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PhosphoSitePlus® Resource

  • Additional protein information
  • Analytical tools


Product Includes Quantity Applications Reactivity MW(kDa) Isotype
Phospho-HSP27 (Ser82) (D1H2F6) XP® Rabbit mAb 9709 20 µl
Western Blotting Immunohistochemistry Immunofluorescence Flow Cytometry
H M 27 Rabbit IgG
HSP27 (G31) Mouse mAb 2402 20 µl
Western Blotting Immunohistochemistry Immunofluorescence
H Mk 27 Mouse IgG1
Phospho-HSP27 (Ser15) Antibody 2404 20 µl
Western Blotting
H Mk 27 Rabbit 
Phospho-HSP27 (Ser78) Antibody 2405 20 µl
Western Blotting Immunohistochemistry Flow Cytometry
H Mk 27 Rabbit 
Anti-rabbit IgG, HRP-linked Antibody 7074 100 µl
Western Blotting
Anti-mouse IgG, HRP-linked Antibody 7076 100 µl
Western Blotting

Product Description

The HSP27 Antibody Kit provides an economical means to evaluate the activation status of the HSP27 protein. The kit contains enough primary antibody to perform two western blot experiments per primary antibody.

Specificity / Sensitivity

Each antibody in the HSP27 Antibody Sampler Kit recognizes endogenous levels of its specific target. Activation state antibodies detect their intended targets only when phosphorylated at the indicated site.

Source / Purification

Monoclonal antibody is produced by immunizing animals with a synthetic phosphopeptide corresponding to residues surrounding Ser82 of human HSP27 and to full-length human HSP27 protein. Polyclonal antibodies are produced by immunizing animals with synthetic phosphopeptides corresponding to residues surrounding Ser15 or Ser78 of human HSP27 protein. Antibodies are purified by protein A and peptide affinity chromatography.

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).

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, 1027-37.

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.

Entrez-Gene Id 3315
Swiss-Prot Acc. P04792

For Research Use Only. Not For Use In Diagnostic Procedures.
Cell Signaling Technology is a trademark of Cell Signaling Technology, Inc.
XP is a registered trademark of Cell Signaling Technology, Inc.

HSP27 Antibody Sampler Kit