Calpain 2 Large Subunit (M-typ

2539:

Flow , Immunofluorescence , Immunoprecipitation , Western Blotting

Calpain 2 Large Subunit (M-type) Antibody detects endogenous levels of total calpain 2 (large subunit) protein. The antibody detects full-length calpain 2 as well as calpain 2 autoproteolytically cleaved at serine 20. The antibody does not detect recombinant calpain 1.

Polyclonal antibodies are produced by immunizing animals with a synthetic peptide corresponding to the human sequence of calpain 2 (large subunit). Antibodies are purified by protein A and peptide affinity chromatography.

Western Blotting

Western blot analysis of extracts from C2C12 and PC3 cells, using Calpain 2 Large Subunit (M-type) Antibody.

Flow Cytometry

Flow cytometric analysis of C2C12 cells, using Calpain 2 Large Subunit (M-type) Antibody (blue) compared to a nonspecific negative control antibody (red).

IF-F

Confocal immunofluorescent analysis of mouse retina using Calpain 2 Large Subunit (M-type) Antibody (red) and Phospho-Tyrosine Mouse mAb (P-Tyr-100) #9411 (green). Blue pseudocolor = DRAQ5^® #4084 (fluorescent DNA dye).

Calpain is a calcium-dependent thiol proteinase that is functionally active as a heterodimer composed of a small regulatory subunit and one of at least two large catalytic subunits (calpain 1 or calpain 2). In vitro, calpain 1 (mu-calpain) requires micromolar levels of calcium, while calpain 2 (M-calpain) requires millimolar levels of calcium for activation. The regulation of calpain in vivo is the subject of many current studies, which suggest that proteolytic activity is regulated post-transcriptionally by mechanisms such as calcium requirements, subcellular localization of the heterodimer, phosphorylation via the EGFR-Erk signaling cascade, endogenous inhibitors (calpastatin) and autoproteolytic cleavage (1). Calpastatin negatively regulates autoproteolytic cleavage of calpain 1 between Gly27 and Leu28 (2). Calpain influences cell migration by modifying rather than degrading its substrates responsible for cell adhesion and cytoskeletal arrangement. Control of calpain activity has caught the attention of drug development since limiting its activity could mute invasiveness of tumors or chronic inflammation (1).

1. Perrin, B.J. and Huttenlocher, A. (2002) Int. J. Biochem. Cell Biol. 34, 722-725.
2. Melloni, E. et al. (1996) Biochem. Biophys. Res. Commun. 229, 193-197.

• Beltran, L. et al. (2011) Proc Natl Acad Sci U S A 108, 16217-22. Applications: IP Western Blotting
• Pilop, C. et al. (2009) Circulation 120, 983-91. Applications: Western Blotting

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For Research Use Only. Not For Use In Diagnostic Procedures.