Analytical Data
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Gene name
HSP90aA1
- Application
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Alternative Names
HSP90aA1；KIAA0719；TOM70；TOMM70A；Mitochondrial import receptor subunit TOM70
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Species
Human
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Source
E. coli
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Tag
His tag N-Terminus
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
P07900
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Expression Region
233-291aa
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AA Sequence
DEAEEKEDKEEEKEKEEKESEDKPEIEDVGSDEEEEKKDGDKKKKKKIKEKYIDQEELN
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Molecular Weight
11.2 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
HSP90aA1, a member of the heat shock protein 90 (HSP90) family, plays a crucial role in cellular processes, including protein folding, signal transduction, and stress responses. Its functional significance is underscored by its involvement in the maturation and stability of various client proteins, many of which are critical for cellular homeostasis and disease progression, particularly in cancer and neurodegenerative disorders. Given the essential nature of HSP90aA1 in maintaining cellular integrity under stress conditions, it has garnered attention as a potential therapeutic target. Research into the recombinant expression of HSP90aA1 allows for the investigation of its structural and functional properties in controlled settings. By producing this protein in a recombinant form, scientists can explore its interactions with client proteins, elucidate its molecular chaperone mechanisms, and assess its potential as a drug target. Furthermore, understanding HSP90aA1's role in various diseases emphasizes its importance in biomedicine, revealing avenues for the development of HSP90 inhibitors that may modulate disease outcomes. Overall, the study of HSP90aA1 recombinant proteins enhances our comprehension of cellular machinery, providing insights that could lead to innovative therapeutic strategies.
