|+1 404 474 4654|
|+1 888 205 9894 (TF)|
Caspase 10, Apoptosis-Related Cysteine Peptidase (CASP10) (Pro-form) antibody
|Synonyms||MCH4, ALPS2, FLICE2, xCaspase-10, mch4, alps2, flice2, MGC107844, caspace-10, caspase-10, xCaspace-10, LOC100101580|
Alternatives Western Blotting (WB), Immunohistochemistry (IHC), Immunocytochemistry (ICC), Immunoprecipitation (IP), Flow Cytometry (FACS)
|3 references available|
|Price||450.00 $ Plus shipping costs $45.00|
|Availability||Will be delivered in 2 to 3 Business Days|
|Description||Other names: CASP10, MCH4, Caspase-10 subunit p12, ICE-like apoptotic protease 4,Apoptotic protease Mch-4,FAS-associated death domain protein interleukin-1B-converting enzyme 2|
|Characteristics||Rabbit Monoclonal Antibody|
|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.|
|Molecular Weight||59 kDA|
Background: 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).
|Application Notes||The suggested dilution is: WB: ~~ 1:500~1000 IP: ~~ 1:10 FC: ~~ 1:50 ICC: ~~ 1:100 IHC: ~~ 1:50~1:100|
|Buffer||50 mM Tris-Glycine (pH 7.4), 0.15 M NaCl, 40% Glycerol, 0.01% sodium azide and 0.05% BSA.|
|Storage||Caspase-10 Antibody (Pro) can be stored at -20°C for up to 12 months from time of receipt.|
|Research Area||Apoptosis/Necrosis, Phospho-specific antibodies, Protein Modifications, Metabolism, Cell Structure|
|Restrictions||For Research Use only|
Fernandes-Alnemri, Armstrong, Krebs et al.: "In vitro activation of CPP32 and Mch3 by Mch4, a novel human apoptotic cysteine protease containing two FADD-like domains." in: Proceedings of the National Academy of Sciences of the United States of America, Vol. 93, Issue 15, pp. 7464-9, 1996 (PubMed).
Vincenz, Dixit: "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." in: The Journal of biological chemistry, Vol. 272, Issue 10, pp. 6578-83, 1997 (PubMed).
Wang, Zheng, Lobito et al.: "Inherited human Caspase 10 mutations underlie defective lymphocyte and dendritic cell apoptosis in autoimmune lymphoproliferative syndrome type II." in: Cell, Vol. 98, Issue 1, pp. 47-58, 1999 (PubMed).