Analytical Data
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Gene name
HSP23.6
- Application
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Alternative Names
/
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Species
Arabidopsis thaliana
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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
Q96331
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Expression Region
32-210aa
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Molecular Weight
24.4 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
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Protein Description
HSP23.6, a member of the heat shock protein (HSP) family, is a small heat shock protein (sHSP) known for its critical role in cellular stress responses. Research into HSP23.6 has gained significance due to its involvement in protecting cells from various forms of stress, including heat shock, oxidative stress, and protein misfolding. This protein functions as a molecular chaperone, helping to maintain protein homeostasis by preventing aggregation and facilitating the refolding of denatured proteins. Given the association of heat shock proteins with various diseases, including neurodegenerative disorders and cancer, HSP23.6 has become a focal point for understanding the mechanisms of cellular resilience and pathology. Additionally, its unique structural properties, which allow it to form oligomeric complexes, enhance our understanding of protein dynamics under stress conditions. Investigating the molecular mechanisms and pathways involving HSP23.6 could provide insights into therapeutic strategies aimed at enhancing cellular protection and improving treatment outcomes in stress-related diseases. This research not only contributes to the fundamental understanding of cell biology but also holds potential for biotechnological applications, such as in protein engineering and drug development. Overall, the study of HSP23.6 recombinant protein is pivotal for unraveling the intricate interplay between protein dynamics, stress responses, and disease progression, offering a promising avenue for future scientific exploration and therapeutic innovation.
