Analytical Data
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Gene name
hsp90a1
- Application
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Alternative Names
hsp90a1；hsp90；hsp90a；hsp90aa1；Heat shock Protein HSP 90-alpha 1
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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
Q90474
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Expression Region
1-725aa
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AA Sequence
MPEKSAQPVMEEEVETFAFQAEIAQLMSLIINTFYSNKEIFLRELISNSSDALDKIRYESLTDPSKLDSCKDLKIELIPDQKERTLTIIDTGIGMTKADLINNLGTIAKSGTKAFMEALQAGADISMIGQFGVGFYSAYLVAEKVTVITKHNDDEQYIWESAAGGSFTVKPDFGESIGRGTKVILHLKEDQSEYVEEKRIKEVVKKHSQFIGYPITLYIEKQREKEVDLEEGEKQEEEEVAAGEDKDKPKIEDLGADEDEDSKDGKNKRKKKVKEKYIDAQELNKTKPIWTRNPDDITNEEYGEFYKSLSNDWEDHLAVKHFSVEGQLEFRALLFVPRRAAFDLFENKKKRNNIKLYVRRVFIMDNCEELIPEYLNFIKGVVDSEDLPLNISREMLQQSKILKVIRKNLVKKCLDLFTELAEDKDNYKKYYEQFSKNIKLGIHEDSQNRKKLSDLLRYYTSASGDEMVSLKDYVSRMKDTQKHIYYITGETKDQVANSAFVERLRKAGLEVIYMIEPIDEYCVQQLKEYDGKNLVSVTKEGLELPEDEEEKKKQDELKAKYENLCKIMKDILDKKIEKVTVSNRLVSSPCCIVTSTYGWTANMERIMKSQALRDNSTMGYMTAKKHLEINPAHPIVETLREKAEADKNDKAVKDLVILLFETALLSSGFTLDDPQTHANRIYRMIKLGLGIDDDDSVVEEISQPAEEDMPVLEGDDDTSRMEEVD
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Molecular Weight
83.3 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
Hsp90 (Heat Shock Protein 90) is a highly conserved molecular chaperone that plays a critical role in protein folding, stabilization, and degradation, significantly influencing cellular response to stress and maintaining proteostasis. Among its isoforms, Hsp90α (Hsp90A1) is particularly important in cancer biology, as it facilitates the proper folding and activation of various client proteins, including many involved in signaling pathways that regulate cell growth, survival, and apoptosis. The overexpression of Hsp90α in many tumors correlates with poor prognosis, making it a potential target for therapeutic intervention. Furthermore, the aberrant function of Hsp90α has been implicated in neurodegenerative diseases and other pathological conditions, highlighting its importance beyond oncology. Research into recombinant Hsp90α proteins has gained momentum, as these proteins can be used to elucidate its intricate mechanisms of action, assist in the identification of novel inhibitors, and aid in the development of targeted therapies. By producing and studying recombinant Hsp90α, scientists can dissect the conformational changes, interaction dynamics, and regulatory mechanisms that govern Hsp90α's functionality, potentially leading to breakthroughs in drug design and therapeutic strategies. Understanding the structure-function relationship of Hsp90α also enhances our comprehension of related diseases and can pave the way for innovative treatments aimed at modulating its activity.
