| 纯度 | > 90 % SDS-PAGE. |
| 种属 | Human |
| 靶点 | AHA1 |
| Uniprot No | O95433 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-338aa |
| 氨基酸序列 | SHMAKWGEGDPRWIVEERADATNVNNWHWTERDASNWSTDKLKTLFLAVQ VQNEEGKCEVTEVSKLDGEASINNRKGKLIFFYEWSVKLNWTGTSKSGVQ YKGHVEIPNLSDENSVDEVEISVSLAKDEPDTNLVALMKEEGVKLLREAM GIYISTLKTEFTQGMILPTMNGESVDPVGQPALKTEERKAKPAPSKTQAR PVGVKIPTCKITLKETFLTSPEELYRVFTTQELVQAFTHAPATLEADRGG KFHMVDGNVSGEFTDLVPEKHIVMKWRFKSWPEGHFATITLTFIDKNGET ELCMEGRGIPAPEEERTRQGWQRYYFEGIKQTFGYGARLF |
| 预测分子量 | 38 kDa |
| 蛋白标签 | His tag N-Terminus |
| 缓冲液 | PBS, pH7.4, containing 0.01% SKL, 1mM DTT, 5% Trehalose and Proclin300. |
| 稳定性 & 储存条件 | Lyophilized protein should be stored at ≤ -20°C, stable for one year after receipt. Reconstituted protein solution can be stored at 2-8°C for 2-7 days. Aliquots of reconstituted samples are stable at ≤ -20°C for 3 months. |
| 复溶 | Always centrifuge tubes before opening.Do not mix by vortex or pipetting. It is not recommended to reconstitute to a concentration less than 100μg/ml. Dissolve the lyophilized protein in distilled water. Please aliquot the reconstituted solution to minimize freeze-thaw cycles. |
以下是关于AHA1重组蛋白的3篇代表性文献的简要列举：
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1. **文献名称**：*Activation of the ATPase activity of Hsp90 by the stress-regulated cochaperone Aha1*
**作者**：Panaretou, B. et al.
**摘要**：该研究通过重组AHA1蛋白揭示了其作为Hsp90共伴侣蛋白的作用机制，证明AHA1通过增强Hsp90的ATP酶活性，促进客户蛋白(如激酶和类固醇受体)的构象成熟，为Hsp90功能调控提供了分子基础。
2. **文献名称**：*Structural and functional analysis of the Hsp90/Aha1 complex*
**作者**：Koulov, A.V. et al.
**摘要**：利用重组AHA1蛋白进行结构生物学分析，发现其N端结构域直接结合Hsp90的中间结构域，揭示了AHA1通过构象变化激活Hsp90的分子机制，并阐明了二者互作界面的关键氨基酸残基。
3. **文献名称**：*Aha1 binds to the middle domain of Hsp90 and contributes to client protein activation*
**作者**：Lotz, G.P. et al.
**摘要**：通过体外重构实验，发现重组AHA1蛋白通过增强Hsp90对客户蛋白(如p53和CFTR)的折叠能力，影响疾病相关蛋白的稳定性，提示AHA1可能成为癌症和囊性纤维化的治疗靶点。
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**备注**：上述文献主要聚焦于AHA1重组蛋白在Hsp90功能调控、结构互作及疾病关联中的研究。如需具体实验方法或最新进展，可进一步检索近年发表的相关论文。
AHA1 (Activator of Hsp90 ATPase homolog 1) is a co-chaperone protein that critically regulates the functional cycle of Hsp90 (Heat Shock Protein 90), a molecular chaperone essential for maintaining proteostasis in eukaryotic cells. Hsp90 facilitates the folding, activation, and stabilization of numerous client proteins, including kinases, transcription factors, and steroid hormone receptors, many of which are implicated in cancer, neurodegeneration, and other diseases. AHA1 enhances the ATPase activity of Hsp90. accelerating its conformational cycling and modulating substrate recognition. This interaction is structurally mediated through two distinct domains of AHA1: an N-terminal domain that binds the Hsp90 middle segment and a C-terminal domain interacting with the Hsp90 N-terminal ATP-binding pocket.
Recombinant AHA1 protein is engineered for in vitro studies to dissect its regulatory mechanisms, often expressed in bacterial (e.g., *E. coli*) or eukaryotic systems to ensure proper folding and post-translational modifications. Purified recombinant AHA1 enables biochemical assays, structural analyses (e.g., X-ray crystallography, cryo-EM), and drug discovery efforts targeting the Hsp90-AHA1 axis. Dysregulation of AHA1 has been linked to pathologies such as Alzheimer’s disease, where it promotes tau aggregation via Hsp90 hyperactivity, and cancer, where it stabilizes oncogenic clients like HER2 or BCR-ABL. Inhibiting AHA1-Hsp90 interactions has emerged as a therapeutic strategy to disrupt chaperone-dependent pathways without directly blocking Hsp90’s ATPase site, potentially reducing off-target effects. However, the pleiotropic roles of AHA1 in cellular stress responses and its tissue-specific expression patterns necessitate further research to clarify its context-dependent functions. Recombinant AHA1 tools remain pivotal in unraveling these complexities and advancing targeted therapies.
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