纯度 | >90%SDS-PAGE. |
种属 | Human |
靶点 | 7-DHC |
Uniprot No | Q9UBM7 |
内毒素 | < 0.01EU/μg |
表达宿主 | E.coli |
表达区间 | 1-475aa |
氨基酸序列 | MAAKSQPNIPKAKSLDGVTNDRTASQGQWGRAWEVDWFSLASVIFLLLFAPFIVYYFIMACDQYSCALTGPVVDIVTGHARLSDIWAKTPPITRKAAQLYTLWVTFQVLLYTSLPDFCHKFLPGYVGGIQEGAVTPAGVVNKYQINGLQAWLLTHLLWFANAHLLSWFSPTIIFDNWIPLLWCANILGYAVSTFAMVKGYFFPTSARDCKFTGNFFYNYMMGIEFNPRIGKWFDFKLFFNGRPGIVAWTLINLSFAAKQRELHSHVTNAMVLVNVLQAIYVIDFFWNETWYLKTIDICHDHFGWYLGWGDCVWLPYLYTLQGLYLVYHPVQLSTPHAVGVLLLGLVGYYIFRVANHQKDLFRRTDGRCLIWGRKPKVIECSYTSADGQRHHSKLLVSGFWGVARHFNYVGDLMGSLAYCLACGGGHLLPYFYIIYMAILLTHRCLRDEHRCASKYGRDWERYTAAVPYRLLPGIF |
预测分子量 | 54,4 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7-DHC(7-脱氢胆固醇)重组蛋白的假设性参考文献示例(内容基于领域常见研究方向虚构,仅供参考格式):
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1. **文献名称**:*Recombinant Expression and Functional Characterization of Human 7-Dehydrocholesterol Reductase (DHCR7)*
**作者**:Smith A, et al.
**摘要**:本研究通过昆虫细胞表达系统成功制备重组人DHCR7蛋白,并验证其催化7-DHC转化为胆固醇的酶活性,为史密斯-莱姆利-奥皮茨综合征(SLOS)的分子机制研究提供了工具。
2. **文献名称**:*Optimization of 7-DHC Binding Protein Production in E. coli for Drug Screening*
**作者**:Johnson B, et al.
**摘要**:开发了一种高效大肠杆菌表达体系,生产可特异性结合7-DHC的重组蛋白,用于高通量筛选调节胆固醇代谢的潜在药物分子。
3. **文献名称**:*Structural Analysis of 7-DHC Stabilized by Recombinant Carriers in vitro*
**作者**:Chen L, et al.
**摘要**:利用重组载体蛋白在体外稳定7-DHC,结合X射线晶体学解析其复合物结构,揭示了7-DHC与载体蛋白相互作用的分子基础。
4. **文献名称**:*Therapeutic Potential of Recombinant DHCR7 in SLOS Cellular Models*
**作者**:Wang Y, et al.
**摘要**:在SLOS患者来源的细胞模型中导入重组DHCR7蛋白,显著恢复胆固醇合成通路功能,为酶替代疗法提供实验依据。
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**说明**:以上文献为示例性内容,实际研究中需检索PubMed、Google Scholar等数据库获取真实文献。建议结合关键词如“7-DHC recombinant protein”“DHCR7 expression”“cholesterol biosynthesis”等进行精准查询。
7-Dehydrocholesterol (7-DHC) is a critical intermediate in the cholesterol biosynthesis pathway, serving as the immediate precursor for both cholesterol and vitamin D3. Its role in human physiology has garnered significant attention, particularly in the context of Smith-Lemli-Opitz syndrome (SLOS), a rare genetic disorder caused by mutations in the DHCR7 gene. This gene encodes the enzyme 7-dehydrocholesterol reductase (DHCR7), which catalyzes the reduction of 7-DHC to cholesterol. Impaired DHCR7 activity leads to the accumulation of 7-DHC and a deficiency in cholesterol, resulting in developmental and neurological abnormalities.
Recombinant 7-DHC-associated proteins, including recombinant DHCR7. are engineered to study the molecular mechanisms underlying SLOS and to develop therapeutic strategies. These proteins are typically produced using heterologous expression systems such as E. coli, yeast, or mammalian cell lines. Recombinant DHCR7. for instance, enables researchers to analyze enzyme kinetics, substrate specificity, and the impact of genetic mutations on catalytic activity. This approach has facilitated high-throughput screening of potential small-molecule correctors or chaperones to restore DHCR7 function in SLOS patients.
Beyond disease research, recombinant 7-DHC-related proteins are valuable tools for industrial applications, including the biosynthesis of vitamin D3 and steroid derivatives. Optimizing their production involves addressing challenges like protein stability, solubility, and post-translational modifications. Recent advances in protein engineering and expression system optimization have improved yields and functional fidelity, enhancing their utility in both basic research and translational medicine. Overall, recombinant 7-DHC proteins represent a bridge between understanding metabolic disorders and developing targeted interventions.
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