Cell Signaling Technology

Product Pathways - Protein Folding/Stability

Calpain 1 Large Subunit (Mu-type) Antibody #2556

Applications Reactivity MW (kDa) Source
W IF-F H M R 75, 80 Rabbit

Applications Key:  W=Western Blotting  IF-F=Immunofluorescence (Frozen)
Reactivity Key:  H=Human  M=Mouse  R=Rat
Species enclosed in parentheses are predicted to react based on 100% sequence homology. Species cross-reactivity is determined by Western blot.

Specificity / Sensitivity

Calpain 1 Large Subunit (Mu-type) Antibody detects endogenous levels of total calpain 1 (large subunit) protein. The antibody detects full-length calpain 1 as well as calpain 1 autoproteolytically cleaved at leucine 28.

Source / Purification

Polyclonal antibodies are produced by immunizing rabbits with a synthetic peptide (KLH-coupled) derived from the human sequence of calpain 1 (large subunit). Antibodies are purified by protein A and peptide affinity chromatography.

Western Blotting

Western Blotting

Western blot analysis of extracts from Jurkat and U937 cells, using Calpain 1 Large Subunit (Mu-type) Antibody.

Background

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.

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