C0355

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

Name: Monoclonal Anti-μ-Calpain, Large Subunit antibody produced in mouse
Brand: SIGMA

clone 15C10, purified immunoglobulin

Sinónimos:

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

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About This Item

UNSPSC Code:

12352203

NACRES:

NA.41

MDL number:

MFCD03457564

Nombre del producto

Monoclonal Anti-μ-Calpain, Large Subunit antibody produced in mouse, clone 15C10, purified immunoglobulin

biological source

mouse

conjugate

unconjugated

antibody form

purified immunoglobulin

antibody product type

primary antibodies

clone

15C10, monoclonal

mol wt

antigen 80 kDa

species reactivity

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

UniProt accession no.

P07384

shipped in

wet ice

storage temp.

−20°C

target post-translational modification

unmodified

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.

Immunogen

purified calpain from human placenta.

Physical form

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

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Clase de almacenamiento

10 - Combustible liquids

wgk

WGK 2

flash_point_f

Not applicable

flash_point_c

Not applicable

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mu-Calpain and calpain-3 are not autolyzed with exhaustive exercise in humans.

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

Involvement of calpains in Ca2+-induced disruption of excitation-contraction coupling in mammalian skeletal muscle fibers.

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

l-arginine ingestion inhibits eccentric contraction-induced proteolysis and force deficit via S-nitrosylation of calpain.

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

Skeletal muscle atrophy in sedentary Zucker obese rats is not caused by calpain-mediated muscle damage or lipid peroxidation induced by oxidative stress.

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

Regional differences in Ca2+ entry along the proximal-middle-distal muscle axis during eccentric contractions in rat skeletal muscle.

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

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