Cell Signaling Technology

Product Pathways - MAPK Signaling

HSP27 (G31) Mouse mAb #2402

Applications Reactivity MW (kDa) Source Isotype
W IHC-P IF-IC H Mk 27 Mouse IgG1

Applications Key:  W=Western Blotting  IHC-P=Immunohistochemistry (Paraffin)  IF-IC=Immunofluorescence (Immunocytochemistry)
Reactivity Key:  H=Human  Mk=Monkey
Species enclosed in parentheses are predicted to react based on 100% sequence homology. Species cross-reactivity is determined by Western blot.

Specificity / Sensitivity

HSP27 (G31) Mouse mAb detects endogenous levels of total HSP27 protein. The antibody does not cross-react with other heat shock proteins.

Source / Purification

Monoclonal antibody is produced by immunizing mice with full length HSP27 protein.

Western Blotting

Western Blotting

Western blot analysis of extracts from SK-N-MC, HeLa and COS cells, using HSP27 (G31) Mouse mAb.

IHC-P (paraffin)

IHC-P (paraffin)

Immunohistochemical analysis of paraffin-embedded human lung carcinoma, using HSP27 (G31) Mouse mAb.

IHC-P (paraffin)

IHC-P (paraffin)

Immunohistochemical analysis of paraffin-embedded human breast carcinoma, untreated (left panels) or lambda phosphatase-treated (right panels), using Phospho-HSP27 (Ser82) Antibody #2401 (upper panels) or HSP27 (G31) Mouse mAb (lower panels).


IF-IC

IF-IC

Immunocytochemical staining of HeLa cells, showing cytoplasmic staining, using HSP27 (G31) Mouse mAb.

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).

  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, 1027-1037.
  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.

Application References

Have you published research involving the use of our products? If so we'd love to hear about it. Please let us know!

Companion Products

Product Pathways

Drug Discovery Tools

Featured Technologies

Protein Classes