Cell Signaling Technology

Product Pathways - MAPK Signaling

Phospho-HSP27 (Ser15) Antibody #2404

Applications Reactivity MW (kDa) Source
W H Mk 27 Rabbit

Applications Key:  W=Western Blotting
Reactivity Key:  H=Human  Mk=Monkey
Species enclosed in parentheses are predicted to react based on 100% sequence homology. Species cross-reactivity is determined by Western blot.

Specificity / Sensitivity

Phospho-HSP27 (Ser15) Antibody detects endogenous levels of HSP27 only when phosphorylated at serine 15.

Source / Purification

Polyclonal antibodies are produced by immunizing rabbits with a synthetic phosphorylated peptide (KLH-coupled) corresponding to residues surrounding Ser15 of human HSP27. Antibodies are purified by protein A and peptide affinity chromatography.

Western Blotting

Western Blotting

Western blot analysis of extracts from HeLa and COS cells, untreated, anisomycin-treated or UV-treated, using Phospho-HSP27 (Ser15) Antibody (upper) or HSP27 (G31) Monoclonal Antibody #2402 (lower).

Background

Heat shock protein (HSP) 27 is one of the small HSPs that are constitutively expressed at different levels in various cell types and tissues. Like other small heat shock proteins, HSP27 is regulated at both the transcriptional and posttranslational levels (1). In response to stress, the expression level of HSP27 increases several-fold to confer cellular resistance to the adverse environmental change. HSP27 is phosphorylated at Ser15, Ser78 and Ser82 by MAPKAP kinase 2 as a result of the activation of the p38 MAP kinase pathway (2,3). Phosphorylation of HSP27 causes a change in its tertiary structure, which shifts from large homotypic multimers to dimers and monomers (4). It has been shown that phosphorylation and increased concentration of HSP27 modulates actin polymerization and reorganization (5,6).

  1. Arrigo, A.P. and Landry, J. (1994) Cold Spring Harbor Laboratory Press, NY, 335-373.
  2. Landry, J. et al. (1992) J. Biol. Chem. 267, 794-803.
  3. Rouse, J. et al. (1994) Cell 78, 1027-1037.
  4. Rogalla, T. et al. (1999) J. Biol. Chem. 274, 18947-18956.
  5. Lavoie, J. et al. (1993) J. Biol. Chem. 268, 24210-24214.
  6. Rousseau, S. et al. (1997) Oncogene 15, 2169-2177.

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