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C6361

Sigma-Aldrich

Anti-Calpain-94 (Domain II, Insert 1), Large Subunit antibody produced in rabbit

~1 mg/mL, buffered aqueous glycerol solution, affinity isolated antibody

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About This Item

MDL number:
UNSPSC Code:
12352203

biological source

rabbit

conjugate

unconjugated

antibody form

affinity isolated antibody

antibody product type

primary antibodies

clone

polyclonal

form

buffered aqueous glycerol solution

species reactivity

human

concentration

~1 mg/mL

technique(s)

immunohistochemistry (frozen sections): suitable
immunoprecipitation (IP): suitable
indirect ELISA: suitable
western blot (chemiluminescent): 1:5,000
western blot: 1:1,000

UniProt accession no.

shipped in

wet ice

storage temp.

−20°C

target post-translational modification

unmodified

Gene Information

human ... CAPN3(825)

Specificity

Recognizes latent and active calpain-94. Binds the reduced and non-reduced protein. Identifies bands at 94 kDa, 82 kDa, 62 kDa, 60 kDa, and a series of further cleaved active forms. The rat 88 kDa and 90 kDa calpains also contain insert 1, so the antibody may cross-react with these forms.

Immunogen

synthetic peptide corresponding to insert 1 in domain-II of the large subunit of human calpain-94 (calpain-3, nCANP, nCL-1, calpain p94, muscle calpain).

Application

Anti-Calpain-94 (Domain II, Insert 1), Large Subunit antibody produced in rabbit is suitable for the following applications:
  • Immunohistochemistry (frozen sections)
  • Immunoprecipitation
  • Indirect ELISA
  • Western blot (chemiluminescent) at a dilution of 1:5,000
  • Western blotting at a dilution of 1:1,000
Applications in which this antibody has been used successfully, and the associated peer-reviewed papers, are given below.
Western Blotting (1 paper)

Biochem/physiol Actions

Calpain is a heterodimer consisting of a larger and a smaller subunit. It is a major intracellular protease. Calpains are a family of calcium-dependent thiol-proteases, which are involved in many physiological processes and pathological conditions. These are calcium-activated non-lysosomal thiolproteases. m- and μ-calpain are ubiquitously expressed and are countered by the endogenous calpain inhibitor calpastatin. Calpains are present in all mammalian tissues and are involved in a variety of processes including cell proliferation, differentiation, vesicle secretion and others. It is also likely to be involved in processing of numerous enzymes and cytoskeletal components by linking their activity to a variety of intracellular events.

Physical form

Solution in 0.01 M phosphate buffered saline containing 50% glycerol and 0.05% 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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X J Chi et al.
FEBS letters, 459(3), 391-394 (1999-10-20)
Proteolytic systems have various involvements in apoptotic pathways. To understand the role of calpain in apoptosis, calpastatin, a specific inhibitor of calpain, was overexpressed in human UV(r)-1 fibroblasts by transfection of its cDNA. The elevated expression of calpastatin resulted in
G V Johnson et al.
BioEssays : news and reviews in molecular, cellular and developmental biology, 19(11), 1011-1018 (1997-12-12)
Calpains are a family of calcium-dependent thiol-proteases which are proposed to be involved in many physiological processes as well as pathological conditions. Calpains are likely to be involved in processing of numerous enzymes and cytoskeletal components, thereby linking their activity
D Balcerzak et al.
Journal of cell science, 108 ( Pt 5), 2077-2082 (1995-05-01)
Previous studies have led to the hypothesis of a possible role for m-calpain (EC 3.4.22.17) in myoblast fusion in culture in vitro. To support this hypothesis, an antisense strategy has been used with cultured primary rat myoblasts. Using an appropriate
Tsubasa Shibaguchi et al.
Physiological reports, 4(15) (2016-08-03)
Astaxanthin is a carotenoid pigment and has been shown to be an effective inhibitor of oxidative damage. We tested the hypothesis that astaxanthin intake would attenuate immobilization-induced muscle atrophy in rats. Male Wistar rats (14-week old) were fed for 24 days
H Ariyoshi et al.
Arteriosclerosis, thrombosis, and vascular biology, 18(3), 493-498 (1998-03-26)
Vascular smooth muscle cell (VSMC) proliferation still remains a poorly understood process, although it is believed to play a critical role in pathological states, including atherosclerosis and hypertension. Several reports have suggested that proteases may be directly involved in this

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