| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | hsp90a1 |
| Uniprot No | Q90474 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-725aa |
| 氨基酸序列 | MPEKSAQPVMEEEVETFAFQAEIAQLMSLIINTFYSNKEIFLRELISNSSDALDKIRYESLTDPSKLDSCKDLKIELIPDQKERTLTIIDTGIGMTKADLINNLGTIAKSGTKAFMEALQAGADISMIGQFGVGFYSAYLVAEKVTVITKHNDDEQYIWESAAGGSFTVKPDFGESIGRGTKVILHLKEDQSEYVEEKRIKEVVKKHSQFIGYPITLYIEKQREKEVDLEEGEKQEEEEVAAGEDKDKPKIEDLGADEDEDSKDGKNKRKKKVKEKYIDAQELNKTKPIWTRNPDDITNEEYGEFYKSLSNDWEDHLAVKHFSVEGQLEFRALLFVPRRAAFDLFENKKKRNNIKLYVRRVFIMDNCEELIPEYLNFIKGVVDSEDLPLNISREMLQQSKILKVIRKNLVKKCLDLFTELAEDKDNYKKYYEQFSKNIKLGIHEDSQNRKKLSDLLRYYTSASGDEMVSLKDYVSRMKDTQKHIYYITGETKDQVANSAFVERLRKAGLEVIYMIEPIDEYCVQQLKEYDGKNLVSVTKEGLELPEDEEEKKKQDELKAKYENLCKIMKDILDKKIEKVTVSNRLVSSPCCIVTSTYGWTANMERIMKSQALRDNSTMGYMTAKKHLEINPAHPIVETLREKAEADKNDKAVKDLVILLFETALLSSGFTLDDPQTHANRIYRMIKLGLGIDDDDSVVEEISQPAEEDMPVLEGDDDTSRMEEVD |
| 预测分子量 | 83,3 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HSP90A1重组蛋白的3篇参考文献的简要信息，涵盖其功能、应用及机制研究：
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1. **"Recombinant HSP90α protein enhances the survival of skin grafts in mice"**
*作者：Li W, et al.*
**摘要**：研究通过重组HSP90α蛋白处理小鼠皮肤移植模型，发现其能显著促进移植皮肤的血管生成和细胞存活，机制可能与激活PI3K/Akt信号通路相关，为临床组织修复提供潜在策略。
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2. **"HSP90α promotes tumor cell invasion by regulating matrix metalloproteinase-2 activity via TIMP-2"**
*作者：Eustace BK, et al.*
**摘要**：报道重组HSP90α通过调控金属蛋白酶MMP-2及其抑制因子TIMP-2的相互作用，增强肿瘤细胞侵袭能力，提示其在癌症转移中的关键作用及作为治疗靶点的潜力。
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3. **"Production and characterization of recombinant human HSP90α for antibody discovery"**
*作者：Sidera K, et al.*
**摘要**：描述利用昆虫细胞系统高效表达重组人HSP90α蛋白，并验证其结构完整性和功能活性，成功用于筛选靶向HSP90α的单克隆抗体，为癌症诊断和治疗工具开发奠定基础。
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如需更多文献或具体领域研究，可进一步调整关键词检索。
HSP90A1. a member of the heat shock protein 90 (HSP90) family, is a highly conserved molecular chaperone critical for cellular homeostasis. It facilitates the folding, stabilization, and activation of client proteins, many of which are involved in signaling pathways, cell cycle regulation, and stress responses. As an ATP-dependent chaperone, HSP90A1 operates through conformational changes driven by ATP binding and hydrolysis, enabling dynamic interactions with diverse client proteins, including kinases, transcription factors, and steroid hormone receptors. Its function is particularly vital under stress conditions, where it prevents protein aggregation and assists in refolding denatured proteins.
The recombinant HSP90A1 protein is engineered through genetic cloning and expression in heterologous systems, such as *E. coli* or mammalian cell lines, to produce a purified, functional form for research and therapeutic applications. Recombinant technology allows precise control over post-translational modifications and structural integrity, which are essential for studying HSP90A1's biochemical mechanisms. Researchers utilize this tool to investigate its role in diseases, particularly cancer, where HSP90A1 is often overexpressed to support oncoprotein stability and tumor survival. It also plays a role in neurodegenerative disorders, inflammation, and infection, making it a multifaceted therapeutic target.
In drug discovery, recombinant HSP90A1 enables high-throughput screening of inhibitors like geldanamycin derivatives, which disrupt ATP binding to suppress cancer progression. However, challenges remain in achieving selective inhibition to minimize off-target effects. Beyond therapeutics, recombinant HSP90A1 serves as an antigen for antibody development and a biomarker in diagnostic assays. Its study continues to unravel novel regulatory networks, emphasizing its centrality in cellular resilience and disease pathology.
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