C268
Monoclonal Anti-m-Calpain (Domain III/IV) antibody produced in mouse
clone 107-82, ascites fluid
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About This Item
Conjugate:
unconjugated
Clone:
107-82, monoclonal
Application:
IF, WB
Citations:
11
biological source
mouse
conjugate
unconjugated
antibody form
ascites fluid
antibody product type
primary antibodies
clone
107-82, monoclonal
mol wt
antigen 80 kDa
species reactivity
pig, human, rat, bovine
technique(s)
indirect immunofluorescence: 1:50, western blot: 1:500
isotype
IgG1
UniProt accession no.
shipped in
dry ice
storage temp.
−20°C
target post-translational modification
unmodified
Quality Level
Gene Information
human ... CAPN2(824)
rat ... Capn2(29154)
General description
Calpain-2 catalytic subunit is a protein encoded by the CAPN2 gene in humans. Calpains are calcium dependent proteases constituting a family of proteins that are involved in essential cellular functions mediated by calcium. They share a homologous cysteine-protease domain and an E-F hand Ca2+-binding domain. The calpain system consists of two ubiquitous forms of calpain (m-calpain and μ-calpain), a tissue specific calpain (n-calpain) and a calpain inhibitory protein (calpastatin).
Immunogen
m-calpain from bovine skeletal muscle.
Application
Monoclonal Anti-m-Calpain (Domain III/IV) antibody produced in mouse is suitable for indirect immunofluorescence at a dilution of 1:50 and for western blotting at a dilution of 1:500.
Biochem/physiol Actions
Calpain plays an important role during cellular processes including cytoskeletal remodeling, apoptosis and survival. Calpain-2 over expression is significantly associated with platinum resistant tumours and in ovarian carcinomas may allow prognostic stratification of patients treated with surgery and platinum-based chemotherapy. Its over expression in basal-like or triple-negative disease is associated with adverse breast cancer-specific survival. m-calpain (calpain-2) is significantly associated with triple-negative and basal-like disease.
Epitope mapping studies indicate the epitope is between amino acids 502-699 (domain III/IV) of human m-calpain. The antibody reacts specifically with m-calpain. It does not cross-react with μ-calpain, n-calpain, calmodulin or calpastatin. It is not recommended for immunoprecipitation. By immunoblotting, reactivity is observed with human platelets and erythrocytes, bovine platelets, heart and skeletal muscle and with rat myoblasts, kidney, liver and spleen. By immunofluorescence on pig LLC-PK1 cells, diffuse cytoplasmic staining is observed.
Physical form
Solution containing 0.05% 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
nwg
flash_point_f
Not applicable
flash_point_c
Not applicable
ppe
Eyeshields, Gloves, multi-purpose combination respirator cartridge (US)
Regulatory Information
常规特殊物品
动植物来源生物产品
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Four genes for the calpain family locate on four distinct human chromosomes.
Ohno S, Minoshima S, Kudoh J, Fukuyama R, Shimizu Y, Ohmi-Imajoh S, Shimizu N, Suzuki K.
Cytogenetics and Cell Genetics (1990)
A Hata et al.
The Journal of biological chemistry, 264(11), 6404-6411 (1989-04-15)
Calcium-dependent protease (CANP, Calpain) is an intracellular protease involved in essential cellular functions mediated by calcium. To understand the mechanism regulating the expression of CANP at the transcriptional level, we isolated a human gene for the large subunit of mCANP
S Imajoh et al.
Biochemistry, 27(21), 8122-8128 (1988-10-18)
A nearly full-length cDNA clone for the large subunit of high-Ca2+-requiring Ca2+-activated neutral protease (mCANP) from human tissues has been isolated. The deduced protein, determined for the first time as an mCANP, has essentially the same structural features as those
Laura Tonnetti et al.
Cancer research, 68(14), 5648-5657 (2008-07-18)
The tumor suppressor retinoblastoma protein (Rb) plays a pivotal role in the regulation of cell proliferation and sensitivity to apoptosis through binding to E2F transcription factors. Loss of Rb in response to genotoxic stress or inflammatory cytokines can enhance cell
Honglin Chen et al.
The Journal of biological chemistry, 285(4), 2368-2374 (2009-12-01)
Androgen ablation therapy is effective in treating androgen-dependent prostate tumors; however, tumors that can proliferate in castrate levels of androgen eventually arise. We previously reported that in CWR22Rv1 (Rv1) cells, the protease calpain 2 can cleave the androgen receptor (AR)
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