Phospho-HSP27 (Ser82) Antibody detects endogenous HSP27 only when phosphorylated at serine 82. The antibody does not recognize other heat shock proteins.
Source / Purification
Polyclonal antibodies are produced by immunizing animals with a synthetic phospho- peptide corresponding to residues surrounding Ser82 of human HSP27. Antibodies are purified by protein A and peptide affinity chromatography.
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).