Human tPA/PLAT Recombinant Protein (RPES1289)

Human tPA/PLAT Recombinant Protein

Tissue plasminogen activator (abbreviated tPA or PLAT), a serine protease that transforms plasminogen into biologically active plasmin. TPA, as a protease, has numerous functions in the blood fibrinolysis, extracellular matrix homeostasis, and post-translational activation of growth factors. tPA is synthesized and secreted as a single chain polypeptide precursor which is cleaved in turn by plasmin. The proteolytic cleavage of the C-terminal side of Arg275 generates the enzyme, which is made up of two subunits: alpha and beta chains. 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 present not only in the blood, where it performs its main thrombolytic function as an enzyme, but also in the central nervous system (CNS). Participates in a number of physiological and pathological events in the brain, as well as the function of neuroserpin as the natural regulator of tPA activity in these processes. Hyperfibrinolysis or hypofibrinolysis occur when tPA activity is increased or decreased, respectively. tPA plays a pivotal role in the pathogenesis of renal interstitial fibrosis through diverse mechanisms. As a fibrogenic cytokine, it promotes the development of kidney disease. Human tPA/PLAT Recombinant Protein is a highly pure recombinant protein developed by Assay Genie for use in a range of applications.