Product Pathways - MAPK Signaling
HSP27 Antibody (Rodent Preferred) #2442
|2442S||100 µl (10 western blots)||---||In Stock||---|
|2442||carrier free and custom formulation / quantity||email request|
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Species cross-reactivity is determined by western blot.
Applications Key: W=Western Blotting, IF-IC=Immunofluorescence (Immunocytochemistry), F=Flow Cytometry
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 animals with a synthetic peptide corresponding to rat HSP27. Antibodies are purified by protein A and peptide affinity chromatography.
Western blot analysis of extracts from C2C12, PC12, HeLa and COS cells using HSP27 Antibody (Rodent Preferred).
Flow cytometric analysis of C2C12 cells using HSP27 Antibody (Rodent Preferred) (blue) compared to a nonspecific negative control antibody (red).
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® #4084 (fluorescent DNA dye).
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 HSPs, HSP27 is regulated at both the transcriptional and posttranslational levels (1). In response to stress, the HSP27 expression increases several-fold to confer cellular resistance to the adverse environmental change. HSP27 is phosphorylated at Ser15, Ser78, and Ser82 by MAPKAPK-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).
- Arrigo, A.P. and Landry, J. (1994) Cold Spring Harbor Laboratory Press, NY, 335-373.
- Landry, J. et al. (1992) J. Biol. Chem. 267, 794-803.
- Rouse, J. et al. (1994) Cell 78, 1027-1037.
- Rogalla, T. et al. (1999) J. Biol. Chem. 274, 18947-18956.
- Lavoie, J. et al. (1993) J. Biol. Chem. 268, 24210-24214.
- Rousseau, S. et al. (1997) Oncogene 15, 2169-2177.
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For Research Use Only. Not For Use In Diagnostic Procedures.
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