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AB81023

Sigma-Aldrich

Anti-Calpain II Antibody, large subunit

Chemicon®, from rabbit

Synonym(s):

M-Calpain, Calpain 2

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About This Item

UNSPSC Code:
12352203
eCl@ss:
32160702
NACRES:
NA.41

biological source

rabbit

Quality Level

antibody form

affinity purified immunoglobulin

antibody product type

primary antibodies

clone

polyclonal

purified by

affinity chromatography

species reactivity

mouse, rat, human

manufacturer/tradename

Chemicon®

technique(s)

western blot: suitable

NCBI accession no.

UniProt accession no.

shipped in

wet ice

target post-translational modification

unmodified

Gene Information

human ... CAPN2(824)

General description

Calpains are cytosolic, calcium-dependent, cysteine proteases that are ubiquitously expressed in mammalian and avian tissues. Calpain-1 and 2 consist of a common small subunit and a large variable subunit. Domains in the large subunit include the amino terminal domain I, the proteinase domain II, domain III, and the EF-hand domain IV.
Type I calpain requires micromolar amounts of calcium, while type II calpain requires millimolar amounts of calcium.

Specificity

The anti-calpain II antibody recognizes the 80 kDa and 58 kDa forms of Calpain II. It does not cross-react with other calpains.

Immunogen

Epitope: large subunit

Application

Anti-Calpain II Antibody, large subunit is an antibody against Calpain II for use in WB.
Research Category
Cell Structure
Research Sub Category
Cytoskeleton
Western blot: 1:1000 for colorimetric substrates or 1:5000 for chemiluminescent substrates (recommended starting concentration).

Optimal working dilutions must be determined by the end user.

Physical form

Affinity purified immunoglobulin. Liquid in PBS pH 7.4 containing 1% BSA and 50% glycerol as a stabilizer.

Storage and Stability

Maintain at -20*C in undiluted aliquots for up to 6 months after date of receipt. Avoid repeated freeze/thaw cycles.

Other Notes

Concentration: Please refer to the Certificate of Analysis for the lot-specific concentration.

Legal Information

CHEMICON is a registered trademark of Merck KGaA, Darmstadt, Germany

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 2


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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Calpain cleavage and inactivation of the sodium calcium exchanger-3 occur downstream of A? in Alzheimer's disease.
Atherton, J; Kurbatskaya, K; Bondulich, M; Croft, CL; Garwood, CJ; Chhabra, R; Wray et al.
Aging Cell null
Shruthi Shanmukha et al.
Disease models & mechanisms, 11(4) (2018-04-19)
Skeletal muscle atrophy is the most prominent feature of amyotrophic lateral sclerosis (ALS), an adult-onset neurodegenerative disease of motor neurons. However, the contribution of skeletal muscle to disease progression remains elusive. Our previous studies have shown that intrathecal injection of
Jasvir Kaur et al.
PloS one, 6(7), e22181-e22181 (2011-07-19)
Retinitis pigmentosa (RP) is a heterogeneous group of inherited neurodegenerative diseases affecting photoreceptors and causing blindness. Many human cases are caused by mutations in the rhodopsin gene. An important question regarding RP pathology is whether different genetic defects trigger the
N-methyl-D-aspartate receptor- and calpain-mediated proteolytic cleavage of K+-Cl- cotransporter-2 impairs spinal chloride homeostasis in neuropathic pain.
Zhou, HY; Chen, SR; Byun, HS; Chen, H; Li, L; Han, HD; Lopez-Berestein, G; Sood, AK; Pan, HL
The Journal of Biological Chemistry null
Vanessa Plantier et al.
eLife, 8 (2019-12-10)
Up-regulation of the persistent sodium current (INaP) and down-regulation of the potassium/chloride extruder KCC2 lead to spasticity after spinal cord injury (SCI). We here identified calpain as the driver of the up- and down-regulation of INaP and KCC2, respectively, in

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