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C0355

Sigma-Aldrich

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

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)

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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WGK

WGK 2

Flash Point(F)

Not applicable

Flash Point(C)

Not applicable

Regulatory Information

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Certificates of Analysis (COA)

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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
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
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
Ryo Takagi et al.
Physiological reports, 6(6), e13660-e13660 (2018-03-30)
Past contraction-induced skeletal muscle injury reduces the degree of subsequent injury; this phenomenon is called the "repeated bout effect (RBE)." This study addresses the mechanisms underlying the RBE, focusing on primary calcium-dependent injury pathways. Wistar rats were subdivided into single
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