tPA – Tissue Plasminogen Activator Antibodies
Affinity Biologicals, Inc. manufactures a broad range of tPA – Tissue Plasminogen Activator Antibodies which can be found in the listing below. Further information about each individual tPA – Tissue Plasminogen Activator Antibody is available by following the associated links. Our tPA – Tissue Plasminogen Activator 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 tPA – Tissue Plasminogen Activator Antibodies are manufactured for use in research applications.
Listing of tPA – Tissue Plasminogen Activator Antibodies
SATPA-IG – Sheep anti human tPA, purified IgG (10mg vial)
SATPA-APBIO – Sheep anti human tPA – Tissue-type Plasminogen Activator, affinity purified, Biotinylated IgG (0.1 mg vial)
SATPA-APFTC – Sheep anti human tPA – Tissue-type Plasminogen Activator, affinity purified, FITC conjugated IgG (0.1 mg vial)
SATPA-HRP – Sheep anti human tPA – Tissue-type Plasminogen Activator, peroxidase conjugated IgG (0.2 mg vial)
SATPA-AP – Sheep anti human tPA – Tissue-type Plasminogen Activator, affinity purified IgG (0.5 mg vial)
Description of Tissue Plasminogen Activator tPA
Tissue-type plasminogen activator (tPA) is one of two major physiologic activators of plasminogen in plasma. It is a serine protease of 68 kDa produced primarily in endothelial cells but is also present in monocytes and megakaryocytes. Normal plasma tPA antigen concentrations have been reported from 20 ng/ml to 5 μg/ml, depending on the assay used, but typically most of the tPA (> 90%) is in complex with it’s primary inhibitor, plasminogen activator inhibitor-1 (PAI-1). Structurally, tPA is a single-chain enzyme that consists of a catalytic domain followed by two kringle structures, an EGF domain and a finger domain. The activation of plasminogen by tPA is dependent on the presence of a fibrin cofactor. The binding of both tPA and plasminogen to fibrin is mediated in part through lysine binding sites within the kringle structures of both enzyme and substrate, but also through the finger domain of tPA. Activation of plasminogen by tPA occurs by cleavage after residue Arg560 to produce the two-chain active serine protease plasmin. The activity of tPA is regulated in part by a very short half life in circulation (t½ of ~4 minutes) and by circulating protease inhibitors PAI-1 and to a lesser extent α2macroglobulin1-3.
References and Review
- Bachmann F; The Plasminogen-Plasmin Enzyme System; in Hemostasis and Thrombosis, 3rd Edition, eds. RW Colman, J Hirsh, VJ Marder and EW Salzman, pp. 1592-1622, J.B. Lippincott Co., Philadelphia PA, USA, 1994.
- Holvoet P, Cleemput H, Collen D; Assay of Human Tissue-Type Plasminogen Activator (t-PA) with an Enzyme-Linked Immunosorbent Assay (ELISA) Based on Three Murine Monoclonal Antibodies to t-PA. Thrombosis and Haemostasis 54, pp. 684-687, 1985.
- Giles AR, Nesheim, et al; The fibrinolytic Potential of the Normal Primate following the Generation of Thrombin In Vivo; Thrombosis and Haemostasis 63, pp. 476-481, 1990.