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Caspase 9 Substrate 1, chromogenic

pNA (4-nitroaniline)-derived caspase substrates are widely used for the colorimetric detection of various caspase activities. Cleavage of pNA peptides by caspases generates pNA that is monitored colorimetrically at ~405 nm. pNA has maximum absorption around 408 nm.

Designed for biological research and industrial applications, not intended for individual clinical or medical purposes.

CAT No: A55003

Custom Peptide Synthesis
cGMP Peptide
  • Registration of APIs
  • CMC information required for an IND
  • IND and NDA support
  • Drug master files (DMF) filing
M.W/Mr.
674.7
Sequence
One Letter Code: Ac-LEHD-pNA
Three Letter Code: Ac-Leu-Glu-His-Asp-pNA
References
1. Grutter MG (2000). Caspases: key players in programmed cell death. Curr Opin Struct Biol 10, 649-55;
2. Gastman BR (2001). Apoptosis and its clinical impact. Head Neck 23, 409-25;
3. Grutter MG (2000). Caspases: key players in programmed cell death. Curr Opin Struct Biol 10, 649-55;
4. Stennicke HR and Salvesen GS (1999). Catalytic properties of the caspases. Cell Death Differ 6, 1054-9;
5. Stennicke HR and Salvesen GS (1998). Properties of the caspases. Biochim Biophys Acta 1387, 17-31;
6. Thornberry NA and Lazebnik Y (1998). Caspases: enemies within. Science 281, 1312-6;
7. Talanian RV, et al. (1997). Substrate specificities of caspase family proteases. J Biol Chem 272, 9677-82;
8. Fassy F, et al. (1998). Enzymatic activity of two caspases related to interleukin-1beta-converting enzyme. Eur J Biochem 253, 76-83; 9. Datta R, et al. (1996). Activation of the CPP32 protease in apoptosis induced by 1-?-D-arabinofuranosylcytosine and other DNA-damaging agents. Blood 88, 1936-43;
10. Koeplinger KA, et al. (2000). Caspase 8: an efficient method for large-scale autoactivation of recombinant procaspase 8 by matrix adsorption and characterization of the active enzyme. Protein Expr Purif 18, 378-87.

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