C1104
Monoclonal Anti-Caspase 7 antibody produced in rat
clone 11E4, purified immunoglobulin, buffered aqueous solution
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About This Item
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biological source
rat
conjugate
unconjugated
antibody form
purified immunoglobulin
antibody product type
primary antibodies
clone
11E4, monoclonal
form
buffered aqueous solution
mol wt
antigen (full length) 35 kDa
antigen (subunit) 20 kDa
species reactivity
human
technique(s)
immunoprecipitation (IP): suitable
microarray: suitable
western blot: 2-4 μg/mL using a whole extract of cultured human acute T cell leukemia Jurkat cells
isotype
IgG2a
UniProt accession no.
shipped in
dry ice
storage temp.
−20°C
target post-translational modification
unmodified
Gene Information
human ... CASP7(840)
General description
Caspase-7 is a apoptosis-related cysteine peptidase, commonly known as CASP7. It is a human protein encoded by the CASP7 gene. CASP7 is a member of the caspase (cysteine aspartate protease) family of proteins and is an executioner protein of apoptosis.
Immunogen
recombinant p20 subunit of human caspase-7.
Application
Monoclonal Anti-Caspase 7 antibody produced in rat is suitable for the following applications:
- Immunoprecipitation
- Microarray
- Western blotting at a concentration of 2-4μg/mL using a whole extract of cultured human acute T cell leukemia Jurkat cells.
Biochem/physiol Actions
Caspase-3 and -7 plays a central role in the execution-phase of cell apoptosis. The gene for caspase 7 (also known as Mch3, CMH-1 and ICELAP3) encodes a “short” prodomain protein product of 35 kDa that belongs to the Ced3/ICE family of cysteine proteases. Caspase 7 undergoes acleavage upon activation by caspase-3, -9 and -10, and granzyme B, leading to p20 and p12 subunits. It is an important intracellular effector of granzyme B-mediated apoptosis and cytotoxic Tlymphocyte- induced cell killing in vivo. Monoclonal antibodies reacting specifically with caspase 7 are useful tools for the study of protease networks involved in development and regulation and governing the life and death of cells and tissues.
Preparation Note
The antibody is purified from culture supernatant of hybridoma cells grown in a bioreactor.
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 Code
10 - Combustible liquids
Certificates of Analysis (COA)
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A M Chinnaiyan et al.
Current biology : CB, 6(7), 897-899 (1996-07-01)
Cytotoxic T lymphocytes (CTLs) and natural killers (NK) cells provide immune surveillance against viruses and neoplasms, and play a central role in the pathogenesis of autoimmune disease, AIDS and graft rejection. Thus, it is important to understand the precise molecular
Witold A Witkowski et al.
Protein science : a publication of the Protein Society, 20(8), 1421-1431 (2011-06-16)
Caspases are a powerful class of cysteine proteases. Introduction of activated caspases in healthy or cancerous cells results in induction of apoptotic cell death. In this study, we have designed and characterized a version of caspase-7 that can be inactivated
E Svandova et al.
Cell death & disease, 5, e1366-e1366 (2014-08-15)
Caspase-3 and -7 are generally known for their central role in the execution of apoptosis. However, their function is not limited to apoptosis and under specific conditions activation has been linked to proliferation or differentiation of specialised cell types. In
Yin Guo et al.
The Journal of biological chemistry, 277(16), 13430-13437 (2002-02-08)
Caspase-2 is one of the earliest identified caspases, but the mechanism of caspase-2-induced apoptosis remains unknown. We show here that caspase-2 engages the mitochondria-dependent apoptotic pathway by inducing the release of cytochrome c (Cyt c) and other mitochondrial apoptogenic factors
H Duan et al.
The Journal of biological chemistry, 271(3), 1621-1625 (1996-01-19)
Members of the ICE/ced-3 gene family have been implicated as components of the cell death pathway. Based on similarities with the structural prototype interleukin-1 beta-converting enzyme (ICE), family members are synthesized as proenzymes that are proteolytically processed to form active
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