Non-cleavable Human tPA


SKU: HTPA-NC Categories: ,

Product Description

Non-cleavable Human tPA

The addition of an arginine to glutamic acid mutation generates human tPA that is 100percent single chain and resistant to cleavage by plasmin. The mutation site is R275E on the mature protein and R310E on the complete mRNA sequence (UniProtKB: locus TPA_HUMAN, accession P00750). Recombinantly produced in insect cells.

1. Functional role of proteolytic cleavage at arginine-275 of human tissue plasminogen activator as assessed by site-directed mutagenesis.
KM Tate, DL Higgins, WE Holmes, ME Winkler, HL Heyneker, and GA Vehar
Biochemistry, January 27, 1987; 26(2): 338-43.

2. Plasmin-Mediated Fibrinolysis by Variant Recombinant Tissue Plasminogen Activators
Shoko Urano, Alan R. Metzger, and Francis J. Castellino
PNAS, Apr 1989; 86: 2568 – 2571.

3. Plasminogen activation with single-chain urokinase-type plasminogen
activator (scu-PA). Studies with active site mutagenized plasminogen
(Ser740Ala) and plasmin-resistant scu-PA (Lys158Glu)
HR Lijnen, B Van Hoef, L Nelles, and D Collen
J. Biol. Chem., Mar 1990; 265: 5232 – 5236.

Gene ID: 5327
Swiss-Prot/UniProt ID: P00750

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