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Detect tPA (Tissue Plasminogen Activator) using this Anti-tPA (Tissue Plasminogen Activator) Antibody, clone GMA-043 validated for use in ELISA & WB.
More>>Detect tPA (Tissue Plasminogen Activator) using this Anti-tPA (Tissue Plasminogen Activator) Antibody, clone GMA-043 validated for use in ELISA & WB. Less<<
SDB (Sicherheitsdatenblätter), Analysenzertifikate und Qualitätszertifikate, Dossiers, Broschüren und andere verfügbare Dokumente.
This gene encodes tissue-type plasminogen activator, a secreted serine protease which converts the proenzyme plasminogen to plasmin, a fibrinolytic enzyme. Tissue-type plasminogen activator is synthesized as a single chain which is cleaved by plasmin to a two chain disulfide linked protein. This enzyme plays a role in cell migration and tissue remodeling. Increased enzymatic activity causes hyperfibrinolysis, which manifests as excessive bleeding; decreased activity leads to hypofibrinolysis which can result in thrombosis or embolism. Alternative splicing of this gene results in multiple transcript variants encoding different isoforms.
FUNCTION: SwissProt: P00750 # Converts the abundant, but inactive, zymogen plasminogen to plasmin by hydrolyzing a single Arg-Val bond in plasminogen. By controlling plasmin-mediated proteolysis, it plays an important role in tissue remodeling and degradation, in cell migration and many other physiopathological events. Play a direct role in facilitating neuronal migration. SIZE: 562 amino acids; 62917 Da SUBUNIT: Heterodimer of chain A and chain B held by a disulfide bond. Binds to fibrin with high affinity. This interaction leads to an increase in the catalytic efficiency of the enzyme between 100-fold and 1000-fold, due to an increase in affinity for plasminogen. Similarly, binding to heparin increases the activation of plasminogen. Binds to annexin A2, cytokeratin-8, fibronectin and laminin. Binds to mannose receptor and the low- density lipoprotein receptor-related protein (LRP1); these proteins are involved in TPA clearance. Yet unidentified interactions on endothelial cells and vascular smooth muscle cells (VSMC) lead to a 100-fold stimulation of plasminogen activation. In addition, binding to VSMC reduces TPA inhibition by PAI-1 by 30-fold. Binds LRP1B; binding is followed by internalization and degradation. SUBCELLULAR LOCATION: Secreted, extracellular space. TISSUE SPECIFICITY: Synthesized in numerous tissues (including tumors) and secreted into most extracellular body fluids, such as plasma, uterine fluid, saliva, gingival crevicular fluid, tears, seminal fluid, and milk. DOMAIN: SwissProt: P00750 Both FN1 and one of the kringle domains are required for binding to fibrin. & Both FN1 and EGF-like domains are important for binding to LRP1. & The FN1 domain mediates binding to annexin A2. & The second kringle domain is implicated in binding to cytokeratin-8 and to the endothelial cell surface binding site. PTM: The single chain, almost fully active enzyme, can be further processed into a two-chain fully active form by a cleavage after Arg-310 catalyzed by plasmin, tissue kallikrein or factor Xa. & Differential cell-specific N-linked glycosylation gives rise to two glycoforms, type I (glycosylated at Asn-219) and type II (not glycosylated at Asn-219). The single chain type I glycoform is less readily converted into the two-chain form by plasmin, and the two-chain type I glycoform has a lower activity than the two- chain type II glycoform in the presence of fibrin. & N-glycosylation of Asn-152; the bound oligomannosidic glycan is involved in the interaction with the mannose receptor. & Characterization of O-linked glycan was studied in Bowes melanoma cell line.DISEASE:SwissProt: P00750 # Increased activity of TPA causes hyperfibrinolysis, with excessive bleeding as a consequence. & Defective release of TPA causes hypofibrinolysis, leading to thrombosis or embolism. SIMILARITY: Belongs to the peptidase S1 family. & Contains 1 EGF-like domain. & Contains 1 fibronectin type-I domain. & Contains 2 kringle domains. & Contains 1 peptidase S1 domain.
Molecular Weight
Mr 63kDa
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routinely evaluated by immunoblot on human tPA
Usage Statement
Unless otherwise stated in our catalog or other company documentation accompanying the product(s), our products are intended for research use only and are not to be used for any other purpose, which includes but is not limited to, unauthorized commercial uses, in vitro diagnostic uses, ex vivo or in vivo therapeutic uses or any type of consumption or application to humans or animals.
Update on intravenous tissue plasminogen activator for acute stroke: from clinical trials to clinical practice Gladstone, D J and Black, S E CMAJ : Canadian Medical Association journal = journal de l'Association medicale canadienne, 165:311-7 (2001)
2001
Plasminogen activators have immense clinical significance as thrombolytic agents for management of stroke and myocardial infarction. Tissue-type plasminogen activator (tPA) is generally preferred as being effective and safer than either urokinase or streptokinase type activators. Large-scale production of tPA became possible through groundbreaking developments in cell lines and bioprocess technology. Nevertheless, at thousands of dollars per treatment, tPA remains expensive. Enhancing cellular productivity and downstream product recovery through new approaches continue to be major challenges as discussed in this review. Recent clinical experience suggests the need for yet better fibrinolytic agents and attempts are underway to modify the tPA molecule to second generation products. Emerging trends in this field are outlined.