C267
Monoclonal Anti-μ-Calpain (Domain II) antibody produced in mouse
clone 2H2A7C2, ascites fluid
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About This Item
origen biológico
mouse
Nivel de calidad
conjugado
unconjugated
forma del anticuerpo
ascites fluid
tipo de anticuerpo
primary antibodies
clon
2H2A7C2, monoclonal
mol peso
antigen 80 kDa
reactividad de especies
pig, rat, bovine, human
técnicas
indirect immunofluorescence: 1:25
western blot: 1:1,000
isotipo
IgG1
Nº de acceso UniProt
Condiciones de envío
dry ice
temp. de almacenamiento
−20°C
Información sobre el gen
human ... CAPN1(823)
rat ... Capn1(29153)
Descripción general
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).
Especificidad
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.
Inmunógeno
μ-calpain from bovine skeletal muscle.
Aplicación
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.
Acciones bioquímicas o fisiológicas
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.
Forma física
Solution containing 0.05% sodium azide
Cláusula de descargo de responsabilidad
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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Código de clase de almacenamiento
10 - Combustible liquids
Clase de riesgo para el agua (WGK)
nwg
Punto de inflamabilidad (°F)
Not applicable
Punto de inflamabilidad (°C)
Not applicable
Equipo de protección personal
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. Sigma-Aldrich.com
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