Anti-phospho-Heat Shock Protein 25 (Ser86) (HSP25)

Heat Shock Protein 25 (HSP25), is a 25kD 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 alpha-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. Applications: Suitable for use in ELISA and Western Blot. Other applications not tested. Recommended Dilution: Western Blot: 1:1000, Optimal dilutions to be determined by the researcher. Positive Controls: NIH3T3 cells with and without anisomycin. , Storage and Stability:, May be stored at 4°C for short-term only. For long-term storage, aliquot and store at -20°C. Aliquots are stable for at least 12 months at -20°C. For maximum recovery of product, centrifuge the original vial after thawing and prior to removing the cap. Further dilutions can be made in assay buffer.