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C5736

Sigma-Aldrich

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

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

biological source

mouse

Quality Level

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

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.

Specificity

Specifically recognizes the 80 kDa subunit of μ-calpain as well as two smaller proteins that are presumed to be degradation products.

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).

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 Code

10 - Combustible liquids

WGK

WGK 1

Flash Point(F)

Not applicable

Flash Point(C)

Not applicable

Personal Protective Equipment

dust mask type N95 (US), Eyeshields, Gloves

Certificates of Analysis (COA)

Search for Certificates of Analysis (COA) by entering the products Lot/Batch Number. Lot and Batch Numbers can be found on a product’s label following the words ‘Lot’ or ‘Batch’.

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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
Wei Cui et al.
Cell & bioscience, 5, 36-36 (2015-07-07)
Under inflammatory conditions or during tumor progression macrophages acquire distinct phenotypes, with factors of the microenvironment such as hypoxia and transforming growth factor β (TGFβ) shaping their functional plasticity. TGFβ is among the factors causing alternative macrophage activation, which contributes

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