Caspase 10, Apoptosis-Related Cysteine Peptidase (CASP10) (pro-form) antibody

Details for Product No. ABIN649428
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Antigen
Synonyms xCaspase-10, alps2, caspace-10, caspase-10, flice2, mch4, xCaspace-10, ALPS2, FLICE2, MCH4
Epitope
pro-form
(30), (7), (6), (4), (4), (4), (3), (2), (2), (2), (2), (2), (1), (1), (1), (1), (1), (1), (1), (1), (1)
Reactivity
Human
(127), (16), (16), (1), (1), (1)
Host
Rabbit
(116), (8), (2), (1), (1)
Clonality
Monoclonal
Conjugate
Un-conjugated
(1), (1), (1), (1), (1), (1), (1), (1), (1), (1), (1)
Application
Western Blotting (WB), Immunohistochemistry (IHC), Immunofluorescence (IF), Flow Cytometry (FACS)
(105), (47), (26), (26), (24), (10), (10), (6), (5), (4), (3), (2), (1)
Pubmed 3 references available
Quantity 100 μL
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Catalog No. ABIN649428
450.00 $
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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.
Alternative Name Caspase-10
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).
Synonyms: 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
Molecular Weight 59 kDA
Gene ID 843
UniProt Q92851
Research Area Apoptosis/Necrosis, Phospho-specific antibodies, Protein Modifications, Metabolism, Cell Structure
Application Notes The suggested dilution is: WB: = 1:500-1000 ,IHC: = 1:50-1:100
Comment

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).

Restrictions For Research Use only
Format Liquid
Buffer 50 mM Tris-Glycine (pH 7.4), 0.15 M NaCl, 40% Glycerol, 0.01% sodium azide and 0.05% BSA.
Preservative Sodium azide
Precaution of Use This product contains sodium azide: a POISONOUS AND HAZARDOUS SUBSTANCE which should be handled by trained staff only.
Storage -20 °C
Storage Comment Caspase-10 Antibody (Pro) can be stored at -20°C for up to 12 months from time of receipt.
Expiry Date 12 months
Background publications 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).

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