C267
Monoclonal Anti-μ-Calpain (Domain II) antibody produced in mouse
clone 2H2A7C2, ascites fluid
Product Name
Monoclonal Anti-μ-Calpain (Domain II) antibody produced in mouse, clone 2H2A7C2, ascites fluid
biological source
mouse
conjugate
unconjugated
antibody form
ascites fluid
antibody product type
primary antibodies
clone
2H2A7C2, monoclonal
mol wt
antigen 80 kDa
species reactivity
pig, rat, bovine, human
technique(s)
indirect immunofluorescence: 1:25
western blot: 1:1,000
isotype
IgG1
UniProt accession no.
shipped in
dry ice
storage temp.
−20°C
Quality Level
Gene Information
human ... CAPN1(823)
rat ... Capn1(29153)
Application
Monoclonal Anti-μ-Calpain (Domain II) antibody produced in mouse is suitable for indirect immunofluorescence at a dilution of 1:25 and western blotting at a dilution of 1:1000.
Biochem/physiol Actions
Calpain is involved in calmodulin-independent pathway for the activation of calcineurin. Endogenous calpain I forms active calcineurin in the human heart by proteolysis of calcineurin A, which may lead to pathogenesis of myocardial disease. μ-calpain, on overexpression, may have relationship with intractable epilepsy as well as the clinicopathological characteristics in such patients. Its activity may increase in skeletal muscle of gastric cancer patients.
Epitope mapping studies indicate the epitope is between amino acids 245-265 (domain II) of human μ-calpain. The antibody reacts specifically with μ-calpain. It does not cross-react with m-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.
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.
General description
Calpain-1 catalytic subunit is a protein encoded by the CAPN1 gene in humans. Calpains are calcium dependent proteases constituting a family of proteins. 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
μ-calpain from bovine skeletal muscle.
Physical form
Solution containing 0.05% sodium azide
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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
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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)
Takayuki Wakasugi et al.
PloS one, 14(2), e0212889-e0212889 (2019-02-27)
Pulmonary arterial hypertension (PAH) is characterized by remodeling and narrowing of the pulmonary arteries, which lead to elevation of right ventricular pressure, heart failure, and death. Proliferation of pulmonary artery smooth muscle cells (PASMCs) is thought to be central to
Zhan-hui Feng et al.
Seizure, 20(5), 395-401 (2011-02-15)
This study aims to investigate μ-calpain expression profiles in the anterior temporal neocortex in patients with intractable epilepsy, and to determine whether its pattern of expression is related to pathological changes seen in these patients. The study subjects consisted of
Bharathi Govindarajan et al.
Biochemistry, 47(2), 817-825 (2007-12-19)
We report that protein adducts of iso[4]levuglandin E2 (iso[4]LGE2), a highly reactive product of free radical-induced lipid oxidation, accumulate in human glaucomatous trabecular meshwork (TM) but not in controls. Reactive oxygen species play a pathogenic role in primary open angle
Jian-Chun Wang et al.
Clinical laboratory, 58(11-12), 1145-1152 (2013-01-08)
The calmodulin-independent pathway is thought to involve the activation of calcineurin by calpain. However, the effect of endogenous calpain on calcineurin in human heart is not well known. Proteolysis and activation of recombinant calcineurin by purified calpain isozymes I and
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