Analytical Data
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Gene name
HSP90b
- Application
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Alternative Names
Heat shock 84KDA
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Species
Human
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Source
E. coli
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Tag
N- His & C- Myc
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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
2-724aa
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Molecular Weight
88.1 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
HSP90b, a member of the heat shock protein 90 family, is a highly conserved chaperone that plays a critical role in protein folding, stabilization, and degradation. It is involved in various cellular processes, including signal transduction, cell cycle control, and response to environmental stresses. Research has shown that HSP90b interacts with numerous client proteins, many of which are implicated in cancer and neurodegenerative diseases, highlighting its potential as a therapeutic target. The study of recombinant HSP90b is particularly important for understanding its functional mechanisms and interactions at the molecular level. By producing recombinant HSP90b, researchers can investigate its structure, binding affinities, and role in client protein maturation. Furthermore, recombinant protein technologies enable the exploration of HSP90b's mechanistic pathways, providing insights into its chaperone activity and the regulation of its function under different physiological conditions. The ability to manipulate HSP90b in vitro enhances our understanding of its contribution to disease processes and may facilitate the development of novel interventions targeting protein misfolding and aggregation. Thus, the study of recombinant HSP90b is pivotal for elucidating its biological significance and exploring its applications in therapeutic strategies, particularly in oncology and neurodegenerative disorders.
