Together with its co-chaperonin GroES, plays an essential role in assisting protein folding. The GroEL-GroES system forms a nano-cage that allows encapsulation of the non-native substrate proteins and provides a physical environment optimized to promote and accelerate protein folding. Source: Recombinant protein corresponding to aa19-525 from Helicobacter pylori 60kD chaperonin, fused to 10X His-Tag at N-terminal and Myc-Tag at C-terminal, expressed in E.coli. Molecular Weight: ~61.7kD Amino Acid Sequence: VRQLHDAVKVTMGPRGRNVLIQKSYGAPSITKDGVSVAKEIELSCPVANMGAQLVKEVASKTADAAGDGTTTATVLAYSIFKEGLRNITAGANPIEVKRGMDKAAEAIINELKKASKKVGGKEEITQVATISANSDHNIGKLIADAMEKVGKDGVITVEEAKGIEDELDVVEGMQFDRGYLSPYFVTNAEKMTAQLDNAYILLTDKKISSMKDILPLLEKTMKEGKPLLIIAEDIEGEALTTLVVNKLRGVLNIAAVKAPGFGDRRKEMLKDIAILTGGQVISEELGLSLENAEVEFLGKAGRIVIDKDNTTIVDGKGHSDDVKDRVAQIKTQIASTTSDYDKEKLQERLAKLSGGVAVIKVGAASEVEMKEKKDRVDDALSATKAAVEEGIVIGGGAALIRAAQKVHLNLHDDEKVGYEIIMRAIKAPLAQIAINAGYDGGVVVNEVEKHEGHFGFNASNGKYVDMFKEGIIDPLKVERIALQNAVSVSSLLLTTEATVHEIKEEK Storage and Stability: Lyophilized and reconstituted products are stable for 6 months after receipt at -20C. Reconstitute with sterile ddH2O. Aliquot to avoid repeated freezing and thawing. Store at -20C. 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.
Supplied as a lyophilized powder from 20mM Tris-HCl, 0.5M sodium chloride, pH 8.0, 6% trehalose. Reconstitute with sterile ddH2O to a concentration of 0.1-1mg/ml.
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