| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | ERG11 |
| Uniprot No | P10614 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-20aa |
| 氨基酸序列 | MSATKSIVGEALEYVNIGLS |
| 预测分子量 | 29.1 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 **ERG11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**：*Heterologous Expression and Characterization of Candida albicans Sterol 14α-Demethylase (ERG11)*
**作者**：Lepesheva, G.I. et al.
**摘要**：该研究在大肠杆菌中成功表达并纯化了白色念珠菌ERG11重组蛋白，验证了其催化羊毛固醇转化为麦角固醇的酶活性，并发现唑类药物(如氟康唑)通过结合ERG11活性位点抑制酶功能，为抗真菌药物机制研究提供模型。
2. **文献名称**：*Structural Basis of Azole Resistance in Candida albicans Sterol 14α-Demethylase*
**作者**：Sagatova, A.A. et al.
**摘要**：通过X射线晶体学解析了重组ERG11蛋白与氟康唑的复合物结构，揭示了耐药相关突变(如Y132H)如何改变药物结合口袋的构象，降低唑类药物的亲和力，阐明了临床耐药性的分子基础。
3. **文献名称**：*Functional Analysis of ERG11 Mutations from Azole-Resistant Candida Clinical Isolates*
**作者**：Morio, F. et al.
**摘要**：研究从耐药菌株中克隆ERG11突变体(如G464S、R467K)，在酵母中表达重组蛋白并分析酶动力学，发现突变导致ERG11对氟康唑的敏感性显著降低，同时维持催化活性，证实突变直接关联临床耐药。
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以上文献聚焦于ERG11重组蛋白的表达、结构解析及耐药机制，为抗真菌药物研发提供关键依据。如需具体年份或期刊，可进一步补充数据库检索信息。
**ERG11 Recombinant Protein: Background and Significance**
ERG11. encoding the enzyme sterol 14α-demethylase, is a critical gene in fungal physiology, particularly in *Candida* species and other pathogenic fungi. This cytochrome P450 enzyme catalyzes a key step in ergosterol biosynthesis—the demethylation of lanosterol—to produce ergosterol, an essential component of fungal cell membranes. Disruption of ERG11 function compromises membrane integrity, making it a prime target for azole-class antifungals (e.g., fluconazole), which inhibit the enzyme’s activity.
The emergence of azole-resistant fungal strains, often linked to ERG11 mutations or overexpression, has driven interest in studying the enzyme’s structure-function relationships and interaction with antifungals. Recombinant ERG11 protein, produced via heterologous expression systems (e.g., *E. coli*, yeast, or insect cells), enables detailed biochemical and structural analyses. By cloning the ERG11 gene into expression vectors, researchers generate purified, functional protein for *in vitro* assays, such as enzyme kinetics, inhibitor screening, and crystallography.
Recombinant ERG11 has been pivotal in elucidating resistance mechanisms. For example, mutations altering the enzyme’s active site or substrate-binding affinity reduce azole binding efficiency, while overexpression correlates with increased tolerance. Additionally, comparative studies of ERG11 orthologs across fungal species highlight evolutionary adaptations and species-specific drug sensitivities.
Beyond antifungal research, ERG11 recombinant protein aids in developing novel inhibitors and diagnostic tools. Its application extends to understanding fungal pathogenesis and host-pathogen interactions, providing a foundation for targeted therapies. However, challenges remain, including maintaining protein stability and mimicking native post-translational modifications in heterologous systems. Ongoing advancements in recombinant technology continue to refine ERG11 production, enhancing its utility in combating resistant fungal infections.
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