Analytical Data
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Gene name
HtpG
- Application
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Alternative Names
Heat shock protein C62.5 Heat shock protein HtpG High temperature protein G
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Species
Escherichia coli
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Source
E. coli
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Tag
Tag Free
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
P0A6Z3
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Expression Region
1-624aa
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Molecular Weight
71.4 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
HtpG, a heat shock protein belonging to the Hsp90 family, plays a crucial role in protein folding, stabilization, and degradation in response to stress conditions in various organisms. Its significance expands beyond mere chaperone activity; HtpG is also involved in critical cellular processes such as signal transduction, cellular development, and stress response. The study of recombinant HtpG proteins has garnered attention due to their potential applications in biotechnology and medicine, particularly in understanding the mechanisms of stress response and protein aggregation related diseases. Researchers have aimed to produce and characterize recombinant forms of HtpG to elucidate its functional properties, explore its interaction with client proteins, and investigate its role in cellular mechanisms. These studies are pivotal for finding therapeutic targets for diseases associated with misfolded proteins, including neurodegenerative disorders. Furthermore, recombinant HtpG serves as a model for examining chaperone function and the intricate dynamics of protein interactions under stress, providing insights that can lead to advancements in protein engineering and drug development.
