TAFI – Thrombin Activatible Fibrinolysis Inhibitor Antibodies
Affinity Biologicals, Inc. manufactures a broad range of TAFI – Thrombin Activatible Fibrinolysis Inhibitor Antibodies which can be found in the listing below. Further information about each individual TAFI – Thrombin Activatible Fibrinolysis Inhibitor Antibody is available by following the associated links. Our TAFI – Thrombin Activatible Fibrinolysis Inhibitor Antibodies are excellent for use in immunoassays where high sensitivity is required and are frequently the preferred reagent for immunopreciptaion techniques and activity neutralization assays. These antibodies have proven to be extremely useful in the preparation of immune-adsorbent resins for use in immuno-depletion of specific proteins from plasma as well as immuno-affinity purification of proteins. Affinity’s TAFI – Thrombin Activatible Fibrinolysis Inhibitor Antibodies are manufactured for use in research applications.
Listing of TAFI – Thrombin Activatible Fibrinolysis Inhibitor Antibodies
SATAFI-IG – Sheep anti human TAFI, purified IgG (10mg vial)
SATAFI-HRP – Sheep anti human TAFI – Thrombin Activatable Fibrinolysis Inhibitor, peroxidase conjugated IgG (0.2 mg vial)
SATAFI-AP – Sheep anti human TAFI – Thrombin Activatable Fibrinolysis Inhibitor, affinity purified IgG (0.5 mg vial)
TAFI-AG – Complete TAFI Antigen ELISA Kit – 1 plate/kit
Description of Thrombin Activatible Fibrinolysis Inhibitor (TAFI)
TAFI (Thrombin Activatable Fibrinolysis Inhibitor), also referred to as plasma procarboxypeptidase-B, procarboxypeptidase-U and R, circulates in plasma as a zymogen with a mass of 58,000 daltons (1-6). Proteolytic activation of TAFI yields an N-terminally derived activation peptide and the C-terminal portion corresponding to the metalloprotease, activated TAFI (TAFIa). TAFIa exhibits exopeptidase activity with carboxypeptidase B-like substrate specificity capable of catalyzing the hydrolysis of C-terminal lysine and arginine residues. Cleavage of these residues on fibrin by TAFIa attenuates clot lysis by inhibiting the formation of the ternary activation complex comprising fibrin cofactor, tPA and plasminogen, thereby inhibiting plasmin generation. Although TAFI can be activated by various proteases including thrombin and plasmin, the physiological activator is proposed to be the complex thrombin-thrombomodulin since the rate of activation is stimulated 1250-fold compared to thrombin alone (4). However, the rate of TAFI activation is highly dependent upon its plasma concentration. Since TAFIa apparently plays a key role in connecting coagulation and fibrinolysis and significantly increases clot stability, determination of plasma concentration of TAFI is likely crucial to assess its subsequent potential antifibrinolytic effects1-6.
References and Reviews
- Eaton, D.L., Malloy, B.E., Tsai, S.P., Henzel, W., Drayna, D., Isolation, Molecular Cloning and Partial Characterization of a Novel Carboxypeptidase B from Human Plasma. J.Biol.Chem. 266:21833-21838, 1991.
- Hendriks, D., Scharpe, S., van Sande, M., Lommaert, M.P., Characterization of a carboxypeptidase in human serum distinct from carboxypeptidase N. J.Clin.Chem.Clin.BioChem. 27:277-285, 1989.
- Campbell, W., Okada, J. An Arginine specific carboxypeptidase generated in blood during coagulation of inflammation which is unrelated to carboxypeptidase N or its subunits. Biochem.Biophys.Res.Commun. 162:933-939, 1989.
- Bajzar, L., Morser, J., Nesheim, M.E. TAFI, or procarboxypeptidase B, couples the coagulation and fibrinolytic cascades through the thrombin-thrombomodulin complex. J.Biol.Chem. 271:16603-16608, 1996.
- Mosnier, L.O., von Dem Borne, P.A. Meijers, J.C., Plasma TAFI levels influence the clot lysis time in healthy individuals in the presence of an intact intrinsic pathway of coagulation. Thromb.Haemost. 80:829-835, 1998.
- Juhan-Vague, I., Renucci, J.F., and Grimaux, M., Morange, P.E., Gouvernet, J., Gourmelin, Y., Laessi, M.C. Thrombin Activatable Fibrinolysis Inhibitor Antigen Levels and cardiovascular Risk Factors. Arter.Thromb.Vascular.Biology. 20:2156-2161, 2000.