C8351
Anti-Caspase 10 antibody produced in rabbit
affinity isolated antibody, buffered aqueous solution
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About This Item
biological source
rabbit
conjugate
unconjugated
antibody form
affinity isolated antibody
antibody product type
primary antibodies
clone
polyclonal
form
buffered aqueous solution
mol wt
antigen 59 kDa
species reactivity
human
technique(s)
microarray: suitable
western blot: 1:500 using a whole extract of Jurkat human acute T leukemia cells extract
UniProt accession no.
shipped in
dry ice
storage temp.
−20°C
target post-translational modification
unmodified
Gene Information
human ... CASP10(843)
General description
Caspases are a family of intracellular proteases that mediate cell death and are the principal effectors of apoptosis. Caspase 10 is a apoptosis-related cysteine protein. It contains two death domains (DED) involved in linking to the death effector domain of the adapter protein FADD and recruiting the complex to TNFR1 and Fas.
Immunogen
synthetic peptide corresponding to amino acid residues 359-372 of human caspase 10a p23/p17 with N-terminal added lysine conjugated to KLH with glutaraldehyde.
Application
Anti-Caspase 10 antibody was used in Immunohistochemistry, western blot and tissue microarray to study the proteomics for esophageal cancer.
Biochem/physiol Actions
Caspase 10 (Mch4, ICE-LAP4, FLICE2) plays an important role in apoptosis which is induced by a variety of inducers such as TNF-α and Anti-Fas antibody. It is a large- prodomain caspase classified together with caspases 2, 8, and 9 as a signaling caspase. Four isoforms of caspase 10 (caspase 10a, 10b, 10c, and 10d) having the same prodomain but different mature large and small subdomain, have been described. It plays a key role in the NF-κB pathway and NF-κB, a signal transduction factor, plays an important part in the carcinogenesis of esophageal cancer. Overexpression of a caspase 10 increases NF-κB activity. The inactive procaspase 10 is variably expressed in many tissues and cell lines as a cytosolic protein. The mature form of caspase 10 comprises two subunits, p23/p17 (splice isoforms) and p12. Caspase 10 can cleave and activate caspases 3, 4, 6, 7, 8, and 9.
Physical form
Solution in 0.01 M phosphate buffered saline, pH 7.4, containing 1% bovine serum albumin and 15 mM sodium azide
Disclaimer
Unless otherwise stated in our catalog or other company documentation accompanying the product(s), our products are intended for research use only and are not to be used for any other purpose, which includes but is not limited to, unauthorized commercial uses, in vitro diagnostic uses, ex vivo or in vivo therapeutic uses or any type of consumption or application to humans or animals.
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Storage Class
10 - Combustible liquids
wgk_germany
WGK 3
flash_point_f
Not applicable
flash_point_c
Not applicable
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Tewis Bouwmeester et al.
Nature cell biology, 6(2), 97-105 (2004-01-27)
Signal transduction pathways are modular composites of functionally interdependent sets of proteins that act in a coordinated fashion to transform environmental information into a phenotypic response. The pro-inflammatory cytokine tumour necrosis factor (TNF)-alpha triggers a signalling cascade, converging on the
C Vincenz et al.
The Journal of biological chemistry, 272(10), 6578-6583 (1997-03-07)
The pivotal discovery that Fas-associated death domain protein (FADD) interleukin-1beta-converting enzyme (FLICE)/MACH was recruited to the CD95 signaling complex by virtue of its ability to bind the adapter molecule FADD established that this protease has a role in initiating the
T Fernandes-Alnemri et al.
Proceedings of the National Academy of Sciences of the United States of America, 93(15), 7464-7469 (1996-07-23)
Emerging evidence suggests that an amplifiable protease cascade consisting of multiple aspartate specific cysteine proteases (ASCPs) is responsible for the apoptotic changes observed in mammalian cells undergoing programmed cell death. Here we describe the cloning of two novel ASCPs from
R V Talanian et al.
The Journal of experimental medicine, 186(8), 1323-1331 (1997-10-23)
We report that the serine protease granzyme B (GrB), which is crucial for granule-mediated cell killing, initiates apoptosis in target cells by first maturing caspase-10. In addition, GrB has a limited capacity to mature other caspases and to cause cell
S M Srinivasula et al.
Proceedings of the National Academy of Sciences of the United States of America, 93(25), 14486-14491 (1996-12-10)
The Fas/APO-1-receptor associated cysteine protease Mch5 (MACH/FLICE) is believed to be the enzyme responsible for activating a protease cascade after Fas-receptor ligation, leading to cell death. The Fas-apoptotic pathway is potently inhibited by the cowpox serpin CrmA, suggesting that Mch5
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