tPA – Tissue-type Plasminogen Activator Polyclonal Antibody – Affinity Purified
Affinity’s tPA – Tissue-type Plasminogen Activator Polyclonal Antibody – Affinity Purified is the highest level of our tPA – Tissue-type Plasminogen Activator antibody family. During the Antigen Affinity Purification process the IgG has had any non-specific immunoglobulin fraction eliminated which enriches the specificity of the remaining immunoglobulin towards the target antigen. The result is a very high-purity product with a substantially higher titre than whole or purified IgG. Our tPA – Tissue-type Plasminogen Activator Polyclonal Antibody – Affinity Purified is provided in a solution of HEPES buffered saline containing 50% glycerol (v/v) and is intended for applications such as immunoblotting, immunostaining of cells and several types of immunoassays where the higher signal-to-noise ratio achieved with this enriched product is required.
Product Code: SATPA-AP
Retail Product Size: 0.5mg vial
Host Animal: Sheep Anti-Human tPA – Tissue-type Plasminogen Activator Polyclonal Antibody – Affinity Purified
Species Cross Reactivity: View Chart
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.
- 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.