ELISA, Immunogen, SDS-PAGE, WB, Bioactivity testing in progress
Species
Escherichia coli
Nature
Recombinant
Endotoxin level
Please contact with the lab for this information.
Purity
>90% as determined by SDS-PAGE.
Predicted molecular weight
59.49 kDa
Form
Lyophilized
Storage buffer
Lyophilized from a solution in PBS pH 7.4, 1 mM EDTA, 4% Trehalose, 1% Mannitol.
Please refer to the specific buffer information in the hardcopy of datasheet or the lot-specific COA.
Reconstitution
Reconstitute in sterile water for a stock solution. Adjust the volume of sterile water so that, after reconstitution, the final stock concentration matches the value indicated on the product label or datasheet.
RECONSTITUTION PROTOCOL 1. Allow the product to be reconstituted and the reconstitution diluent to reach room temperature. 2. Tap or briefly centrifuge the product vial before opening to dislodge any lyophilized material that may be dispersed on the wall or cap of the vial. 3. Use the diluent and stock concentration recommended in the product datasheet. If preparing a stock concentration higher than recommended, contact Technical Service. 4. After adding the diluent, re-cap the vial and invert gently by hand or place on a slow rocking platform to allow the reconstitution diluent to coat all the surfaces inside the vial. Note: Do not mix by vortexing or by pipetting the material up and down. 5. Allow the vial to sit at room temperature with gentle agitation for at least 15 minutes before aliquotting or using. 6. Store the reconstituted material in single use aliquots in polypropylene or siliconized tubes. Aliquots of 10 μL or larger are recommended.
Shipping
In general, proteins are provided as lyophilized powder/frozen liquid. They are shipped out with dry ice/blue ice unless customers require otherwise.
Stability and Storage
Use a manual defrost freezer and avoid repeated freeze thaw cycles. Store at 2 to 8°C for frequent use. Store at -20 to -80°C for twelve months from the date of receipt.
Chaperonin GroEL is a ~57 kDa protein. 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, probably by preventing aggregation and by entropically destabilizing folding intermediates. Rapid binding of ATP, followed by slower binding of the non-native substrate protein and GroES to the cis open ring of GroEL initiates productive folding of the non-native protein inside a highly stable GroEL-ATP-GroES complex. Binding of ATP and GroES induces conformational changes that result in the release of the substrate protein into a nano-cage compartment, within the GroEL central cavity, for folding in isolation. To discharge GroES and substrate protein, ATP hydrolysis in the cis ring is required to form a GroEL-ADP-GroES complex with decreased stability.
1. Goloubinoff, P. et al. (1989) Nature 342, 884-9. PMID: 10532860
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