Caspase 13 (ERICE), an orthologue of human caspase 4, is a cysteine protease which may be detected using a variety of chromogenic and fluorogenic peptide substrates built around the LEED (Leu-Glu-Glu-Asp) sequence. These substrates include: Ac-LEED-pNa (acetyl-Leu-Glu-Glu-Asp-p-nitroanalide), chromogenic and Ac-LEED-AMC (Acetyl-Leu-Glu-Glu-Asp- amino-4-methylcoumarin), fluorogenic.
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Biochemical and biophysical research communications, 285(5), 1150-1154 (2001-08-02)
Caspase-13 was reported to be a member of the human caspase family of proteases (Humke, E., et al., J. Biol. Chem. 273, 15702-15707, 1998). By contrast, a recent study (Lin, X., et al., J. Biol. Chem. 275, 39920-39926, 2000) could
DNA sequence : the journal of DNA sequencing and mapping, 10(6), 387-394 (2000-05-29)
Caspases are cysteine proteases which have important roles in the activation of cytokines and in apoptosis. The ICE subfamily of caspases comprise peptides closely related to caspase-1, or interleukin-1beta (IL-1beta) converting enzyme (ICE), which promotes maturation of interleukin IL-1beta and
The Journal of biological chemistry, 273(25), 15702-15707 (1998-06-23)
Programmed cell death, or apoptosis, is a process of fundamental importance to cellular homeostasis in metazoan organisms (Ellis, R. E., Yuan, J., and Horvitz, H. R. (1991) Annu. Rev. Cell Biol. 7, 663-698). The caspase family of mammalian proteases, related
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