Chromogenic substrate cleaved by cathepsin G, subtilisins, chymotrypsin, chymase, and cyclophilins, but not neutrophil elastase. Release of pNA is monitored at 405-410 nm. This substrate is useful for inhibitor screening and kinetic analysis. Also available: calibration standard pNA (BML-KI145).
Product Details
| Alternative Name: | Suc-Ala-Ala-Pro-Phe-pNA |
| |
| Sequence: | Suc-Ala-Ala-Pro-Phe-pNA [Suc=succinyl; pNA=p-nitroanilide] |
| |
| MW: | 624.65 |
| |
| Purity: | ≥99% |
| |
| Shipping: | Blue Ice |
| |
| Long Term Storage: | -20°C |
| |
| Regulatory Status: | RUO - Research Use Only |
| |
Product Literature References
Cell penetrable, clickable and tagless activity-based probe of human cathepsin L: D. Dana, et al.; Bioorg. Chem.
85, 505 (2019),
Application(s): Activity assay,
Abstract;
Chymase-dependent production of angiotensin II: an old enzyme in old hearts: G. Froogh, et al.; Am. J. Physiol. Heart Circ. Physiol.
312, H223 (2017),
Abstract;
Cloning and characterization of a basic cysteine-like protease (cathepsin L1) expressed in the gut of larval Diaprepes abbreviatus L.(Coleoptera: Curculionidae): S. Ben-Mahmoud, et al.; J. Insect Physiol.
72, 1 (2015),
Abstract;
