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Merck
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Principaux documents

C0355

Sigma-Aldrich

Monoclonal Anti-μ-Calpain, Large Subunit antibody produced in mouse

clone 15C10, purified immunoglobulin

Synonyme(s) :

Anti-CANP, Anti-CANP1, Anti-CANPL1, Anti-SPG76, Anti-muCANP, Anti-muCL

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About This Item

Numéro MDL:
Code UNSPSC :
12352203
Nomenclature NACRES :
NA.41

Source biologique

mouse

Niveau de qualité

Conjugué

unconjugated

Forme d'anticorps

purified immunoglobulin

Type de produit anticorps

primary antibodies

Clone

15C10, monoclonal

Poids mol.

antigen 80 kDa

Espèces réactives

rat, mouse, human, bovine

Technique(s)

immunoprecipitation (IP): 1-2 μg
indirect ELISA: 0.5-1 μg/mL
western blot: 0.5-1 μg/mL

Numéro d'accès UniProt

Conditions d'expédition

wet ice

Température de stockage

−20°C

Modification post-traductionnelle de la cible

unmodified

Informations sur le gène

human ... CAPN1(823)
mouse ... Capn1(12333)

Immunogène

purified calpain from human placenta.

Forme physique

Solution containing phosphate buffered saline, ≤ 0.1% sodium azide and 50% glycerol.

Clause de non-responsabilité

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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Code de la classe de stockage

10 - Combustible liquids

Classe de danger pour l'eau (WGK)

WGK 2

Point d'éclair (°F)

Not applicable

Point d'éclair (°C)

Not applicable


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Consulter la Bibliothèque de documents

Robyn M Murphy et al.
American journal of physiology. Cell physiology, 290(1), C116-C122 (2005-08-19)
mu-Calpain and calpain-3 are Ca2+-dependent proteases found in skeletal muscle. Autolysis of calpains is observed using Western blot analysis as the cleaving of the full-length proteins to shorter products. Biochemical assays suggest that mu-calpain becomes proteolytically active in the presence
Esther Verburg et al.
American journal of physiology. Cell physiology, 296(5), C1115-C1122 (2009-03-20)
In skeletal muscle fibers, the coupling between excitation of the surface membrane and the release of Ca(2+) from the sarcoplasmic reticulum is irreversibly disrupted if cytoplasmic Ca(2+) concentration ([Ca(2+)]) is raised to micromolar levels for a prolonged period. This excitation-contraction
Keita Kanzaki et al.
Physiological reports, 6(2) (2018-01-26)
It has been shown that calpains are involved in the proteolysis of muscle proteins that occurs with eccentric contraction (ECC) and that exogenously applied nitric oxide decreases the calpain-mediated proteolysis. The aim of this study was to examine the effects
Ayaka Tabuchi et al.
Journal of applied physiology (Bethesda, Md. : 1985), 127(3), 828-837 (2019-08-02)
Eccentric (ECC) contraction-induced muscle damage is associated with calcium ion (Ca2+) influx from the extracellular milieu through stretch-activated channels. It remains unknown whether Ca2+ influx consequent to repetitive ECC contractions is nonuniform across different muscle regions. We tested the hypothesis
Nancy Pompeani et al.
Journal of negative results in biomedicine, 13, 19-19 (2014-12-31)
Skeletal muscle undergoes significant atrophy in Type 2 diabetic patients and animal models. We aimed to determine if atrophy of Zucker rat skeletal muscle was due to the activation of intracellular damage pathways induced by excess reactive oxygen species production

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