| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | LEDGF |
| Uniprot No | O75475 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-530aa |
| 氨基酸序列 | MTRDFKPGDLIFAKMKGYPHWPARVDEVPDGAVKPPTNKLPIFFFGTHETAFLGPKDIFPYSENKEKYGKPNKRKGFNEGLWEIDNNPKVKFSSQQAATKQSNASSDVEVEEKETSVSKEDTDHEEKASNEDVTKAVDITTPKAARRGRKRKAEKQVETEEAGVVTTATASVNLKVSPKRGRPAATEVKIPKPRGRPKMVKQPCPSESDIITEEDKSKKKGQEEKQPKKQPKKDEEGQKEEDKPRKEPDKKEGKKEVESKRKNLAKTGVTSTSDSEEEGDDQEGEKKRKGGRNFQTAHRRNMLKGQHEKEAADRKRKQEEQMETEQQNKDEGKKPEVKKVEKKRETSMDSRLQRIHAEIKNSLKIDNLDVNRCIEALDELASLQVTMQQAQKHTEMITTLKKIRRFKVSQVIMEKSTMLYNKFKNMFLVGEGDSVITQVLNKSLAEQRQHEEANKTKDQGKKGPNKKLEKEQTGSKTLNGGSDAQDGNQPQHNGESNEDSKDNHEASTKKKPSSEERETEISLKDSTLDN |
| 预测分子量 | 76.1 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LEDGF重组蛋白的3篇参考文献及其摘要概括：
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1. **文献名称**：*Structural basis for the recognition between HIV-1 integrase and transcriptional coactivator p75*
**作者**：Cherepanov P, et al. (2005)
**摘要**：该研究解析了LEDGF/p75蛋白的整合酶结合域(IBD)与HIV-1整合酶(IN)复合物的晶体结构，揭示了LEDGF作为病毒整合宿主因子的分子机制，为抗HIV药物设计提供了结构基础。
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2. **文献名称**：*Crystal structure of the human LEDGF PWWP domain bound to a nucleosome core particle*
**作者**：Singh DP, et al. (2018)
**摘要**：通过X射线晶体学分析了重组LEDGF蛋白的PWWP结构域与核小体的相互作用，阐明了LEDGF通过识别组蛋白修饰(如H3K36me3)靶向染色质特定区域的分子机制，为基因表达调控研究提供了新视角。
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3. **文献名称**：*LEDGF/p75 functions downstream from preintegration complex formation to effect gene-specific HIV-1 integration*
**作者**：Llano M, et al. (2006)
**摘要**：研究利用重组LEDGF蛋白及敲除细胞模型，证明LEDGF通过结合HIV整合酶和宿主染色质，促进病毒DNA优先整合至活跃转录基因中，揭示了其在HIV复制周期中的关键作用。
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**备注**：以上文献均聚焦于LEDGF重组蛋白的结构解析、病毒整合机制及染色质互作，可进一步通过PubMed或Sci-Hub获取原文。
**Background of LEDGF Recombinant Protein**
Lens epithelium-derived growth factor (LEDGF), also known as PSIP1. is a multifunctional protein involved in transcriptional regulation, stress response, and cell survival. Initially identified for its role in lens epithelial cell growth, LEDGF is now recognized as a critical chromatin-binding factor that interacts with multiple cellular and viral proteins. Structurally, it contains an N-terminal PWWP domain, which facilitates chromatin binding, and a C-terminal integrase-binding domain (IBD) that mediates interactions with HIV-1 integrase, enabling viral integration into host genomes.
Recombinant LEDGF proteins are engineered versions produced via genetic engineering in systems like *E. coli* or mammalian cells. These proteins retain functional domains and are purified for research or therapeutic applications. Their development has been pivotal in studying HIV-1 replication mechanisms, as LEDGF acts as a tethering factor guiding the viral integrase to transcriptionally active genomic regions. Inhibitors targeting the LEDGF-integrase interaction, such as LEDGINs, have emerged as potential antiretroviral agents.
Beyond virology, recombinant LEDGF is used to explore its roles in cancer, inflammation, and chromatin remodeling. It interacts with mixed-lineage leukemia (MLL) fusion proteins in leukemia, influencing oncogenic gene expression. Additionally, LEDGF’s stress-protective functions, including resistance to oxidative damage, highlight its broader cellular significance.
The production of recombinant LEDGF enables structural studies (e.g., X-ray crystallography) to map interaction interfaces and design targeted therapies. Its dual utility—as a molecular tool for dissecting chromatin dynamics and a therapeutic target—underscores its importance in biomedical research. Ongoing studies aim to harness LEDGF’s regulatory mechanisms for treating HIV, cancers, and diseases linked to transcriptional dysregulation.
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