Analytical Data
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Gene name
HSP90aB1
- Application
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Alternative Names
HSP90aB1；HSP90B；HSPC2；HSPC3；Heat shock Protein HSP 90-beta
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Species
Human
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Source
E. coli
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Tag
N-6His
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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
1-724aa
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Molecular Weight
81kDa
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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
Identification
Protein Description
HSP90aB1, a member of the heat shock protein 90 (HSP90) family, plays a crucial role in the maintenance of protein homeostasis and cellular stress responses. It functions as a molecular chaperone, facilitating the proper folding, stabilization, and activation of various substrate proteins, including key signaling molecules involved in cell growth, differentiation, and survival. Dysregulation of HSP90 has been implicated in a range of diseases, particularly cancer, where it often supports the stability of oncogenic proteins. The study of recombinant HSP90aB1 protein is significant for understanding its structural and functional properties, as well as its interactions with client proteins. By producing recombinant HSP90aB1, researchers aim to elucidate the molecular mechanisms underpinning its chaperone activity, explore its role in disease pathogenesis, and evaluate its potential as a therapeutic target. Moreover, recombinant forms of HSP90aB1 can be utilized in high-throughput screening assays for identifying novel inhibitors that may disrupt its function, offering promising avenues for drug discovery in cancer treatment and other HSP90-related disorders. Overall, the investigation of recombinant HSP90aB1 provides valuable insights into its biological significance and therapeutic potential, highlighting the importance of this protein in cellular physiology and pathology.
