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.
以下是3篇关于CRYBB2(βB2-晶状体蛋白)重组蛋白研究的文献示例(注：文献信息为模拟概括，具体需以实际论文为准)：
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1. **标题**: "Expression and Purification of Recombinant Human CRYBB2 in Escherichia coli for Cataract Research"
**作者**: Zhang L, et al.
**摘要**: 本研究成功在大肠杆菌中表达了重组人CRYBB2蛋白，并通过亲和层析纯化获得高纯度蛋白。实验发现，重组CRYBB2在体外易形成聚集体，模拟了先天性白内障相关的蛋白异常聚集机制。
2. **标题**: "Structural Analysis of CRYBB2 Mutants Linked to Congenital Cataracts Using Recombinant Protein Models"
**作者**: Gupta R, et al.
**摘要**: 通过构建CRYBB2常见致病变异体(如p.R188H)，利用圆二色光谱和动态光散射分析发现，突变导致蛋白二级结构改变及热稳定性下降，揭示了白内障的分子病理机制。
3. **标题**: "CRYBB2 Recombinant Protein Rescues Lens Opacity in an In Vitro Cell Model"
**作者**: Wang Y, et al.
**摘要**: 在晶状体上皮细胞模型中，外源添加野生型重组CRYBB2蛋白可部分逆转由CRYBB2缺失引起的细胞氧化损伤和浑浊表型，为基因治疗提供潜在策略。
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**注**：以上内容为示例，实际文献需通过PubMed、Web of Science等平台检索关键词“CRYBB2 recombinant protein”或“CRYBB2 expression”获取。真实文献可能涉及重组蛋白的疾病机制、药物筛选或晶体结构解析等方向。
CRYBB2 (β-crystallin B2) is a member of the β/γ-crystallin superfamily, primarily expressed in the vertebrate eye lens. Encoded by the *CRYBB2* gene located on chromosome 22 in humans, it contributes to lens transparency and refractive properties by forming structural components of crystallins, which account for ~90% of lens proteins. β-crystallins, including CRYBB2. adopt a conserved two-domain "Greek key" fold, enabling tight packing and stability critical for maintaining lens integrity over decades. They typically form hetero- or homo-oligomers, with CRYBB2 interacting with other β-crystallins (e.g., CRYBB1. CRYBB3) to regulate solubility and prevent aggregation.
Mutations in *CRYBB2* are linked to congenital cataracts, a leading cause of childhood blindness. Over 20 pathogenic variants (e.g., Q155X, G220W) disrupt protein folding, solubility, or interactions, promoting light-scattering aggregates. These autosomal dominant or recessive mutations highlight CRYBB2's structural sensitivity and its role in lens homeostasis.
Recombinant CRYBB2 protein is produced via bacterial (e.g., *E. coli*) or mammalian expression systems for functional studies. Its production enables analysis of folding kinetics, aggregation mechanisms, and mutational effects in vitro. Researchers use techniques like X-ray crystallography, CD spectroscopy, and thermal stability assays to probe structure-function relationships. Recombinant CRYBB2 also aids in screening anti-cataract compounds and developing gene therapies. Despite challenges in expressing full-length soluble protein due to its aggregation-prone nature, advancements in fusion tags (e.g., His-tag) and refolding protocols have improved yields. Current studies focus on understanding CRYBB2's role in age-related cataracts and its potential as a therapeutic target, bridging basic research and clinical applications.
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