P0059
Pro-carboxypeptidase B human
≥2.0 units/mg protein
Synonym(s):
Thrombin Activatable Fibrinolysis Inhibitor (TAFI)
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About This Item
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Quality Level
specific activity
≥2.0 units/mg protein
mol wt
60 kDa
UniProt accession no.
shipped in
dry ice
storage temp.
−70°C
Gene Information
human ... CPB1(1360)
Biochem/physiol Actions
TAFI is supplied in its 60 kDa zymogen form. The N-terminal of TAFI contains four N-linked glycans and a plasminogen recognition sequence. Hydrolysis of the activation peptide by thrombin releases a 36-kDa active proteolytic domain homologous to tissue carboxypeptidase B. Complexation with thrombomodulin increases thrombin activation of TAFI 1250 fold. TAFI exerts it′s inhibition of fibrinolytic activity by binding to plasminogen and by cleaving C-terminal lysine residues of fibrin resulting in the reduction of plasmin and tPA binding sites on fibrin. Experiments in TAFI-deficient mice point to a regulatory role on complement C5a.
Unit Definition
One unit will hydrolyze 1 micromole of Hippuryl-L-Arginine per minute at pH 7.4 at 25 °C.
Physical form
Solution containing 20 mM Hepes and 150 mM Sodium chloride. pH 7.4
Storage Class
10 - Combustible liquids
wgk_germany
WGK 1
flash_point_f
Not applicable
flash_point_c
Not applicable
ppe
Eyeshields, Gloves, multi-purpose combination respirator cartridge (US)
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Toshihiko Nishimura et al.
Blood, 109(5), 1992-1997 (2006-11-16)
Plasma procarboxypeptidase B (proCPB) is activated by the endothelial thrombin-thrombomodulin [corrected] complex. Activated proCPB [corrected] (CPB) functions as a fibrinolysis inhibitor, but it may play a broader role by inactivating inflammatory mediators. To test this hypothesis, C5a-induced alveolitis was studied
B N Bouma et al.
Journal of thrombosis and haemostasis : JTH, 1(7), 1566-1574 (2003-07-23)
Recently, a new inhibitor of fibrinolysis was described, which downregulated fibrinolysis after it was activated by thrombin, and was therefore named TAFI (thrombin-activatable fibrinolysis inhibitor; EC 3.4.17.20). TAFI turned out to be identical to the previously described proteins, procarboxypeptidase U
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