| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | aLA |
| Uniprot No | Q8IYS1 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-436aa |
| 氨基酸序列 | MRPGGERPVE GGACNGRSEL ELLKLRSAEC IDEAAERLGA LSRAIWSQPE LAYEEHHAHR VLTHFFEREP PAASWAVQPH YQLPTAFRAE WEPPEARAPS ATPRPLHLGF LCEYDALPGI GHACGHNLIA EVGAAAALGV RGALEGLPRP PPPVKVVVLG TPAEEDGGGK IDLIEAGAFT NLDVVFMAHP SQENAAYLPD MAEHDVTVKY YGKASHSASY PWEGLNALDA AVLAYNNLSV FRQQMKPTWR VHGIIKNGGV KPNIIPSYSE LIYYFRAPSM KELQVLTKKA EDCFRAAALA SGCTVEIKGG AHDYYNVLPN KSLWKAYMEN GRKLGIEFIS EDTMLNGPSG STDFGNVSFV VPGIHPYFHI GSNALNHTEQ YTEAAGSQEA QFYTLRTAKA LAMTALDVIF KPELLEGIRE DFKLKLQEEQ FVNAVE |
| 预测分子量 | 47,7 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. |
以下是关于重组α-乳白蛋白(aLA)的示例参考文献，内容基于典型研究方向合理虚构，仅供参考：
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1. **标题**：*Expression and Purification of Recombinant Human Alpha-Lactalbumin in Escherichia coli*
**作者**：Smith, J. et al.
**摘要**：研究通过大肠杆菌表达系统成功生产重组人α-乳白蛋白，优化了诱导条件和纯化工艺，获得高纯度蛋白，验证其钙离子结合活性，为工业化生产提供参考。
2. **标题**：*Functional Characterization of Recombinant aLA from Transgenic Tobacco Plants*
**作者**：Lee, S. & Kim, H.
**摘要**：利用植物生物反应器在烟草中表达重组aLA，证实其与天然蛋白相似的二级结构和乳糖合成酶活性，探讨其在功能性食品中的应用潜力。
3. **标题**：*Enhancing Solubility of Recombinant aLA via Fusion Tags in Pichia pastoris*
**作者**：Zhang, Y. et al.
**摘要**：通过在毕赤酵母表达系统中引入硫氧还蛋白融合标签，显著提高重组aLA的可溶性和产量，为解决包涵体问题提供新策略。
4. **标题**：*Recombinant aLA in Cancer Therapy: Mechanisms and Applications*
**作者**：Johnson, R. & Patel, M.
**摘要**：综述重组aLA的抑癌机制，包括诱导肿瘤细胞凋亡和调节免疫反应，并讨论其在靶向药物递送系统中的研究进展。
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**注**：以上文献为示例性质，实际研究中请通过学术数据库检索真实发表的论文。如需具体文献支持，可进一步提供研究方向或关键词优化检索。
**Background of Recombinant α-Lactalbumin (aLA)**
α-Lactalbumin (aLA) is a small, calcium-binding whey protein predominantly found in mammalian milk, playing a critical role in lactose synthesis during lactation. Structurally, it belongs to the lysozyme superfamily and consists of a single polypeptide chain with four disulfide bonds, conferring stability and a compact globular fold. Its primary biological function is to modulate galactosyltransferase activity, enabling the production of lactose in mammary glands. Beyond nutrition, aLA has garnered attention for its bioactive properties, including immunomodulatory, antimicrobial, and apoptotic effects, particularly in its partially unfolded, calcium-depleted state (HAMLET-like complexes).
Recombinant aLA is produced via genetic engineering, where the *LALBA* gene encoding human or bovine aLA is inserted into microbial (e.g., *E. coli*, yeast) or mammalian expression systems. This approach overcomes limitations of natural extraction, such as low yield, allergenicity (e.g., bovine aLA allergies), and ethical concerns. Recombinant technology enables scalable production, customization (e.g., site-specific mutations, fusion tags), and enhanced purity, making it suitable for biomedical and industrial applications.
In nutrition, recombinant aLA is explored for infant formula fortification due to its amino acid profile and bioavailability. In biomedicine, it serves as a carrier for drug delivery, leveraging its ability to bind fatty acids and membranes, and is studied for cancer therapy due to its selective tumoricidal activity. Additionally, recombinant variants are engineered to improve stability or functional properties, such as altered calcium affinity or protease resistance.
Overall, recombinant aLA exemplifies the fusion of biotechnology and protein science, offering sustainable, tailored solutions for healthcare, food technology, and beyond.
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