Analytical Data
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Gene name
hsp90a.1
- Application
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Alternative Names
hsp90 (hsp90a) (hsp90aa1)
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Species
Zebrafish
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Source
Baculovirus
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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
Q90474
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Expression Region
151-355aa
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Molecular Weight
27.9 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
Hsp90a.1, a member of the heat shock protein 90 family, plays a crucial role in protein folding, stability, and cellular stress responses. It is highly conserved across species and is involved in the maturation and function of various client proteins, including many involved in cancer and neurodegenerative diseases. The study of Hsp90a.1 recombinant protein has gained significant attention in recent years due to its potential as a therapeutic target. Abnormal Hsp90 activity is often associated with tumor progression, making it a promising candidate for cancer therapy. Additionally, understanding Hsp90a.1's mechanisms can offer insights into its function in cellular signaling pathways and stress response, presenting opportunities for the development of novel biotechnological applications. The recombinant expression of Hsp90a.1 allows for detailed biochemical characterization and the exploration of its interactions with client proteins, contributing to a deeper understanding of its role in health and disease. Moreover, this research lays the foundation for the design of small molecule inhibitors that can selectively disrupt Hsp90's function, thereby offering new strategies for disease intervention. Overall, the investigation of Hsp90a.1 recombinant protein is pivotal in unraveling its biological significance and therapeutic potential.
