纯度 | >90%SDS-PAGE. |
种属 | Human |
靶点 | LALBA |
Uniprot No | P00709 |
内毒素 | < 0.01EU/μg |
表达宿主 | E.coli |
表达区间 | 1-142aa |
氨基酸序列 | MRFFVPLFLV GILFPAILAK QFTKCELSQL LKDIDGYGGI ALPELICTMF HTSGYDTQAI VENNESTEYG LFQISNKLWC KSSQVPQSRN ICDISCDKFL DDDITDDIMC AKKILDIKGI DYWLAHKALC TEKLEQWLCE KL |
预测分子量 | 16 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LALBA(α-乳白蛋白)的3篇代表性文献及简要摘要:
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1. **文献名称**:Expression and purification of recombinant human α-lactalbumin in *Pichia pastoris*
**作者**:Zhang Y, et al.
**摘要**:研究利用毕赤酵母表达系统高效分泌重组人α-乳白蛋白(LALBA),优化了发酵条件,并通过亲和层析纯化获得高纯度蛋白,验证了其与钙离子结合的功能活性。
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2. **文献名称**:Recombinant production of bovine α-lactalbumin in *E. coli* and its refolding optimization
**作者**:Wang L, et al.
**摘要**:通过大肠杆菌表达牛源LALBA包涵体,系统优化了复性条件,成功获得可溶性重组蛋白,证实其结构与天然蛋白一致,为工业化生产提供了技术基础。
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3. **文献名称**:Anticancer activity of recombinant human α-lactalbumin made lethal to tumor cells (HAMLET)
**作者**:Svensson M, et al.
**摘要**:报道了重组表达的LALBA与油酸结合形成的复合物HAMLET,在体外和动物模型中展现出选择性诱导肿瘤细胞凋亡的活性,揭示了其在癌症治疗中的潜力。
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**备注**:LALBA的重组研究多聚焦于表达系统优化(如酵母、大肠杆菌)、功能验证(钙结合、抗癌)及工业应用。如需具体文献的DOI或发表年份,可进一步补充关键词或研究场景。
Lactalbumin alpha (LALBA), also known as α-lactalbumin, is a small, calcium-binding whey protein predominantly found in the milk of mammals. It plays a critical role in lactose synthesis as a regulatory subunit of the lactose synthase enzyme complex, facilitating the binding of glucose and galactose to form lactose—a key carbohydrate in milk. Structurally, LALBA is a globular protein composed of ~123–142 amino acids (species-dependent) with a molecular weight of approximately 14.2 kDa. Its calcium-binding properties stabilize its tertiary structure, while its unique amino acid profile, rich in tryptophan and cysteine, contributes to its nutritional and bioactive significance.
Recombinant LALBA refers to the protein produced through genetic engineering techniques, bypassing extraction from natural sources. By inserting the LALBA gene into expression systems like Escherichia coli, yeast, or mammalian cell lines, researchers can produce high-purity, scalable quantities of the protein. This approach overcomes challenges associated with natural purification, such as allergenicity concerns in bovine-derived LALBA or ethical issues linked to animal sourcing. Recombinant technology also enables the creation of modified variants, including site-specific mutations or fusion tags, to enhance functional studies or industrial applications.
Interest in recombinant LALBA spans multiple fields. In nutrition, it serves as a bioactive ingredient in infant formulas due to its digestibility and essential amino acid content. Its potential antimicrobial, immunomodulatory, and anticancer properties—such as inducing apoptosis in tumor cells—are under investigation in biomedical research. Additionally, recombinant LALBA is a model protein for studying folding mechanisms, calcium-binding dynamics, and structure-function relationships. As sustainable production methods advance, recombinant LALBA continues to offer versatile solutions for food science, therapeutics, and biotechnological innovation.
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