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Key Documents

C267

Sigma-Aldrich

Monoclonal Anti-μ-Calpain (Domain II) antibody produced in mouse

clone 2H2A7C2, ascites fluid

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About This Item

MDL number:
UNSPSC Code:
12352203
NACRES:
NA.41

biological source

mouse

Quality Level

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

Gene Information

human ... CAPN1(823)
rat ... Capn1(29153)

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).

Specificity

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.

Immunogen

μ-calpain from bovine skeletal muscle.

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.

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_germany

nwg

flash_point_f

Not applicable

flash_point_c

Not applicable

ppe

Eyeshields, Gloves, multi-purpose combination respirator cartridge (US)


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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)
T Glaser et al.
Proceedings of the National Academy of Sciences of the United States of America, 91(17), 7879-7883 (1994-08-16)
Limited proteolysis by calpain (Ca(2+)-activated protease; EC 3.4.22.17) is believed to regulate the function of membrane enzymes and modify the behavior of membrane structural proteins. Calpain is activated by autolysis. The degradation of band 3 protein by mu-calpain is known
A Ravid et al.
Endocrinology, 135(6), 2822-2825 (1994-12-01)
mu-Calpain is a calcium-dependent neutral thiol protease activated by micromolar concentrations of calcium. mu-Calpain is implicated in various cellular functions regulated by calcium including exocytosis, cell fusion, apoptosis and control of cell proliferation. We studied the effect of 1,25-(OH)2D3 on
R W Neumar et al.
Journal of neurochemistry, 66(1), 421-424 (1996-01-01)
Proteolytic degradation of numerous calpain substrates, including cytoskeletal and regulatory proteins, has been observed during brain ischemia and reperfusion. In addition, calpain inhibitors have been shown to decrease degradation of these proteins and decrease postischemic neuronal death. Although these observations
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

Artículos

Quantitative and qualitative western blotting to validate knockdown by esiRNA.

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