| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | SCD |
| Uniprot No | O00767 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-359aa |
| 氨基酸序列 | MPAHLLQDDISSSYTTTTTITAPPSRVLQNGGDKLETMPLYLEDDIRPDIKDDIYDPTYKDKEGPSPKVEYVWRNIILMSLLHLGALYGITLIPTCKFYTWLWGVFYYFVSALGITAGAHRLWSHRSYKARLPLRLFLIIANTMAFQNDVYEWARDHRAHHKFSETHADPHNSRRGFFFSHVGWLLVRKHPAVKEKGSTLDLSDLEAEKLVMFQRRYYKPGLLMMCFILPTLVPWYFWGETFQNSVFVATFLRYAVVLNATWLVNSAAHLFGYRPYDKNISPRENILVSLGAVGEGFHNYHHSFPYDYSASEYRWHINFTTFFIDCMAALGLAYDRKKVSKAAILARIKRTGDGNYKSG |
| 预测分子量 | 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3篇关于SCD(Stearoyl-CoA Desaturase)重组蛋白研究的模拟参考文献(注：文献为虚构示例，仅供格式参考)：
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1. **文献名称**: "Heterologous Expression and Characterization of Recombinant SCD1 in Escherichia coli"
**作者**: Zhang et al.
**摘要**: 本研究成功在大肠杆菌中表达了人源SCD1重组蛋白，通过优化诱导条件和纯化步骤获得高纯度蛋白。酶活分析表明，重组SCD1具有催化硬脂酰-CoA转化为油酰-CoA的功能，为体外脂肪酸代谢研究提供了工具。
2. **文献名称**: "Structural Insights into SCD2 Recombinant Protein via Cryo-EM"
**作者**: Li & Wang
**摘要**: 利用昆虫细胞表达系统制备了鼠源SCD2重组蛋白，并通过冷冻电镜解析其三维结构。研究发现SCD2的活性中心具有独特的疏水通道结构，揭示了底物特异性机制，为靶向抑制剂设计奠定基础。
3. **文献名称**: "Functional Analysis of Recombinant SCD in Cancer Cell Lipid Metabolism"
**作者**: Chen et al.
**摘要**: 通过哺乳动物细胞表达系统生产功能性SCD重组蛋白，并验证其在癌细胞模型中对脂质合成的调控作用。实验表明，SCD过表达显著增加单不饱和脂肪酸含量，促进肿瘤细胞增殖，提示其作为抗癌靶点的潜力。
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(注：实际文献需通过PubMed/Google Scholar等平台检索关键词如"recombinant SCD protein"、"SCD heterologous expression"获取。)
**Background of SCD Recombinant Proteins**
Stearoyl-CoA desaturase (SCD) is a rate-limiting enzyme that catalyzes the conversion of saturated fatty acids (SFAs) into monounsaturated fatty acids (MUFAs), primarily palmitoleic acid (C16:1) and oleic acid (C18:1). This process is critical for maintaining cellular membrane fluidity, lipid metabolism, and energy homeostasis. SCD activity is tightly linked to metabolic disorders, including obesity, diabetes, and cardiovascular diseases, making it a potential therapeutic target.
Recombinant SCD proteins are engineered using genetic cloning techniques, where the SCD gene is inserted into expression vectors (e.g., bacterial, mammalian, or insect cell systems) to produce purified, functional enzymes. These proteins retain catalytic activity and structural integrity, enabling researchers to study SCD's biochemical properties, substrate specificity, and interactions with inhibitors or activators in controlled environments.
The development of recombinant SCD has advanced drug discovery, particularly in metabolic and cancer research. For instance, SCD overexpression is associated with tumor progression and chemotherapy resistance, prompting investigations into SCD inhibitors as anticancer agents. Additionally, recombinant SCD facilitates high-throughput screening for compounds that modulate its activity, aiding in the design of therapies for metabolic syndromes.
Challenges in SCD recombinant production include its transmembrane nature and hydrophobicity, which complicate solubilization and purification. Advances in protein engineering, such as codon optimization, fusion tags, and membrane mimetics, have improved yields and stability.
Overall, recombinant SCD proteins serve as vital tools for unraveling lipid metabolism mechanisms and developing targeted treatments, bridging gaps between biochemical research and clinical applications. Their use continues to expand our understanding of SCD's role in health and disease.
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