Clone: MCH2 14 1-190
Background: Caspase-6 (Cysteine-Requiring Aspartate Proteases) is part of a family of intracellular cysteine proteases that cleave their substrates after aspartic acid residues. These proteases play an integral role in inducing apoptosis in cells. Procaspase-6 (Mch2), a member of the ICE/ced-3 subfamily, is an inactive proenzyme that is activated to form caspase-6 by proteolytic cleavage at certain aspartic acid residues. During cleavage, the N-terminal is removed and the proenzyme is converted into a large (p18) and small (p11) subunits. Caspase-6 has two isoforms, and , produced by alternative splicing. Over-expression of the isoform of caspase-6 without its prodomain can induce apoptosis. The isoform does not seem to display proteolytic activity. Together with caspases-3 and -7, the isoform of caspase-6 is classified as an effector/execution caspase. Caspase-3, caspase-8 and caspase-10 can cleave procaspase-6. Active caspase-6 cleaves several other proteins such as lamins, NuMa and Keratin 18. A possible cleavage of caspases-8 and -10 in cytochrome-C dependent apoptosis was reported recently.
Positive Control: MCF-7 cell lysate
Immunogen: Hybridoma produced by the fusion of splenocytes from mice immunized with recombinant human capase-6 protein and mouse myeloma cells.
Purification Method: Protein A/G Chromatography
Concentration: See vial for concentration
Formulation: Provided as solution in phosphate buffered saline with 0.08% sodium azide
References: 1. Kidd, V.J., Proteolytic activities that mediate apoptosis. Annu. Rev. Physiol. 1998, 60, 533-5732. Fernandes – Alnemri, T., et al., Mch2, a new member of the apoptotic Ced-3/Ice cysteine protease gene family. Cancer Res. 1995, 55, 2737-27423. Orth, K., et al., The CED-3/ICE-like protease Mch2 is activated during apoptosis and cleaves the death substrate lamin A. J. Biol. Chem. 1996, 271, 164434. Hirata, H., et al., Caspases are activated in a branched protease cascade and control distinct downstream processes in Fas-induced apoptosis. J. Exp. Med. 1998, 187, 587-6005. Slee, E. A., et al., Ordering the cytochrome c-initiated caspase cascade: hierarchial activation of caspases-2, -3, -6, -7, -8 and -10 in a caspase-9-dependent manner. J. Cell Biol., 144, 281 (1999)6. Cohen, G.M., et al. Caspases: the executioners of apoptosis. Biochem. J. 1997, 326, 1-16
UniProt: P55212
Caution: This product is intended FOR RESEARCH USE ONLY, and FOR TESTS IN VITRO, not for use in diagnostic or therapeutic procedures involving humans or animals.
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