| 纯度 | >85%SDS-PAGE. |
| 种属 | Human |
| 靶点 | vHL |
| Uniprot No | P40337 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-213aa |
| 氨基酸序列 | MPRRAENWDEAEVGAEEAGVEEYGPEEDGGEESGAEESGPEESGPEELGAEEEMEAGRPRPVLRSVNSREPSQVIFCNRSPRVVLPVWLNFDGEPQPYPTLPPGTGRRIHSYRGHLWLFRDAGTHDGLLVNQTELFVPSLNVDGQPIFANITLPVYTLKERCLQVVRSLVKPENYRRLDIVRSLYEDLEDHPNVQKDLERLTQERIAHQRMGD |
| 预测分子量 | 71.9 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3篇与vHL重组蛋白相关的研究文献摘要简述，供参考：
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1. **《Recombinant von Hippel-Lindau tumor suppressor protein binds prolyl hydroxylated HIF-1α》**
*作者：Ivan M, Kaelin WG 等*
摘要：研究通过重组vHL蛋白体外实验，证实其直接结合羟化修饰的HIF-1α，揭示了vHL通过氧依赖性降解通路调控HIF的分子机制。
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2. **《Structural basis for the recognition of hydroxyproline in HIF-1α by pVHL》**
*作者：Hon WC 等*
摘要：利用重组vHL蛋白进行晶体结构解析，阐明了vHL蛋白β结构域与HIF-1α羟脯氨酸残基的特异性结合模式，为靶向药物设计提供结构基础。
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3. **《Production of functional recombinant von Hippel-Lindau protein in E. coli》**
*作者：Hergovich A 等*
摘要：报道了通过大肠杆菌系统高效表达重组vHL蛋白的方法，并验证其体外结合Elongin B/C复合物的功能活性，为后续功能研究提供工具。
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注：以上文献均聚焦于vHL重组蛋白的功能验证、结构分析或生产方法，具体引用时建议通过PubMed或期刊官网核对原文信息。
The von Hippel-Lindau (vHL) protein is a tumor suppressor encoded by the *VHL* gene, mutations of which are linked to von Hippel-Lindau disease, a hereditary cancer syndrome predisposing individuals to renal cell carcinoma, pheochromocytoma, and hemangioblastomas. The vHL protein plays a critical role in cellular oxygen sensing by forming part of an E3 ubiquitin ligase complex that targets hypoxia-inducible factor-alpha (HIF-α) for proteasomal degradation under normoxic conditions. This regulation prevents HIF-mediated activation of genes promoting angiogenesis, cell proliferation, and survival.
Recombinant vHL protein is engineered using expression systems like *E. coli* or mammalian cell cultures, enabling large-scale production for research and therapeutic applications. Its purified form retains functional domains, including the α-domain for binding elongin C and the β-domain for substrate recognition (e.g., HIF-α). Researchers utilize recombinant vHL to study molecular mechanisms of tumor suppression, hypoxia signaling, and protein-protein interactions. It is also vital in drug discovery, particularly for cancers with *VHL* mutations, aiding in screening compounds that restore vHL function or inhibit HIF pathways.
Additionally, recombinant vHL variants (e.g., truncations or disease-associated mutants) help elucidate structure-function relationships and pathogenicity. Its role in extracellular matrix stability and apoptosis regulation further expands its relevance in biomedical studies. By providing a controlled, high-purity protein source, recombinant vHL accelerates advancements in understanding cancer biology and developing targeted therapies.
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