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Tissue Plasminogen Activator Protein / tPA (PLAT Protein)

Tissue Plasminogen Activator / tPA Products

Tissue Plasminogen Activator / tPA Protein, Recombinant

Molecule Species Description //For Detailed Info. and Price------CLICK! Cat No
tPA/PLAT Human PLAT / tPA Protein, Recombinant 10157-H01H1
tPA/PLAT Human tPAβ /Fc Protein, Recombinant 10157-H01H2
tPA/PLAT Human tPAβ Protein, Recombinant 10157-HNCH2
tPA/PLAT Mouse PLAT Protein, Recombinant 50910-M01H1

Tissue Plasminogen Activator / tPA cDNA Clone

Molecule Species Description //For Detailed Info. and Price------CLICK! Cat No
tPA/PLAT Human Homo sapiens tPAβ DNA transcript variant 1 cDNA Clone(NM_000930.3) HG10157-M
tPA/PLAT Mouse Mouse tPA/PLAT cDNA Clone / ORF Clone MG50910-G

Tissue Plasminogen Activator / tPA Related Areas

Enzyme>>Protease & Regulator>>Serine Protease & Regulator>>tPA/PLAT

Immunology>>Innate Immunity>>Coagulation>>tPA/PLAT

Cardiovascular>>Coagulation>>tPA/PLAT

Tissue Plasminogen Activator / tPA Alternative Names

PLAT, TPA, T-PA, DKFZp686I03148 [Homo sapiens]

Plat, t-PA, tPA, AU020998, AW212668, D8Ertd2e, MGC18508 [Mus musculus]

Tissue Plasminogen Activator / tPA Background

Tissue plasminogen activator (abbreviated tPA or PLAT), is traditionally viewed as a simple serine protease whose main function is to convert plasminogen into biologically active plasmin. As a protease, tPA plays a crucial role in regulating blood fibrinolysis, in maintaining the homeostasis of extracellular matrix and in modulating the post-translational activation of growth factors. tPA is synthesized and secreted as a single chain polypeptide precursor which is cleaved in turn by plasmin. Proteolytic cleavage at the C-terminal side of Arg275 generates the enzyme composed of two subunits, designated as α and β chains which are held together by a single disulfide bond. Unlike the other members of the chymotrypsin family, tPA has one particular distinction in that the catalytic efficiency of the single-chain enzyme is only slightly lower than that of the proteolytically cleaved form and is therefore not a true zymogen. tPA is found not only in the blood, where its primary function is as a thrombolytic enzyme, but also in the central nervous system (CNS). It participats in a number of physiological and pathological events in the CNS, as well as the role of neuroserpin as the natural regulator of tPA's activity in these processes. Increased or decreased activity of tPA leads to hyperfibrinolysis or hypofibrinolysis, respectively. In addition, as a cytokine, tPA plays a pivotal role in the pathogenesis of renal interstitial fibrosis through diverse mechanisms. Thus, as a fibrogenic cytokine, it promotes the progression of kidney diseases.

Tissue Plasminogen Activator / tPA Related Studies

  1. Yepes M, et al. (2004) New functions for an old enzyme: nonhemostatic roles for tissue-type plasminogen activator in the central nervous system. Exp Biol Med (Maywood). 229(11): 1097-104.
  2. Samson AL, et al. (2006) Tissue-type plasminogen activator: a multifaceted modulator of neurotransmission and synaptic plasticity. Neuron. 50(5): 673-8.
  3. Skrzypiec AE, et al. (2008) Tissue plasminogen activator in the amygdala: a new role for an old protease. J Physiol Pharmacol. 59 Suppl 8: 135-46.
  4. Hu K, et al. (2008) Novel actions of tissue-type plasminogen activator in chronic kidney disease. Front Biosci. 13: 5174-86.

 

 

Tissue Plasminogen Activator related areas, pathways, and other information

 

 

Please note: All products are "FOR RESEARCH USE ONLY AND ARE NOT INTENDED FOR DIAGNOSTIC OR THERAPEUTIC USE"
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