Analytical Data
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基因名
AHSA2
- Application
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别名
Activator of 90 kDa heat shock Protein ATPase homolog 2; AHA1
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种属
Human
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表达系统
E. coli
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标签
GST-tag at N-terminal
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纯度
Greater than 90% as determined by SDS-PAGE.
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蛋白编号
Q719I0
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表达区间
1-137aa
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氨基酸序列
MILPTKAMATQELTVKRKLSGNTLQVQASSPVALGVRIPTVALHMMELFDTTVEQLYSIFTVKELTNKKIIMKWRCGNWPEEHYAMVALNFVPTLGQTELQLKEFLSICKEENMKFCWQKQHFEEIKGSLQLTPLNG
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分子量
42.1 kDa
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内毒素
< 1.0 EU per μg protein as determined by the LAL method.
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性状
Freeze-dried powder
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缓冲液
PBS, pH7.4, containing 0.01% SKL, 1mM DTT, 5% Trehalose and Proclin300.
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复溶方法
Reconstitute in ddH2O to a concentration of 0.1-0.5 mg/mL. Do not vortex.
- 个性化定制
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稳定性测试
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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保存条件 & 期限
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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运输条件
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.












