Caspase 2 is a cysteine protease that is potentially involved in cell cycle regulation and tumour suppression may be detected using peptides that contain the pentapeptide VDVAD such as the chromogenic and fluorogenic substrates: Ac-VDVAD-pNa (Acetyl-Val-Asp-Val-Ala-Asp-p- nitroanalide), chromogenic and MCA-VDVADGW-DNP-K-NH2, fluorogenic.
Storage Class Code
11 - Combustible Solids
WGK
WGK 1
Flash Point(F)
Not applicable
Flash Point(C)
Not applicable
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Apoptosis : an international journal on programmed cell death, 14(7), 829-848 (2009-05-30)
The caspases are an evolutionarily conserved family of cysteine proteases, with essential roles in apoptosis or inflammation. Caspase-2 was the second caspase to be cloned and it resembles the prototypical nematode caspase CED-3 more closely than any other mammalian protein.
The Journal of biological chemistry, 286(39), 34147-34154 (2011-08-11)
Caspase-2, the most evolutionarily conserved member in the human caspase family, may play important roles in stress-induced apoptosis, cell cycle regulation, and tumor suppression. In biochemical assays, caspase-2 uniquely prefers a pentapeptide (such as VDVAD) rather than a tetrapeptide, as
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