Measured by its ability to cleave a fluorogenic peptide substrate, (7-methoxycoumarin-4-yl) acetyl-Arg-Pro-Lys-Pro-Val-Glu-Nva-Trp-Arg-Lys (2, 4-dinitrophenyl)-NH2. Cleavage of substrate can be measured using excitation and emission wavelength at 320 nm and 405 nm, respectively.The specific activity is >300 pmoles/min/μg.
Thiol protease. Key protease responsible for the removal of the invariant chain from MHC class II molecules and MHC class II antigen presentation. The bond-specificity of this proteinase is in part similar to the specificities of cathepsin L1 Publication. Catalytic activity: Similar to cathepsin L, but with much less activity on Z-Phe-Arg-|-NHMec, and more activity on the Z-Val-Val-Arg-|-Xaa compound.
生物活性
Measured by its ability to cleave a fluorogenic peptide substrate, (7-methoxycoumarin-4-yl) acetyl-Arg-Pro-Lys-Pro-Val-Glu-Nva-Trp-Arg-Lys (2, 4-dinitrophenyl)-NH2. Cleavage of substrate can be measured using excitation and emission wavelength at 320 nm and 405 nm, respectively.The specific activity is >300 pmoles/min/μg.
Recombinant Human Cathepsin S protein (rp143673) - SDS-PAGE 2 μg/lane of Recombinant Human Cathepsin S Protein was resolved with SDS-PAGE under reducing (R) and non-reducing (N) conditions and visualized by Coomassie® Blue staining, showing the bands at 39 kDa (Pro) & 28 kDa (mature). Human Cathepsin S is synthesized as a preproenzyme of 331 amino acid residues consisting a signal peptide (residues 1‑16), a pro region (residues 17‑114), and the mature enzyme (residues 115‑331).
ZJ25F1028481
危险品化学品经营许可证（带存储）