Background: Apoptosis is related to many diseases and induced by a family of cell death receptors and their ligands. Cell death signals are transduced by death domain (DD)- containing adapter molecules and members of the ICE/CED-3 protease family. A novel ICE/CED-3 protease was identified recently, designated FLICE2 and Mch4(1,2) and renamed as caspase-10. Caspase-10 has two death effector domains (DEDs) that bind to the DED in the adapter molecule FADD and recruits both TNFR1 and CD95 to form complexes with these receptors. Caspase-10 is therefore involved in the CD95 and TNFR1 induced apoptosis(1) . Caspase-10 cleaves and activates caspase-3, -4, -6, -7, -8 and -9, which causes the proteolytic cleavage of many key proteins such as PARP. Cleavage of PARP occurs in many different systems during apoptosis and is the hallmark of programmed cell death (3). Caspase-10 is expressed in many tissues and cell lines(1,2).
Positive Control: HeLa whole cell lysates.
Immunogen: Synthetic peptide corresponding to amino acids 505-521 of human FLICE2.
Purification Method: Antigen Immunoaffiinity Purification.
Formulation: Provided in phosphate buffered saline solution containing 0.02% sodium azide as a preservative.
References: 1. Vincenz, C. and Dixit, V.M. Fas-associated death domain protein interleukin-1beta-converting enzyme 2 (FLICE2), an ICE/Ced-3 homologue, is proximally involved in CD95- and p55-mediated death signaling. J. Biol. Chem. 1997;272:6578-6583
2. Fernandes-Alnemri, T., et al., In vitro activation of CPP32 and Mch3 by Mch4, a novel human apoptotic cysteine protease containing two FADD-like domains. Proc. Natl. Acad. Sci. USA. 1996, 93, 7464-7469
3. Cohen, G.M., Caspases: the executioners of apoptosis. Biochem. J. 1997, 326, 1-16.
UniProt: Q92851.
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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