Contents: Polyclonal anti-human caspase-10 (C-terminus, FLICE2)
Catalog Number: 14-6259
Formulation: This product is supplied as purified rabbit IgG fraction in PBS containing 0.02% NaN3.
Storage Conditions: Store at 4°C, stable for 6 months. Stable at –20°C for one year. Avoid multiple freeze/thaw cycles.
Clone: Polyclonal
Isotype: Rabbit IgG
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Description
The antibody reacts with human caspase-10 (C-terminus); the antibody was raised against residues 505-521 of human caspase-10/b, also known as FLICE2. Caspase-10 has at least 4 different isoforms: caspase-10/a (Mch4), caspase-10/b (FLICE2), caspase-10/c, caspase-10/d. Caspase-10 has two death effector domains (DEDs) that bind to the DED in the adaptor 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 . 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. Caspase-10 is expressed in many tissues and cell lines.
Applications Reported
For research use only, not for diagnostic or therapeutic use. This polyclonal antibody has been reported for use in immunoblotting (WB), and is human, mouse and rat reactive. It recognizes only the FLICE2 form of caspase-10.
Applications Tested
This polyclonal antibody has been tested by immunoprecipitation (~0.5-1 μg/ml) of human FLICE2 (caspase-10/b). It is recommended that the reagent be carefully titrated for optimal performance in the assay of interest.
References
Vincenz C, Dixit VM. 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;272:6578-83.
Fernandes-Alnemri T, Armstrong RC, Krebs J, Srinivasula SM, Wang L, Bullrich F, Fritz LC, Trapani JA, Tomaselli KJ, Litwack G, Alnemri ES. In vitro activation of CPP32 and Mch3 by Mch4, as novel human apoptotic cysteine protease containing two FADD-like domains.
Proc Natl Acad Sci USA. 1996;93:7464-69.
Cohen GM. Caspases: the executioners of apoptosis.
Biochem J 1997;326:1-16.
Ng PW, Porter AG, Janicke RU. Molecular cloning and characterization of two novel pro-apoptotic isoforms of caspase-10.
J Bio Chem, 1999;274(15):10301-10308
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