85-1411-10　［取扱停止］GroES, Recombinant (Chaperonin 10, cpn10, Heat Shock Protein 10, HSP10) 200ug　G8976-05

特徴

• The E.coli heat shock proteins GroEL and GroES are two of the most thoroughly characterized members of a class of proteins known collectively as “molecular chaperones”. GroEL (cpn60; Hsp60 homolog) is an acidic 60kD E. coli heat shock protein which possesses a weak ATPase activity. In its native form, GroEL exists as a 14-mer consisting of two stacked rings each composed of seven identical subunits of Mr ~57,250. GroES (cpn10; Hsp10 homolog) consists of a single ring of seven identical subunits of Mr ~10,350 (2,3). Molecular chaperones, such as GroEL and GroES, are thought to function by interacting with transiently exposed interactive surfaces during their nascent synthesis, folding, transport and oligomerization. The net effect of chaperone participation in these processes is a reduction in inappropriate protein-protein interactions that might produce a nonfunctional structure. The GroEL and GroES genes, constituting the GroE operon, are members of the heat shock regulon of E. coli (7,8). Synthesis of the GroE protein, which accounts for approximately 1% of the cellular protein at 37°C, increases to about 10% of the total protein content upon shifting the growth temperature to 46°C.
• Activity Assay:GroES is assayed for its ability to suppress GroELís ATPase activity.
• Applications:Suitable for use in Functional Activity Assay and Western Blot. Other applications not tested.
• Recommended Dilution:Western Blot: 50-100ng per lane. Use G8980-25 GroES Pab RbxOptimal dilutions to be determined by the researcher.
• Storage and Stability:Aliquot to avoid repeated freezing and thawing and store at -70°C. Aliquots are stable for 6 months after receipt. For maximum recovery of product, centrifuge the original vial after thawing and prior to removing the cap.