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GroEL/GroES (chaperonin 60/chaperonin 10)

GroEL/GroES is called as Molecular Ice. Folding intermediates were captured by a hydrophobic cavity in 14mer GroEL, native form of proteins can be released by adding  ATP-Mg++, GroES. A subset of E. coli proteins need  chaperonin to gain an active form. Refolding of proteins from inclusion body expressed in prokaryotic system may be painful. For small amount of functional protein, the best way is to try chaperonin system, since it is perfected in the billions of year by Nature. 

GroEL/GroES are purified in a small scale with the protocol developed in our Lab. The GroES is the purest sample on the market. 

GroEL       95% Pure    2mg    (2500nM 14mer)               Cat. No. 20010068    $380.00
GroES       95% Pure  0.2mg    (2850nM  7mer)               Cat. No. 20010069    $380.00
GroEL/GroES (1:1) 95% 1.55mg   (1800nM 14mer/1800nM 7mer)   Cat. No. 20010070    $380.00

Hip         95%       0.5mg        Coming Soon             Cat. No. 20040210    $380.00
Hop         95%       0.5mg        Coming Soon             Cat. No. 20040220    $380.00
Hsp40       95%       0.5mg                                Cat. No. 20040230    $380.00


Refolding Capacity
(2mg of GroEL, based on one round of binding and refolding) 
60Kd        0.15mg 
40Kd          0.1mg 
20Kd        0.05mg 

Denaturing Condition
50mM Tris-HCl, pH8.0
4M GnHCl,
1% 2-Mercaptoethanol,
Water bath, 100C, 3~5min,
Note: denatured sample has to be made freshly

Refolding Condition
20mM Tris-HCl, (or PBS), pH 6.8-7.2 
200-500nM GroEL/GroES (14mer/7mer) 
10mM Mg++ 
2mM ATP 
100mM KCl 
Room Temperature. 
Final concentration of GnHCl: 100-200mM 
Final protein concentration: 2~3x chaperonin complex 
(Optional, 7.5-10% Glycerol, 4-15 degree) 

Xie Z, Hendrix RW. Assembly in vitro of bacteriophage HK97 proheads. J Mol Biol. 1995 Oct 13;253(1):74-85.