C267
Monoclonal Anti-μ-Calpain (Domain II) antibody produced in mouse
clone 2H2A7C2, ascites fluid
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About This Item
Origine biologica
mouse
Livello qualitativo
Coniugato
unconjugated
Forma dell’anticorpo
ascites fluid
Tipo di anticorpo
primary antibodies
Clone
2H2A7C2, monoclonal
PM
antigen 80 kDa
Reattività contro le specie
pig, rat, bovine, human
tecniche
indirect immunofluorescence: 1:25
western blot: 1:1,000
Isotipo
IgG1
N° accesso UniProt
Condizioni di spedizione
dry ice
Temperatura di conservazione
−20°C
Informazioni sul gene
human ... CAPN1(823)
rat ... Capn1(29153)
Descrizione generale
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).
Specificità
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.
Immunogeno
μ-calpain from bovine skeletal muscle.
Applicazioni
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.
Azioni biochim/fisiol
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.
Stato fisico
Solution containing 0.05% sodium azide
Esclusione di responsabilità
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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Codice della classe di stoccaggio
10 - Combustible liquids
Classe di pericolosità dell'acqua (WGK)
nwg
Punto d’infiammabilità (°F)
Not applicable
Punto d’infiammabilità (°C)
Not applicable
Dispositivi di protezione individuale
Eyeshields, Gloves, multi-purpose combination respirator cartridge (US)
Certificati d'analisi (COA)
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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
Articoli
Quantitative and qualitative western blotting to validate knockdown by esiRNA. Sigma-Aldrich.com
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