Analytical Data
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Gene name
AHSA1
- Application
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Alternative Names
p38
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Species
Human
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Source
E. coli
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Tag
N- GST
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
O95433
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Expression Region
1-338aa
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Molecular Weight
65.3 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
AHSA1 (Activator of HSP90 ATPase Activity 1) is a key co-chaperone protein that plays a critical role in the function of HSP90, a molecular chaperone essential for the maturation and stability of numerous client proteins involved in various cellular processes, including signal transduction, cell cycle regulation, and protein degradation. The dysregulation of HSP90 and its co-chaperones, such as AHSA1, has been implicated in the development of several diseases, particularly cancer. Research on AHSA1 and its recombinant protein has gained traction due to its potential as a therapeutic target. The understanding of AHSA1’s structure and function can provide insights into the mechanisms of HSP90 activity modulation and the subsequent impact on oncogenic signaling pathways. Moreover, the generation of recombinant AHSA1 offers a valuable tool for elucidating its biochemical properties and interactions with HSP90 and client proteins, facilitating the development of novel inhibitors that could disrupt aberrant chaperone activity in cancer cells. This line of research holds promise not only for identifying new strategies for cancer treatment but also for dissecting the broader roles of protein homeostasis in cellular physiology and pathology. Understanding the dynamics of AHSA1 in relation to HSP90 is therefore vital in advancing therapeutic approaches and improving clinical outcomes for cancer patients.
