Heat Shock Protein 27 (HSP27) (Biotin)

Human HSP27, mouse HSP25 and alpha-beta-crystallin are part of a diverse family of small heat shock proteins which are produced in all organisms. They function as chaperone-like proteins by binding unfolded polypeptides and preventing uncontrolled protein aggregation. HSP27 is believed to exist mainly as oligomers of as many as 8–40 HSP27 protein monomers. Data suggests that the large oligomers of HSP27 have a chaperone-like activity by serving as a site where unfolding proteins may bind until ATP and HSP70-dependent refolding can occur (1). The state of phosphorylation and oligomerization of HSP27 may regulate microfilament organization; data demonstrates that only the non-phosphorylated lower molecular weight forms of HSP27 bind actin barbed ends and inhibit polymerization (2). HSP27 may also protect cells by enhancing cellular glutathione levels. Wild-type HSP27 and mutant forms have shown that cellular glutathione levels depend on the oligomerization of HSP27 (3). Recent findings indicate that HSP27 is a negative regulator of cytochrome c-dependent activation of procaspase-3 (4).||Applications: |Suitable for use in Western Blot. Other applications not tested.||Recommended Dilution:|Western Blot (ECL): 1:1,000|Optimal dilutions to be determined by the researcher.||Positive Control:|H1838-01: HeLa Heat Shocked Cell Lysate, |H1830-57: Recombinant Human Hsp27 Protein||Storage and Stability:|Store product at 4°C if to be used immediately within two weeks. For long-term storage, aliquot to avoid repeated freezing and thawing and store at -20°C. Aliquots are stable at -20°C for 12 months after receipt. Dilute required amount only prior to immediate use. Further dilutions can be made in assay buffer. For maximum recovery of product, centrifuge the original vial after thawing and prior to removing the cap.