Analytical Data
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Gene name
GroES
- Application
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Alternative Names
HSPE1;10 kDa heat shock Protein. mitochondrial
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Species
E.coli
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Source
E. coli
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Tag
His tag N-Terminus
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
P42386
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Expression Region
1-94aa
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AA Sequence
MNLNMLHDNVLIEALEECNSSSPIQLPDSAKKKPTQGKVVAVGPGVYNHSGNILPMTIKVGDVVFYRQWAGNEIEFHEKKYIVMKESDIIAKEA
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Molecular Weight
17.5 kDa
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Endotoxin
< 1.0 EU per μg protein as determined by the LAL method.
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Form
Freeze-dried powder
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Buffer formulation
PBS, pH7.4, containing 0.01% SKL, 1mM DTT, 5% Trehalose and Proclin300.
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Reconstitution
Reconstitute in ddH2O to a concentration of 0.1-0.5 mg/mL. Do not vortex.
- Customization
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Stability Test
The thermal stability is described by the loss rate. The loss rate was determined by accelerated thermal degradation test, that is, incubate the protein at 37℃ for 48h, and no obvious degradation and precipitation were observed. The loss rate isless than 8% within the expiration date under appropriate storage condition.
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Storage & Shelf Life
Samples are stable for up to twelve months from date of receipt at -20℃ to -80℃. Store it under sterile conditions at -20℃ to -80℃. It is recommended that the protein be aliquoted for optimal storage. Avoid repeated freeze-thaw cycles.
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Shipping
In general, recombinant proteins are supplied as lyophilized powder and shipped at ambient temperature. For bulk packages, the proteins are provided as frozen liquid and shipped with blue ice, unless otherwise requested by the customer.
Quality inspection process
Related Products
Protein Description
GroES is a significant molecular chaperone in bacterial cells, functioning as a co-chaperonin that assists in the proper folding of proteins in conjunction with GroEL, a heat shock protein. The research into GroES and its recombinant protein applications has grown in importance due to its essential role in cellular stress responses and protein maturation. Understanding the mechanisms of protein folding and assembly has substantial implications in biotechnology and medicine, particularly in the production of recombinant proteins, which are vital for therapeutics and research. The study of GroES provides insights into the evolution of chaperonin systems and their diverse functions across various organisms. Recombinant GroES is often produced for experimental applications, allowing researchers to investigate its interactions, effects on protein misfolding diseases, and its potential use in enhancing the yield and stability of target proteins in biotechnological processes. As a model system, the GroEL/GroES complex has also revealed fundamental principles of protein folding dynamics, making it a valuable tool in both basic and applied sciences.
