84-1056-92　Heat Shock Protein 27 (HSP27) 50ug　H1834-05B

特徴

• 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 in cells and 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 has been suggested to regulate microfilament organization because data demonstrates that only the nonphosphorylated lower molecular weight forms of Hsp27 bind actin barbed ends and inhibit polymerization (2).
• Hsp27 is also believed to protect cells by enhancing cellular glutathione levels and elevated glutathione levels have been measured in cells overexpressing hsp27.
• Data from studies using wild-type Hsp27 and mutant forms in which the serine phosphorylation sites were mutated to alanines, glycines or aspartates, have shown that cellular glutathione levels depend on the oligomerization of Hsp27 (3).
• Recent findings indicate a novel function for Hsp27 which is that HSp27 is a negative regulator of cytochrome c-dependent activation of procaspase-3 (4).
• Applications:Western Blot (Colorimetric) (7,8): 1:5,000 Immunoprecipitation (6): 1:100 Immunohistochemistry (9): 1:200 ELISA: 1:1,000 Optimal dilutions to be determined by researcher.
• Positive Controls:Recombinant Human Hsp27 ProteinHeLa Heat Shocked Cell Lysate
• Storage and Stability:May be stored at 4°C for short-term only.
• Aliquot to avoid repeated freezing and thawing.
• Store at -20°C.
• Aliquots are stable for 12 months after receipt.
• For maximum recovery of product, centrifuge the original vial after thawing and prior to removing the cap.