Analytical Data
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Gene name
groEL
- Application
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Alternative Names
57KDA chlamydial hypersensitivity antigen GroEL protein Heat shock protein 60 HSP60 Protein Cpn60
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Species
Chlamydia trachomatis
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Source
E. coli
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Tag
N- His-SUMO
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
P0C0Z7
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Expression Region
2-544aa
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Molecular Weight
74.0 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
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Protein Description
GroEL is a well-studied molecular chaperone that plays a crucial role in protein folding and assembly within the cell. Found in bacteria, GroEL forms a double-ring structure that provides an enclosed environment for polypeptides that are misfolded or unfolding due to various stresses, such as heat shock or genetic mutations. The necessity for proper protein folding is paramount because misfolded proteins can lead to cellular dysfunction and diseases, including neurodegenerative disorders. Research into GroEL has provided significant insights into the mechanisms of protein maturation, revealing a dynamic system involving ATP hydrolysis and the interaction with co-chaperone GroES, which works in tandem to facilitate correct folding. The exploration of GroEL's function has also led to therapeutic implications, where its potential to assist in the refolding of therapeutic proteins makes it valuable in biotechnology and pharmaceutical industries. Additionally, recombinant GroEL is utilized in various experimental applications, including the production of complex proteins that require careful folding. As the understanding of GroEL continues to evolve, it remains a focal point in cell biology and biochemistry, shedding light on the intricacies of cellular protein homeostasis.
