CPB2, also known as Thrombin-Activatable Fibrinolysis Inhibitor (TAFI), is a metalloprotease synthesized in the liver and secreted into plasma. It regulates fibrinolysis by removing C-terminal lysine residues from fibrin, thereby reducing plasminogen activation . Structurally, CPB2 comprises 423 amino acids (48 kDa) and requires proteolytic activation by thrombin or plasmin .
Catalytic domain: Responsible for enzymatic cleavage of basic residues (lysine/arginine).
Pro-domain: Maintains zymogen inactivity until proteolytic activation .
CPB-2 antibodies are critical for detecting and quantifying CPB2 in experimental models.
CPB2 deficiency exacerbates inflammation: Cpb2−/− mice exhibited severe arthritis in collagen-induced models due to unregulated C5a activity .
Therapeutic potential: Anti-C5a antibodies improved survival in CPB2-deficient mice, highlighting CPB2's role in modulating complement-driven inflammation .
ProCPU/TAFI polymorphism: The Thr325Ile variant prolongs CPB2 activity, increasing thrombotic risk .
Inhibitor development: CPB2 inhibitors are under investigation to enhance fibrinolysis in stroke and myocardial infarction .
Clostridium perfringens β2-toxin: CPB2 antibodies (e.g., 1E23, 2G7) neutralize cytotoxicity in intestinal epithelial cells by targeting epitopes (AA 98–109 and 252–263) .
Host adaptation: The cpb2 gene in C. perfringens shows host-specific variations, influencing virulence in porcine enteritis .
Western blot validation: Antibodies like CAB15266 detect CPB2 at ~48 kDa in human liver lysates .
Neutralization assays: Preincubation with 1E23 reduced rCPB2-induced apoptosis in NCM460 cells by 70% .
Immunohistochemistry: AF6036 localizes CPB2 in cytoplasm, aiding cancer biomarker studies .