C5736
Monoclonal Anti-μ-Calpain (Calpain I, subunit p80) antibody produced in mouse
clone 15C10, purified immunoglobulin, buffered aqueous glycerol solution
Synonym(s):
Anti-CANP, Anti-CANP1, Anti-CANPL1, Anti-SPG76, Anti-muCANP, Anti-muCL
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About This Item
Conjugate:
unconjugated
Clone:
15C10, monoclonal
Application:
ELISA (i), IP, WB CL
Citations:
10
biological source
mouse
conjugate
unconjugated
antibody form
purified immunoglobulin
antibody product type
primary antibodies
clone
15C10, monoclonal
form
buffered aqueous glycerol solution
species reactivity
bovine, mouse, rat, human
technique(s)
immunoprecipitation (IP): 2-5 μL (native and denaturing conditions), indirect ELISA: suitable, western blot (chemiluminescent): 1:1,000
isotype
IgG1
UniProt accession no.
shipped in
wet ice
storage temp.
−20°C
Quality Level
Gene Information
human ... CAPN1(823), CAPNS1(826)
mouse ... Capn1(12333), Capns1(12336)
rat ... Capn1(29153), Capns1(29156)
General description
Calpain-1 (CAPN1), an intracellular, calcium-dependent cysteine protease, has four domains, such as, the N-terminal anchor helix region, the CysPc protease domain, the C2 domain-like domain and the penta-EF-hand domain (PEF). CAPN1 codes for μ-calpain protein. CAPN1 gene is abundantly expressed in the central nervous system (CNS). This gene is located on human chromosome 11q13.1.
Immunogen
purified human μ-calpain from placenta (calpain-I, protein kinase-C activating factor, E.C. 3.4.22.17).
Application
Monoclonal Anti-μ-Calpain (Calpain I, subunit p80) antibody produced in mouse has been used in:
- western blotting
- co-immunoprecipitation
- immunofluorescence
- immunofluorescence staining
Biochem/physiol Actions
Calpain-1 (CAPN1) plays a key role in microtubular regulation, cerebellar development, synaptic plasticity, synaptic restructuring, axon maturation and maintenance. CAPN1 activation is essential to provide a neuro-protective role in central nervous system (CNS). Mutations on CAPN1 gene results in spastic paraplegia 76 (SPG7), a complicated form of hereditary spastic paraplegia (HSP).
Specifically recognizes the 80 kDa subunit of μ-calpain as well as two smaller proteins that are presumed to be degradation products.
Physical form
Solution in 20 mM sodium phosphate, 150 mM sodium chloride, 50% glycerol, pH 7.5, and 3 mM sodium azide.
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
10 - Combustible liquids
wgk
WGK 1
flash_point_f
Not applicable
flash_point_c
Not applicable
ppe
Eyeshields, Gloves, multi-purpose combination respirator cartridge (US)
Regulatory Information
常规特殊物品
低风险生物材料
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Aakash Shetty et al.
European journal of medical genetics, 62(12), 103605-103605 (2018-12-21)
To characterize the phenotype of CAPN1 (SPG76) mutations in patients diagnosed with hereditary spastic paraplegia (HSP). The CAPN1 gene, located on chromosome 11q13.1, is a protein-coding gene involved in neuronal plasticity, migration, microtubular regulation and cerebellar development. Several families with
Fang Peng et al.
Orphanet journal of rare diseases, 14(1), 83-83 (2019-04-27)
Hereditary spastic paraplegias (HSP) are of great clinical and genetic heterogeneity. According to the clinical features, HSP can be divided into pure or complicated subtypes which combined with other neurological symptoms including cerebellar ataxia. Up to date, 78 loci or
Bruno A Cisterna et al.
Biochimica et biophysica acta, 1862(11), 2168-2176 (2016-09-01)
Denervated fast skeletal muscles undergo atrophy, which is associated with an increase in sarcolemma permeability and protein imbalance. However, the mechanisms responsible for these alterations remain largely unknown. Recently, a close association between de novo expression of hemichannels formed by
Monica Averna et al.
Biochimica et biophysica acta, 1812(12), 1649-1657 (2011-10-11)
We are here reporting that in peripheral blood mononuclear cells (PBMC) of patients homozygous for F508del-CFTR the calpain-calpastatin system undergoes a profound alteration. In fact, calpain basal activity, almost undetectable in control PBMC, becomes measurable at a significant extent in
Christian Giordano et al.
PloS one, 10(6), e0131068-e0131068 (2015-06-25)
Short-term intermittent hypoxia (IH) is common in patients with acute respiratory disorders. Although prolonged exposure to hypoxia induces atrophy and increased fatigability of skeletal muscle, the response to short-term IH is less well known. We hypothesized that the diaphragm and
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