Analytical Data
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Gene name
HSPb6
- Application
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Alternative Names
HSP20; Heat Shock Protein 20 kD; Heat Shock Protein B6, Alpha Crystallin Related; Heat shock 20 kDa-like protein p20
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Species
Rat
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Source
E. coli
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Tag
N-His
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
P97541
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Expression Region
Met1~Lys162
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Molecular Weight
19kDa
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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
HSPb6, a member of the small heat shock protein (sHSP) family, has garnered attention due to its essential role in cellular stress responses and its potential implications in various diseases, including neurodegenerative disorders and cancer. Small heat shock proteins, including HSPb6, are known to function as molecular chaperones, preventing protein aggregation and misfolding, which are key processes in maintaining cellular homeostasis. The study of recombinant HSPb6 protein is particularly important as it allows for the detailed investigation of its structure-function relationships, as well as its interaction with other cellular proteins under stress conditions. Furthermore, understanding the mechanisms by which HSPb6 exerts its protective effects could lead to new therapeutic strategies for diseases characterized by protein misfolding and aggregation. Advances in recombinant protein technology have enabled the production of HSPb6 in various expression systems, facilitating studies on its biophysical properties and biological functions. As research progresses, elucidating the precise molecular mechanisms through which HSPb6 contributes to stress tolerance and cytoprotection will not only enhance our understanding of its physiological roles but may also uncover novel targets for drug development in conditions where the heat shock response is compromised.
