tPA / PLAT Protein (Fc tag) (recombinant human)

Protein Construction: A DNA sequence encoding the a chain (Tyr 37-Arg 310) of mature human tPA (NP_000921.1) was expressed with the fused Fc region of human IgG1 at the N-terminus. Sequence: Tyr 37-Arg 310. Fusion tag: N-Fc Endotoxin: < 1.0 EU per µg as determined by the LAL method. Apparent Molecular Mass: 59 kDa. Protein function: 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 alpha and beta 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 thrombol Protein function: 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. Plays a direct role in facilitating neuronal migration. [The UniProt Consortium]