By immunoblotting against the reduced protein, the antibody reacts with bands at 80 kDa and 58 kDa and a series of further cleaved active forms. It also reacts with non-reduced m-calpain. The antibody does not cross-react with other calpain family members (μ-calpain, calpain-94, ncl-2, ncl-3, etc.).
Immunogen
synthetic peptide corresponding to the N-terminal of the domain-III in the large subunit of rat m-calpain (E.C. 3.4.22.17, calpain-II, protein kinase-C activating factor).
Application
Anti-m-Calpain (Domain III), Large Subunit antibody produced in rabbit is suitable for western blotting at a working dilution of 1:1,000 using an alkaline phosphatase conjugated secondary antibody and BCIP/NBT as substrate.
Biochem/physiol Actions
The calpains are calcium-activated non-lysosomal thiolproteases. m-Calpain is called as calpain-II. It is an intracellular, Ca2+-dependent cysteine protease. m- and μ-calpain are ubiquitously expressed and are countered by the endogenous calpain inhibitor calpastatin. The calpain family members are heterodimers. Calpains are present in all mammalian tissues and are involved in a variety of processes including cell proliferation, differentiation, vesicle secretion and others.
Physical form
Solution in 0.01 M phosphate buffered saline, pH 7.4, containing 50% glycerol, 1% BSA and 0.02% sodium azide
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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.
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
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
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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