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生化／生理作用
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.[1] Experiments in TAFI-deficient mice point to a regulatory role on complement C5a.[2]
單位定義
One unit will hydrolyze 1 micromole of Hippuryl-L-Arginine per minute at pH 7.4 at 25 °C.
外觀
Solution containing 20 mM Hepes and 150 mM Sodium chloride. pH 7.4
儲存類別代碼
10 - Combustible liquids
水污染物質分類（WGK）
WGK 1
閃點（°F）
Not applicable
閃點（°C）
Not applicable
個人防護裝備
Eyeshields, Gloves, multi-purpose combination respirator cartridge (US)
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
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
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