| 纯度 | >90%SDS-PAGE. |
| 种属 | E.coli |
| 靶点 | bLg |
| Uniprot No | Q29614 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-174aa |
| 氨基酸序列 | MKFLLLTVGLALIGAIQAVENIRSKNDLGVEKFVGSWYLREAAKTMEFSIPLFDMDIKEVNLTPEGNLELVLLEKADRCVEKKLLLKKTQKPTEFEIYISSESASYTFSVMETDYDSYFLFCLYNISDREKMACAHYVRRIEENKGMNEFKKILRTLAMPYTVIEVRTRDMCHV |
| 预测分子量 | 20,2 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条关于β-乳球蛋白(β-Lactoglobulin, BLG)重组蛋白研究的参考文献示例(注：部分信息为模拟虚构，仅用于展示格式)：
1. **"Heterologous expression and purification of recombinant β-lactoglobulin in Escherichia coli"**
*作者：Zhang et al., 2015*
**摘要**：研究通过在大肠杆菌中克隆并表达重组BLG，优化了表达条件(如诱导温度、IPTG浓度)，并通过亲和层析纯化获得高纯度蛋白，验证了其结构与天然BLG的相似性。
2. **"Allergenicity assessment of recombinant β-lactoglobulin produced in Pichia pastoris"**
*作者：Müller et al., 2018*
**摘要**：利用毕赤酵母系统表达重组BLG，通过免疫印迹和患者血清IgE结合实验发现，重组蛋白的致敏性低于天然BLG，提示其在低致敏性乳制品开发中的潜力。
3. **"Recombinant BLG as a nanocarrier for hydrophobic nutrient delivery"**
*作者：Wang & Chen, 2020*
**摘要**：证实重组BLG可通过自组装包埋维生素D3.显著提高其水溶性和体外释放稳定性，为功能性食品开发提供了新策略。
4. **"Site-specific glycosylation of recombinant β-lactoglobulin alters its thermal stability"**
*作者：Kuroda et al., 2022*
**摘要**：通过基因工程技术在BLG特定位点引入糖基化修饰，发现修饰后蛋白的热稳定性显著增强，拓展了其在高温加工食品中的应用。
(注：以上文献为示例，实际引用需以真实出版物为准。)
**Background of Recombinant β-Lactoglobulin (BLG)**
β-Lactoglobulin (BLG), a small whey protein predominantly found in ruminant milk, is a member of the lipocalin family. It comprises 162 amino acids, folds into a β-barrel structure, and functions as a carrier for hydrophobic molecules like retinol and fatty acids. Historically studied for its role in milk digestion and allergenicity, BLG has gained attention in biotechnology due to its stability, binding properties, and potential applications in food and pharmaceutical industries.
Traditional BLG extraction from animal milk faces challenges, including allergenicity concerns, ethical issues, and batch variability. Recombinant DNA technology offers a sustainable alternative by enabling BLG production in microbial or mammalian expression systems. For instance, *E. coli*, yeast, or insect cells are engineered to express the BLG gene, ensuring controlled, scalable, and allergen-free synthesis. This approach also allows structural modifications (e.g., reducing immunogenicity or enhancing functionality) through site-directed mutagenesis.
Recombinant BLG is explored for diverse applications: as a nutraceutical carrier, a scaffold for drug delivery, or a bioactive ingredient in functional foods. Its ability to form gels or stabilize emulsions makes it valuable in food texture engineering. In biomedicine, modified BLG shows promise in targeted therapies or vaccine development. However, challenges remain, including achieving proper post-translational modifications in microbial systems and ensuring cost-effective large-scale production.
Overall, recombinant BLG represents a convergence of dairy science and synthetic biology, addressing sustainability and customization needs while mitigating traditional limitations. Ongoing research focuses on optimizing expression platforms and expanding its utility in precision nutrition and therapeutics.
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