Analytical Data
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Gene name
AHSA2
- Application
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Alternative Names
Activator of 90 kDa heat shock Protein ATPase homolog 2; AHA1
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Species
Human
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Source
E. coli
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Tag
GST-tag at N-terminal
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
Q719I0
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Expression Region
1-137aa
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AA Sequence
MILPTKAMATQELTVKRKLSGNTLQVQASSPVALGVRIPTVALHMMELFDTTVEQLYSIFTVKELTNKKIIMKWRCGNWPEEHYAMVALNFVPTLGQTELQLKEFLSICKEENMKFCWQKQHFEEIKGSLQLTPLNG
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Molecular Weight
42.1 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
AHSA2, or Activator of Hsp90 ATPase 2, is a co-chaperone protein that plays a critical role in the regulation of heat shock proteins, particularly Hsp90, which are essential for the proper folding, stability, and function of a wide array of client proteins involved in signal transduction, cell cycle regulation, and apoptosis. The understanding of AHSA2 has gained traction due to its implications in various diseases, including cancer, where it is often overexpressed, contributing to the survival and proliferation of tumor cells by enhancing the activity of oncogenic client proteins. Researchers have focused on the recombinant expression of AHSA2 to study its structure and function, with an aim to develop potential therapeutic strategies that target its interaction with Hsp90 and its client proteins. The ability to produce AHSA2 in vitro allows for detailed biochemical assays and structural analysis, shedding light on its mechanism of action and revealing potential binding sites for small molecule inhibitors. Furthermore, the investigation into AHSA2’s role in stress response mechanisms highlights its importance in cellular homeostasis and provides insights into the development of strategies to manipulate its activity for therapeutic benefits. Consequently, AHSA2 has emerged as a promising target in cancer research and treatment, making the study of its recombinant protein an essential area of focus in molecular and cellular biology.
