|Application ||WB, IHC, IF, FC|
|Calculated MW||58951 Da|
|Other Names||Caspase-10, CASP-10, Apoptotic protease Mch-4, FAS-associated death domain protein interleukin-1B-converting enzyme 2, FLICE2, ICE-like apoptotic protease 4, Caspase-10 subunit p23/17, Caspase-10 subunit p12, CASP10, MCH4|
|Target/Specificity||A synthetic peptide corresponding to N-terminal residues of human Caspase-10 subunit p23/17 was used as immunogen. The antibody does not cross-react with other Caspase family members.|
|Format||50 mM Tris-Glycine (pH 7.4), 0.15 M NaCl, 40% Glycerol, 0.01% sodium azide and 0.05% BSA.|
|Storage||Maintain refrigerated at 2-8°C for up to 6 months. For long term storage store at -20°C in small aliquots to prevent freeze-thaw cycles.|
|Precautions||Caspase-10 Antibody (Pro) is for research use only and not for use in diagnostic or therapeutic procedures.|
|Function||Involved in the activation cascade of caspases responsible for apoptosis execution. Recruited to both Fas- and TNFR-1 receptors in a FADD dependent manner. May participate in the granzyme B apoptotic pathways. Cleaves and activates caspase- 3, -4, -6, -7, -8, and -9. Hydrolyzes the small- molecule substrates, Tyr-Val-Ala-Asp-|-AMC and Asp-Glu-Val-Asp-|-AMC.|
|Tissue Location||Detectable in most tissues. Lowest expression is seen in brain, kidney, prostate, testis and colon|
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Provided below are standard protocols that you may find useful for product applications.
Caspases are a family of cytosolic aspartate-specific cysteine proteases involved in the initiation and execution of apoptosis. Caspase-10 (MCH4, FLICE2) is one of the initiator caspases (1,2), and is localized to various tissues. Pro-caspase-10 has two death effector domains (DEDs) that bind FADD and recruits both TNFR1 and CD95 to form complexes with these receptors and induce apoptosis (1,2). This death domain complex cleaves pro-caspase-10 into a large active fragment and a small fragment. Cleaved caspase-10 leads to the processing of caspase-3 and caspase-7, initiating a caspase cascade and subsequent apoptosis (3,4). It has been shown that the Caspase-10 protein is not produced in neither mouse nor rat (5).
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. 272: 6578
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 93: 7464
3. Srinivasula, S.M. et al. Molecular ordering of the Fas-apoptotic pathway: the Fas/APO-1 protease Mch5 is a CrmA-inhibitable protease that activates multiple Ced-3/ICE-like cysteine proteases. Proc. Natl. Acad. Sci., USA 93: 14486
4. Wang, J. et al. Inherited human Caspase 10 mutations underlie defective lymphocyte and dendritic cell apoptosis in autoimmune lymphoproliferative syndrome type II. Cell 98: 47
5. Janicke RU, Science 312(5782): 1874, 2006.
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