TPA (36-310) Human
Tissue-type plasminogen activator, EC 3.4.21.68, tPA, t-PA, t-plasminogen activator, TPA, T-PA, DKFZp686I03148, PLAT and tPA, Alteplase, Reteplase, Plasminogen Activator, Tissue, Plasminogen/Activator Kringle.
Greater than 90.0% as determined by SDS-PAGE.
Description
TPA Human Recombinant produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 284 amino acids (36-310a.a.) and having a molecular mass of 32.0kDa (Molecular size on SDS-PAGE will appear at approximately 28-40kDa).
TPA is expressed with a 6 amino acids His tag at C-Terminus and purified by proprietary chromatographic techniques.
Product Specs
Tissue-type plasminogen activator, EC 3.4.21.68, tPA, t-PA, t-plasminogen activator, TPA, T-PA, DKFZp686I03148, PLAT and tPA, Alteplase, Reteplase, Plasminogen Activator, Tissue, Plasminogen/Activator Kringle.
ADPSYQVICR DEKTQMIYQQ HQSWLRPVLR SNRVEYCWCN SGRAQCHSVP VKSCSEPRCF NGGTCQQALY FSDFVCQCPE GFAGKCCEID TRATCYEDQG ISYRGTWSTA ESGAECTNWN SSALAQKPYS GRRPDAIRLG LGNHNYCRNP DRDSKPWCYV FKAGKYSSEF CSTPACSEGN SDCYFGNGSA YRGTHSLTES GASCLPWNSM ILIGKVYTAQ NPSAQALGLG KHNYCRNPDG DAKPWCHVLK NRRLTWEYCD VPSCSTCGLR QYSQPQFRHH HHHH.
Product Science Overview
Tissue Plasminogen Activator (tPA) is a serine protease enzyme involved in the breakdown of blood clots. It plays a crucial role in the fibrinolytic system by converting plasminogen to plasmin, which then degrades fibrin clots. The recombinant form of tPA, specifically the fragment spanning amino acids 36 to 310, has been engineered for various research and therapeutic applications.
The recombinant tPA fragment (36-310 a.a.) is a human protein expressed in baculovirus-infected insect cells. This fragment includes the essential domains responsible for its activity, such as the kringle domains and the serine protease domain. The kringle domains are involved in binding to fibrin, while the serine protease domain is responsible for the enzymatic activity that converts plasminogen to plasmin .
The recombinant tPA (36-310 a.a.) is produced with a His tag at the C-terminus, facilitating its purification through affinity chromatography. The protein is typically purified to over 90% purity and has an endotoxin level of less than 1 EU/µg, making it suitable for various biochemical assays and research applications .
Recombinant tPA is widely used in research to study the mechanisms of fibrinolysis and to develop therapeutic agents for thrombolytic therapy. It is also used in high-throughput screening assays to identify potential inhibitors or enhancers of tPA activity. In clinical settings, tPA is used as a thrombolytic agent to treat acute ischemic stroke by dissolving blood clots and restoring blood flow to the brain .
tPA exerts its effect by binding to fibrin in a blood clot and converting the entrapped plasminogen to plasmin. Plasmin then degrades the fibrin matrix of the clot, leading to clot dissolution. This process is crucial for maintaining vascular patency and preventing conditions such as stroke and myocardial infarction .
