HSP27 involved in stress resistance and actin organization.
General functions of HSP27 are the thermotolerance in vivo, the cytoprotection, and the support of cell survival under stress conditions. Special functions are manifold and complex. In vitro it acts as an ATPindependent chaperone by inhibiting protein aggregation and by stabilizing partially denatured proteins, which ensures refolding by the Hsp70-complex. HSP27 is also involved in the apoptotic signalling pathway which interacts with the outer mitochondrial membranes and interferes with the activation of cytochrome c/Apaf-1/dATP complex and therefore inhibits the activation of procaspase-9. A well documented function of HSP27 is the interaction with actin and intermediate filaments. It prevents the formation of non-covalent filament/filament interactions of the intermediate filaments and protects actin filaments from fragmentation. It also preserves the focal contacts fixed at the cell membrane.
Another function of HSP27 is the activation of the proteasome. It speeds up the degradation of irreversibly denatured proteins and junkproteins by binding to ubiquitinated proteins and to the 26S proteasome. HSP27 enhances the activation of the NF-?B pathway, that controls a lot of processes, such as cell growth and inflammatory and stress responses.

The antibody is stable for at least 1 year from the date of receipt when stored at -20°C to -70°C. Reconstituted antibody can also be aliquotted and stored at 4°C for 1 month or at -20°C to -70°C in a manual defrost freezer for many months without detectable loss activity. Please avoid freeze-thaw cycles.

The antibody can specifically bind to its immunogen, and did not show any cross reactivity with unrelated antigens in ELISA. The specificity for binding to recombinant protein, cellular protein and native antigen is not defined. Cross reactivity with mouse and rat HSP70 has not yet been tested.

Mouse Anti-Human Heat Shock Protein 27 (cat# DS-MB-01441) Recombinant Human Heat Shock Protein 27 (cat# 228-10789-3)