Product Pathways - MAPK Signaling
Phospho-HSP27 (Ser82) Antibody II #2406
|W IHC-P IHC-F IF-IC F||H M R Mk||Endogenous||27||Rabbit|
Reactivity Key: H=Human M=Mouse R=Rat Mk=Monkey
Species cross-reactivity is determined by western blot. Species enclosed in parentheses are predicted to react based on 100% sequence homology.
Specificity / Sensitivity
Phospho-HSP27 (Ser82) Antibody II detects endogenous HSP27 only when phosphorylated at Ser82. The antibody does not recognize other heat shock proteins.
Source / Purification
Polyclonal antibodies are produced by immunizing animals with a synthetic phosphopeptide corresponding to residues surrounding Ser82 of human HSP27. Antibodies are purified by protein A and peptide affinity chromatography.
Western blot analysis of extracts from HeLa and PC12 cells, treated with λ-phosphatase or UV as indicated, using Phospho-HSP27 (Ser82) Antibody II.
Immunohistochemical analysis of paraffin-embedded human lung carcinoma using Phospho-HSP27 (Ser82) Antibody II.
Immunohistochemical analysis of paraffin-embedded human melanoma using Phospho-HSP27 (Ser82) Antibody II.
Immunohistochemical analysis of frozen H1650 xenograft using Phospho-HSP27 (Ser82) Antibody II.
Flow cytometric analysis of HeLa cells, untreated (blue) or UV-treated (green), using Phospho-HSP27 (Ser82) Antibody II.
Confocal immunofluorescent analysis of HeLa cells, untreated (left) or anisomycin-treated (right), using Phospho-HSP27 (Ser82) Antibody II (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.