| 纯度 | >90%SDS-PAGE. |
| 种属 | E.coli |
| 靶点 | ERG26 |
| Uniprot No | P53199 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-349aa |
| 氨基酸序列 | MSKIDSVLIIGGSGFLGLHLIQQFFDINPKPDIHIFDVRDLPEKLSKQFTFNVDDIKFHKGDLTSPDDMENAINESKANVVVHCASPMHGQNPDIYDIVNVKGTRNVIDMCKKCGVNILVYTSSAGVIFNGQDVHNADETWPIPEVPMDAYNETKAIAEDMVLKANDPSSDFYTVALRPAGIFGPGDRQLVPGLRQVAKLGQSKFQIGDNNNLFDWTYAGNVADAHVLAAQKLLDPKTRTAVSGETFFITNDTPTYFWALARTVWKADGHIDKHVIVLKRPVAICAGYLSEWVSKMLGKEPGLTPFRVKIVCAYRYHNIAKAKKLLGYTPRVGIEEGINKTLAWMDEGL |
| 预测分子量 | 46.1 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ERG26重组蛋白的3篇代表性文献的简要列举(注：以下内容基于领域内典型研究方向虚构，实际文献需通过数据库核实)：
1. **文献名称**：*"Functional characterization of recombinant ERG26 protein in Saccharomyces cerevisiae sterol biosynthesis"*
**作者**：Smith J, et al.
**摘要**：本研究成功在大肠杆菌中重组表达并纯化了酵母ERG26蛋白，证实其催化麦角固醇生物合成中C-3脱氢步骤的活性，并揭示其依赖NADPH的氧化还原机制。
2. **文献名称**：*"Crystallographic analysis of ERG26 reveals structural insights into fungal sterol modification"*
**作者**：Wang L, et al.
**摘要**：通过X射线晶体学解析了重组ERG26蛋白的三维结构，发现其活性位点关键氨基酸残基与底物结合模式，为抗真菌药物靶点设计提供结构基础。
3. **文献名称**：*"ERG26 gene knockout and recombinant complementation in Candida albicans: Implications for azole resistance"*
**作者**：Garcia-Rodriguez R, et al.
**摘要**：利用重组ERG26蛋白回补实验证明，该基因缺失导致白色念珠菌麦角固醇合成缺陷及唑类药物敏感性增强，提示ERG26在真菌耐药性中的调控作用。
建议通过PubMed或Web of Science检索关键词 "ERG26 recombinant" "sterol biosynthesis" 获取最新实证文献。
**Background of ERG26 Recombinant Protein**
ERG26 is a gene encoding a key enzyme involved in sterol biosynthesis, primarily studied in eukaryotic organisms such as yeast (*Saccharomyces cerevisiae*) and fungi. The ERG26 protein, also known as C-3 sterol dehydrogenase (C-3DH), catalyzes a critical step in the ergosterol biosynthesis pathway—the conversion of 4-methylzymosterol-4-carboxylate to zymosterol. Ergosterol, a fungal-specific sterol analogous to cholesterol in mammals, is essential for maintaining membrane fluidity, cell integrity, and function in fungi.
The production of recombinant ERG26 protein enables detailed biochemical and structural studies to elucidate its enzymatic mechanism, substrate specificity, and interactions with inhibitors. This is particularly relevant for antifungal drug development, as ergosterol biosynthesis is a major target of antifungals (e.g., azoles). Dysregulation of ERG26 or mutations in its coding gene can lead to compromised sterol profiles, affecting fungal viability and stress responses.
Recombinant ERG26 is typically expressed in heterologous systems like *E. coli* or insect cells, followed by purification via affinity chromatography. Studies using the recombinant protein have revealed insights into sterol intermediate processing and regulatory checkpoints in the pathway. Additionally, ERG26 homologs in plants and mammals (e.g., human NSDHL) share functional similarities, making it a model for understanding conserved sterol metabolism mechanisms and related disorders (e.g., congenital hemidysplasia).
Overall, ERG26 recombinant protein serves as a vital tool for exploring sterol biology, antifungal resistance mechanisms, and therapeutic strategies targeting lipid metabolism.
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