracellular space; extracellular region

Molecular Function: peptidase activity; zinc ion binding; carboxypeptidase activity; metallopeptidase activity; hydrolase activity; metal ion binding; metallocarboxypeptidase activity

Biological Process: fibrinolysis; negative regulation of fibrinolysis; response to heat; hemostasis; proteolysis; blood coagulation