Cell Signaling Technology

Product Pathways - Protein Folding/Stability

HSP27 Antibody (Rodent Preferred) #2442

Applications Reactivity MW (kDa) Source
W IF-IC F M R 27 Rabbit

Applications Key:  W=Western Blotting  IF-IC=Immunofluorescence (Immunocytochemistry)  F=Flow Cytometry
Reactivity Key:  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

HSP27 Antibody (Rodent Preferred) detects endogenous levels of total HSP27 protein. The antibody does not cross-react with other heat shock proteins.

Source / Purification

Polyclonal antibodies are produced by immunizing rabbits with a synthetic peptide (KLH-coupled) corresponding to rat HSP27. Antibodies are purified by protein A and peptide affinity chromatography.

Western Blotting

Western Blotting

Western blot analysis of extracts from C2C12, PC12, HeLa and COS cells using HSP27 Antibody (Rodent Preferred).

Flow Cytometry

Flow Cytometry

Flow cytometric analysis of C2C12 cells using HSP27 Antibody (Rodent Preferred) (blue) compared to a nonspecific negative control antibody (red).

IF-IC

IF-IC

Confocal immunofluorescent analysis of C2C12 cells using HSP27 Antibody (Rodent Preferred) (green). Actin filaments have been labeled with Alexa Fluor® 555 phalloidin (red). Blue pseudocolor = DRAQ5™ (fluorescent DNA dye).


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.

Application References

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