Heat Shock Protein 27, phosphorylated (Ser82) (HSP27)

A major function of these proteins is to serve as chaperones that bind to and stabilize the active conformation of other proteins. HSP27, along with other members of the small HSP group, possesses a C-terminal a-crystalline homology domain. HSP27 is localized to the cytoplasm of unstressed cells but can redistribute to the nucleus in response to stress, where it may function to stabilize DNA and/or the nuclear membrane. Cytoplasmic HSP27 exists in multiple complexes. One complex consists of HSP27, Akt (PKB), MAPKAP-kinase 2, and p38 MAPK. The presence of HSP27 in this complex is required for Akt activation by stress stimuli. Another complex consists of HSP27 and the IKK complex. HSP27 is\nalso an actin capping protein that binds to the barbed (growing) ends of actin filaments, thereby inhibiting filament extension. Phosphorylation of HSP27 on serine 82 by MAPKAP-kinase 2 leads to HSP27 dissociation from the Akt/MAPKAP-kinase 2/p38 complex and from actin filaments, and stimulates HSP27 binding to the IKK complex.\n\nApplications: \nSuitable for use in Western Blot. Other applications not tested.\n\nRecommended Dilution:\nWestern Blot: 1:1000 \nOptimal dilutions to be determined by the researcher.\n\nPositive Control: \nHeLa cells treated with TNF-a Heat Shock Protein 27 (HSP27) is a 27kD member of a family of proteins whose expression and function are stimulated by heat shock and other stress stimuli. \n\nStorage and Stability:\nMay be stored at 4 degrees C for short-term only. Aliquot to avoid repeated freezing and thawing. Store at -20 degrees C. Aliquots are stable for at least 12 months. For maximum recovery of product, centrifuge the original vial after thawing and prior to removing the cap.

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SPECIFICATIONS

Catalog Number

H1830-52H

Size

10 Blots

Applications

WB

Hosts

Rabbit

Reactivities

Hum

Form

Supplied as a liquid in PBS (without Mg2+ and Ca2+), 1mg/ml BSA (IgG, protease free), pH 7.3, 0.05% sodium azide, 50% glycerol.

P Type

Pab

Purity

Purified by immunoaffinity chromatography.

References

1. Keezer, S.M., et al. (2003) Angiogenesis inhibitors target the endothelial cell cytoskeleton through\naltered regulation of heat shock protein 27 and cofilin. Cancer Res. 63(19):6405-6412. 2. Pantos, C., et al. (2003) Thyroxine pretreatment increases basal myocardial heat-shock protein 27 expression and accelerates translocation and phosphorylation of this protein upon ischaemia. Eur. J. Pharmacol. 478(1):53-60. 3. Park, K.J., et al. (2003) Heat shock protein 27 association with the IkB kinase complex regulates tumor necrosis factor a-induced NF-kB activation. J. Biol. Chem. 278(37):35272-35278. 4. Rane, M.J., et al. (2003) Heat shock protein 27 controls apoptosis by regulating Akt activation. J. Biol. Chem. 278(30):27828-27835. 5. Geum, D., et al. (2002) Phosphorylation-dependent cellular localization and thermoprotective role of heat shock protein 25 in hippocampal progenitor cells. J. Biol. Chem. 277(22):19913-19921. 6. Garcia, J.G., et al. (2002) Critical involvement of p38 MAP kinase in pertussis toxin-induced cytoskeletal reorganization and lung permeability. FASEB J. 16(9):1064-1076.

Additional Info

Recognizes human HSP27. This antibody does not detect endogenous mouse HSP25 [pS86] protein in extracts of NIH3T3 cells treated with anisomycin; however, interaction with the human HSP27 protein is inhibited by the phosphopeptide used to generate the mouse HSP25 [pS86] antibody.