TPA (36-310), Human Recombinant

Tissue plasminogen activator (PLAT or tPA) is a secreted serine protease which converts the proenzyme plasminogen to plasmin, a fibrinolytic enzyme. Plasminogen is synthesized as a single chain which is cleaved by PLAT into the two chain disulfide linked plasmin. 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. TPA Human Recombinant produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 284 amino acids (36-310 a.a.) and having a molecular mass of 32.0 kDa (Molecular size on SDS-PAGE will appear at approximately 28-40 kDa). TPA is expressed with a 6 amino acids His tag at C-Terminus and purified by proprietary chromatographic techniques.