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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

Synonyme(s) :

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

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About This Item

Numéro MDL:
MFCD03455420
Code UNSPSC :
12352203
Nomenclature NACRES :
NA.41

Source biologique

mouse

Niveau de qualité

200

Conjugué

unconjugated

Forme d'anticorps

purified immunoglobulin

Type de produit anticorps

primary antibodies

Clone

15C10, monoclonal

Forme

buffered aqueous glycerol solution

Espèces réactives

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

Numéro d'accès UniProt

P07384

Conditions d'expédition

wet ice

Température de stockage

−20°C

Informations sur le gène

human ... CAPN1(823) , CAPNS1(826)
mouse ... Capn1(12333) , Capns1(12336)
rat ... Capn1(29153) , Capns1(29156)

Description générale

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.

Spécificité

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

Immunogène

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[1][2]
  • co-immunoprecipitation
  • immunofluorescence
  • immunofluorescence staining[3]

Actions biochimiques/physiologiques

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).

Forme physique

Solution in 20 mM sodium phosphate, 150 mM sodium chloride, 50% glycerol, pH 7.5, and 3 mM sodium azide.

Clause de non-responsabilité

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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Code de la classe de stockage

10 - Combustible liquids

Classe de danger pour l'eau (WGK)

WGK 1

Point d'éclair (°F)

Not applicable

Point d'éclair (°C)

Not applicable

Équipement de protection individuelle

Eyeshields, Gloves, multi-purpose combination respirator cartridge (US)

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Certificats d'analyse (COA)

Lot/Batch Number
SLCH3147
SLBX5491
SLBT9007
SLBM7763V
SLBD6290V

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Retrouvez la documentation relative aux produits que vous avez récemment achetés dans la Bibliothèque de documents.

Consulter la Bibliothèque de documents

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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