产品名称
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.
shipped in
wet ice
storage temp.
−20°C
target post-translational modification
unmodified
Quality Level
Gene Information
human ... CAPN1(823)
mouse ... Capn1(12333)
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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存储类别
10 - Combustible liquids
wgk
WGK 2
flash_point_f
Not applicable
flash_point_c
Not applicable
法规信息
常规特殊物品
此项目有
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
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
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
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