| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | HSP90aB1 |
| Uniprot No | P08238 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 2-724aa |
| 氨基酸序列 | PEEVHHGEEEVETFAFQAEIAQLMSLIINTFYSNKEIFLRELISNASDALDKIRYESLTDPSKLDSGKELKIDIIPNPQERTLTLVDTGIGMTKADLINNLGTIAKSGTKAFMEALQAGADISMIGQFGVGFYSAYLVAEKVVVITKHNDDEQYAWESSAGGSFTVRADHGEPIGRGTKVILHLKEDQTEYLEERRVKEVVKKHSQFIGYPITLYLEKEREKEISDDEAEEEKGEKEEEDKDDEEKPKIEDVGSDEEDDSGKDKKKKTKKIKEKYIDQEELNKTKPIWTRNPDDITQEEYGEFYKSLTNDWEDHLAVKHFSVEGQLEFRALLFIPRRAPFDLFENKKKKNNIKLYVRRVFIMDSCDELIPEYLNFIRGVVDSEDLPLNISREMLQQSKILKVIRKNIVKKCLELFSELAEDKENYKKFYEAFSKNLKLGIHEDSTNRRRLSELLRYHTSQSGDEMTSLSEYVSRMKETQKSIYYITGESKEQVANSAFVERVRKRGFEVVYMTEPIDEYCVQQLKEFDGKSLVSVTKEGLELPEDEEEKKKMEESKAKFENLCKLMKEILDKKVEKVTISNRLVSSPCCIVTSTYGWTANMERIMKAQALRDNSTMGYMMAKKHLEINPDHPIVETLRQKAEADKNDKAVKDLVVLLFETALLSSGFSLEDPQTHSNRIYRMIKLGLGIDEDEVAAEEPNAAVPDEIPPLEGDEDASRMEEVD |
| 预测分子量 | 84.0 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HSP90AB1重组蛋白的3篇参考文献示例(注：文献信息为示例性概括，实际引用需核实具体来源)：
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1. **"Structural and functional analysis of human HSP90β recombinant protein in ATPase activity"**
*作者：Prodromou C, et al. (2000)*
**摘要**：研究报道了重组人HSP90β蛋白的表达与纯化方法，并分析了其ATP酶活性特征。通过晶体结构解析，揭示了HSP90β的ATP结合域构象变化对分子伴侣功能的影响。
2. **"HSP90AB1 as a therapeutic target in cancer: Role of recombinant protein in client protein stabilization"**
*作者：Trepel J, et al. (2010)*
**摘要**：探讨了重组HSP90β蛋白在癌细胞中与客户蛋白(如AKT、EGFR)的相互作用，证明其通过稳定致癌蛋白促进肿瘤进展，为HSP90抑制剂开发提供实验依据。
3. **"Recombinant HSP90β enhances stress resilience in vitro by modulating oxidative stress pathways"**
*作者：Chen B, et al. (2015)*
**摘要**：利用重组HSP90β蛋白验证其在细胞应激反应中的作用，发现其过表达可减少氧化损伤并提高细胞存活率，机制涉及Nrf2信号通路的激活。
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如需具体文献，建议通过PubMed或Google Scholar以关键词“HSP90AB1 recombinant protein”搜索最新研究，并优先选择高影响力期刊论文。
HSP90AB1. a member of the heat shock protein 90 (HSP90) family, is a molecular chaperone critical for maintaining cellular homeostasis under stress conditions. It plays a central role in folding, stabilizing, and activating client proteins, many of which are involved in signal transduction, cell cycle regulation, and stress response. Unlike its isoform HSP90AA1. HSP90AB1 (also known as HSP90β) is constitutively expressed and contributes to basal cellular functions, even in non-stressed environments. Structurally, it contains three domains: an N-terminal ATP-binding domain, a middle domain for client protein interaction, and a C-terminal dimerization domain.
Recombinant HSP90AB1 protein is produced via genetic engineering, typically using bacterial (e.g., *E. coli*) or mammalian expression systems. This allows large-scale production of the purified protein for research and therapeutic applications. The recombinant form retains its functional properties, including ATPase activity and client protein-binding capacity, making it invaluable for studying HSP90-mediated pathways, drug screening, and structural biology. Its applications extend to cancer research, as HSP90AB1 overexpression is linked to tumor progression, drug resistance, and poor prognosis. Inhibitors targeting HSP90 (e.g., geldanamycin derivatives, 17-AAG) are under investigation for anticancer therapies.
Additionally, HSP90AB1 is implicated in neurodegenerative diseases, inflammation, and infection, highlighting its broad biomedical relevance. Recombinant HSP90AB1 serves as a tool to explore these roles and develop targeted therapies, emphasizing its dual utility in basic science and translational medicine.
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