|Tested applications||WB IHC IF|
|Recommended Dilution||WB 1:500 - 1:2000
IHC 1:50 - 1:200
IF 1:50 - 1:200|
|Observed MW||Refer to Figures|
|Immunogen||A phospho specific peptide corresponding to residues surrounding S82 of human HSPB1|
|Storage Buffer||Store at -20℃. Avoid freeze / thaw cycles.
Buffer: PBS with 0.02% sodium azide, 50% glycerol, pH7.3.|
|Synonym||CMT2F; HMN2B; HSP27; HSP28; Hsp25; SRP27; HS.76067; DKFZp586P1322|
Western blot analysis of extracts of HeLa cell line, using Phospho-HSPB1-S82 antibody.
Immunofluorescence analysis of U2OS cell using Phospho-HSPB1-S82 antibody. Blue: DAPI for nuclear staining.
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).
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