GROEL (27-573) Human
Description
GROEL is fused to a 25 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Product Specs
MGSSHHHHHH SSGLVPRGSH MGSHMAKDVK FGADARALML QGVDLLADAV AVTMGPKGRT VIIEQSWGSP KVTKDGVTVA KSIDLKDKYK NIGAKLVQDV ANNTNEEAGD GTTTATVLAR SIAKEGFEKI SKGANPVEIR RGVMLAVDAV IAELKKQSKP VTTPEEIAQV ATISANGDKE IGNIISDAMK KVGRKGVITV KDGKTLNDEL EIIEGMKFDR GYISPYFINT SKGQKCEFQD AYVLLSEKKI SSIQSIVPAL EIANAHRKPL VIIAEDVDGE ALSTLVLNRL KVGLQVVAVK APGFGDNRKN QLKDMAIATG GAVFGEEGLT LNLEDVQPHD LGKVGEVIVT KDDAMLLKGK GDKAQIEKRI QEIIEQLDVT TSEYEKEKLN ERLAKLSDGV AVLKVGGTSD VEVNEKKDRV TDALNATRAA VEEGIVLGGG CALLRCIPAL DSLTPANEDQ KIGIEIIKRT LKIPAMTIAK NAGVEGSLIV EKIMQSSSEV GYDAMAGDFV NMVEKGIIDP TKVVRTALLD AAGVASLLTT AEVVVTEIPK EEKDPGMGAM GGMGGGMGGG MF.
Product Science Overview
GroEL is a large, cylindrical protein complex composed of 14 identical subunits arranged in two stacked heptameric rings. Each subunit has a molecular mass of approximately 60 kDa . The recombinant form of GroEL (HSP60) (27-573 a.a.) is produced in Escherichia coli and consists of a single, non-glycosylated polypeptide chain containing 572 amino acids (27-573 a.a.) . This recombinant protein is often fused to a His-tag at the N-terminus to facilitate purification .
GroEL functions in conjunction with its co-chaperonin, HSP10 (GroES), which forms a unique complex with GroEL. HSP10 is a single heptameric protein ring with a molecular mass of 10 kDa . This complex is essential for the ATPase activity of GroEL, which is necessary for the proper folding of polypeptides .
The primary function of GroEL is to assist in the correct folding of newly synthesized and stress-denatured proteins. The process involves several steps:
- Binding of Unfolded Proteins: Unfolded or partially folded polypeptides bind to the hydrophobic regions of GroEL.
- ATP Binding and Hydrolysis: ATP binds to GroEL, causing a conformational change that allows the binding of GroES.
- Encapsulation: GroES caps the GroEL complex, creating an enclosed environment where the polypeptide can fold without the risk of aggregation.
- Release of Folded Proteins: ATP hydrolysis leads to the release of GroES and the correctly folded protein .
The recombinant GroEL (HSP60) protein is typically stored in a solution containing Tris-HCl buffer, DTT, and glycerol to maintain its stability. It should be stored at 4°C for short-term use and at -20°C for long-term storage. Avoiding multiple freeze-thaw cycles is crucial to preserve its functionality .
