| 纯度 | >85%SDS-PAGE. |
| 种属 | Human |
| 靶点 | FDFT1 |
| Uniprot No | P37268 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-283aa |
| 氨基酸序列 | MGSSHHHHHH SSGLVPRGSH MGSMEFVKCL GHPEEFYNLV RFRIGGKRKV MPKMDQDSLS SSLKTCYKYL NQTSRSFAAV IQALDGEMRN AVCIFYLVLR ALDTLEDDMT ISVEKKVPLL HNFHSFLYQP DWRFMESKEK DRQVLEDFPT ISLEFRNLAE KYQTVIADIC RRMGIGMAEF LDKHVTSEQE WDKYCHYVAG LVGIGLSRLF SASEFEDPLV GEDTERANSM GLFLQKTNII RDYLEDQQGG REFWPQEVWS RYVKKLGDFA KPENIDLAVQ CLNELITNAL HHIPDVITYL SRLRNQ |
| 预测分子量 | 35 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FDFT1重组蛋白的3篇参考文献示例(注：内容为虚构，仅作格式参考)：
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1. **文献名称**：*High-yield Expression and Functional Analysis of Recombinant Human FDFT1 in Insect Cells*
**作者**：Chen H, et al.
**摘要**：研究利用杆状病毒-昆虫细胞系统表达人源FDFT1重组蛋白，优化表达条件后获得高活性蛋白，并验证其催化法尼基二磷酸生成角鲨烯的功能，为酶动力学研究提供基础。
2. **文献名称**：*Crystal Structure of FDFT1 Reveals Substrate Binding Sites for Cholesterol Biosynthesis*
**作者**：Yamamoto T, et al.
**摘要**：通过X射线晶体学解析FDFT1重组蛋白的三维结构，明确其底物结合域及催化活性中心，揭示了该酶在胆固醇合成中的构效关系。
3. **文献名称**：*Recombinant FDFT1 as a Target for Screening Natural Product Inhibitors in Hyperlipidemia Therapy*
**作者**：Gupta S, et al.
**摘要**：利用重组FDFT1蛋白建立体外抑制模型，筛选出多种天然产物来源的潜在抑制剂，为调控胆固醇代谢提供新药物开发策略。
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**说明**：以上文献摘要围绕FDFT1重组蛋白的**表达体系**、**结构解析**及**应用研究**展开，涵盖基础研究与转化方向。实际文献需通过PubMed、Web of Science等平台检索关键词“FDFT1 recombinant protein”获取。
FDFT1 (farnesyl-diphosphate farnesyltransferase 1), also known as squalene synthase (SQS), is a pivotal enzyme in the mevalonate pathway, catalyzing the head-to-head condensation of two farnesyl pyrophosphate (FPP) molecules to form squalene. This reaction represents the first committed step in cholesterol and sterol biosynthesis, making FDFT1 a critical regulatory node in cellular lipid metabolism. The enzyme is ubiquitously expressed, with particularly high activity in cholesterol-synthesizing tissues such as the liver, adrenal glands, and brain.
Recombinant FDFT1 protein is typically produced using heterologous expression systems (e.g., E. coli, yeast, or mammalian cells) to enable detailed biochemical and structural studies. Its 47-kDa structure contains multiple transmembrane domains, posing challenges for soluble expression that are often addressed through detergent solubilization or truncation strategies. Purification frequently employs affinity tags like His-tags combined with chromatographic techniques.
Research on recombinant FDFT1 has gained momentum due to its therapeutic potential. As a rate-limiting enzyme in cholesterol biosynthesis, it serves as a target for developing hypolipidemic agents and anticancer drugs. Small-molecule inhibitors of FDFT1. such as zaragozic acids, have shown promise in reducing cholesterol levels and suppressing tumor growth. The recombinant protein is instrumental in high-throughput screening for novel inhibitors, enzyme kinetics studies, and structural biology approaches like X-ray crystallography.
Moreover, FDFT1 dysregulation has been linked to metabolic disorders, neurodegenerative diseases, and Smith-Lemli-Opitz syndrome. Recombinant variants with specific mutations help elucidate genotype-phenotype correlations. Recent advances in cryo-EM and membrane protein engineering have enabled better characterization of its catalytic mechanism and interaction with lipid bilayers, providing insights for targeted drug design while minimizing off-target effects on other prenyltransferases.
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