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Merck
CN

C0355

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

clone 15C10, purified immunoglobulin

Synonym(s):

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

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About This Item

MDL number:
MFCD03457564
UNSPSC Code:
12352203
NACRES:
NA.41

Key Documents

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biological source

mouse

Quality Level

200

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

Gene Information

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

Related Categories

Immunogen

purified calpain from human placenta.

Physical form

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

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 Code

10 - Combustible liquids

WGK

WGK 2

Flash Point(F)

Not applicable

Flash Point(C)

Not applicable

Regulatory Information

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Certificates of Analysis (COA)

Lot/Batch Number
SLCQ3344
SLCB7537
SLCB0806
SLBV8775
SLBR3780V

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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
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
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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