Analytical Data
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Gene name
HSP90
- Application
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Alternative Names
HSP90B; HSPC2; HSPC3; HSPCB
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Species
Human
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Source
E. coli
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Tag
Avi
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
P08238
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Expression Region
T285-G689
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Protein Length
Partial
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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
HSP90, or Heat Shock Protein 90, is a highly conserved molecular chaperone that plays a crucial role in the folding, stabilization, and activation of various client proteins, including many involved in signal transduction and cellular stress responses. Its significance is underscored by its involvement in numerous cellular processes, such as cell proliferation, differentiation, and apoptosis. Over the years, extensive research has highlighted the role of HSP90 in cancer biology, where it has been shown to assist in the maturation of key oncogenes and tumor suppressors, making it a potential target for therapeutic intervention. The recombinant production of HSP90 has become an important focus within the field of molecular biology, allowing for the detailed study of its structure, function, and interactions with client proteins. Advances in recombinant DNA technology have facilitated the cloning and expression of HSP90 in various systems, providing insights into its biochemical properties and the mechanisms by which it contributes to diseases. Moreover, the ability to produce large quantities of functional HSP90 in vitro is essential for high-throughput screening of small molecules that could inhibit its activity, paving the way for novel cancer therapies. Researchers are also investigating the role of post-translational modifications and co-chaperones in modulating HSP90 activity, further emphasizing its complexity as a chaperone system. Overall, the recombinant study of HSP90 continues to be a vital area of investigation for understanding its fundamental roles in health and disease and for developing targeted therapeutic strategies.
