NSB536 Heat Shock Protein 25 (HSP25) antibody

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Rabbit anti Mouse Heat Shock Protein 25 (HSP25)

Product Description for Heat Shock Protein 25 (HSP25)

Rabbit anti Mouse Heat Shock Protein 25 (HSP25).
Product is tested for Western blot / Immunoblot.

Properties for Heat Shock Protein 25 (HSP25)

Product Category Primary Antibodies
Quantity 0.1 ml
Synonyms 28 kDa heat shock protein, Estrogen-regulated 24 kDa protein, Growth-related 25 kDa protein, HSP-27, HSP25, HSP28, HSPB1, Heat Shock Protein 27, Heat Shock Protein beta-1, SRP27, Stress-responsive protein 27
Reactivity Ms
Applications WB
Clonality Polyclonal
Host Rabbit
Shipping to Not USA/Canada
PDF datasheet View Datasheet
Manufacturer Novus Biologicals Inc.

Datasheet Extract

The antiserum was produced against a chemically synthesized phosphopeptide derived from a region of mouse HSP25 that contains serine 86.
Add. information Research Areas: Cellular Markers
Application Western Blot, The antibody has been used for Western blotting. No other applications have been tested. Recommended starting dilutions: Western Blot - 1:1000 *The optimal antibody concentration should be determined empirically for each specific application. , Western Blot
Background Heat Shock Protein 25 (HSP25), is a 25 kDa member of a family of proteins whose expression and function are stimulated by heat shock and other stress stimuli. A major function of these proteins is to serve as chaperones that bind to and stabilize the active conformation of other proteins. HSP25, along with other members of the small HSP group, possesses a C-terminal a-crystalline homology domain. HSP25 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 HSP25 exists in multiple complexes. One complex consists of HSP25, Akt (PKB), MAPKAP-kinase 2, and p38 MAPK. The presence of HSP25 in this complex is required for Akt activation by stress stimuli. Another complex consists of HSP25 and the IKK complex. HSP25 is also an actin capping protein that binds to the barbed (growing) ends of actin filaments, thereby inhibiting filament extension. Phosphorylation of HSP25 on serine 86 by MAPKAP-kinase 2 leads to HSP25 dissociation from the Akt/MAPKAP-kinase 2/p38 MAPK complex and from actin filaments, and stimulates HSP25 binding to the IKK complex.
General Readings Keezer, S.M., et al. (2003) Angiogenesis inhibitors target the endothelial cell cytoskeleton through altered regulation of heat shock protein 27 and cofilin. Cancer Res. 63(19):6405-6412.
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.
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.
Rane, M.J., et al. (2003) Heat shock protein 27 controls apoptosis by regulating Akt activation. J. Biol. Chem. 278(30):27828-27835.
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.
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.
Storage Aliquot and store at -20C or -80C. Avoid freeze-thaw cycles.
Affinity purified
Buffer System:
0.05% Sodium Azide
Affinity purified
HSP25 Phosphospecific [Ser86]

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