Liquid. In sterile-filtered 150 mM NaCl, 25 mM Tris, 10 mM CaCl2, pH 7.5. AVOID FREEZE/THAW CYCLES. Recombinant, human HCV NS3/4A protease expressed in E. coli and purified by affinity chromatography using FPLC. Purified as the single-chain form that requires activation with thermolysin or thrombin. HGFA is a serine protease that cleaves the single-chain HGF precursor, generating the active heterodimer. HGFA is secreted by the liver and normally circulates in the blood as an inactive zymogen, which can be activated by thrombin. The active protease is regulated by HGFA inhibitors. Speificity is measured using 250 µg activated enzyme and 10 µM substrate (MCA-Arg-Pro-Lys-Pro-Val-Glu-Nva-Trp-Arg-Lys-DNP-NH2). Specific activity: ≥15 pmol/min/µg activated HGFA. Purity: ≥95% by SDS-PAGE. Ref.: Kataoka, H., et al. 2000. J. Biol. Chem. 275, 40453. Miyazawa, K., et al. 1996. J. Biol. Chem. 271, 3615. Miyazawa, K., et al. 1993. J. Biol. Chem. 268, 10024. Shimomura, T., et al. 1993. J. Biol. Chem. 268, 22927. |
