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C3114

Sigma-Aldrich

Anti-Calpain-13 (Domain III, N-Terminal), Large Subunit antibody produced in rabbit

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

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About This Item

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

biological source

rabbit

Quality Level

conjugate

unconjugated

antibody form

affinity isolated antibody

antibody product type

primary antibodies

clone

polyclonal

form

buffered aqueous glycerol solution

species reactivity

rat, human, mouse

concentration

~1 mg/mL

technique(s)

immunohistochemistry: suitable
immunoprecipitation (IP): suitable
indirect ELISA: suitable
western blot: 1:1,000

UniProt accession no.

shipped in

wet ice

storage temp.

−20°C

Gene Information

General description

Calpains are calcium-activated, non-lysosomal cysteine proteases that cleave cytoskeletal and submembranous proteins. It is an intracellular cysteine protease that is present in all mammalian tissues. Anti-Calpain-13 (Domain I, N-Terminal), Large Subunit is developed in rabbit using a synthetic peptide corresponding to domain I of the large subunit of human calpain 13 (capn-13) as immunogen. The antibody is affinity purified using agarose to which the immunogen peptide has been bound.

Immunogen

synthetic peptide corresponding to domain III of the large subunit of human calpain 13.

Application

Anti-Calpain-13 is suitable for immunohistochemistry, immunoprecipitation and indirect ELISA. It is also suitable for western blot at a dilution of 1:1,000

Biochem/physiol Actions

Calpains are involved in a variety of processes including cytoskeletal reorganization, muscle protein degradation, cell proliferation, differentiation, and vesicular secretion. Anti-Calpain-13 (Domain I, N-Terminal), Large Subunit recognizes domain I in the large subunit of human calpain 13 by various immunochemical techniques including immunoblotting, immunoprecipitation, immunohistochemistry, and ELISA. It detects human, rat, and mouse calpain 13 and does not crossreact with other calpain family members (calpain 1, calpain 2, calpain 3, etc.). The antibody binds to the reduced and non-reduced protein. By immunoblotting against the reduced protein, the antibody identifies bands at approximately 64 kDa, 52 kDa, 48 kDa, 40 kDa, and aseries of smaller forms.

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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Storage Class

10 - Combustible liquids


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S Kulkarni et al.
The Journal of biological chemistry, 274(30), 21265-21275 (1999-07-20)
Integrin-induced adhesion leads to cytoskeletal reorganizations, cell migration, spreading, proliferation, and differentiation. The details of the signaling events that induce these changes in cell behavior are not well understood but they appear to involve activation of Rho family members which
D Stockholm et al.
Experimental cell research, 252(2), 392-400 (1999-10-21)
We have synthesized dextran derivatives called RGTAs (for regenerating agents) that were designed to mimic some of the properties of heparin or heparan sulfate to interact with and protect heparin binding growth factors. Some of these growth factors have been
S S Murray et al.
Experimental cell research, 233(2), 297-309 (1997-06-15)
The calpain-calpastatin system, which consists of calpains I and II (two ubiquitously distributed calcium-activated papain-like cysteine proteases), as well as calpastatin (the endogenous calpain inhibitor), plays an important role in cell proliferation and differentiation in many tissues. However, its contribution
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

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