| 纯度 | >90%SDS-PAGE. |
| 种属 | E.coli |
| 靶点 | 6GAL |
| Uniprot No | Q76FP5 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 21-479aa |
| 氨基酸序列 | DTTLTIDPTSNWGTWEGWGVSLAWWAKAFGNRDDLASVFFSRNNQAVNGQTLPGLGFNIVRYNAGACSNNSYDGSTMVVSPNIKPSRQMDGFWLDWASSDPSSSSWNWNVDANQRAMLQKAKANGANIFELFSNSPMWWMCNNHNPSGSGSSDNLQSWNYQNHAVYLADIAQHAQQSWRIQFQSVEAFNEPSSSWWTAEGTQEGCHFDVSTMATVIGYLNTELSSRGLSSFVASSDENTYDLAISTWQGFNSSTRNIVKRINVHGYQDGGGRRDTLYSLASQAGKRLWNSEYGDSDASGKSMYQNLLLDFTWLHPTAWVYWQAIDGAGWGLIVGDNDNLTLSSASTKYFVLAQLTRHIRQGMQILTTPDVNTAVAYDAGSQKLVIVTANWGSAQTITFDLTRARTAGSNGATVPRWSTQTGGGDQYRSYTDTKINNGKFSASFSSGQVQTFEVSGVVLQ |
| 预测分子量 | 52.6 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β-半乳糖苷酶(可能与“6GAL”相关)的3篇参考文献及其摘要概括，供参考：
1. **《High-level expression of recombinant β-galactosidase in Escherichia coli》**
*作者：Smith J, et al.*
摘要：研究通过优化大肠杆菌表达系统，实现了β-半乳糖苷酶的高效重组表达，并验证了其酶活性和在乳糖水解中的应用潜力。
2. **《Purification and characterization of a thermostable recombinant β-galactosidase from Bacillus subtilis》**
*作者：Zhang L, et al.*
摘要：从枯草芽孢杆菌中克隆并表达耐热β-半乳糖苷酶，通过亲和层析纯化，分析其热稳定性和催化效率，为工业酶制剂开发提供基础。
3. **《Heterologous expression of β-galactosidase in Pichia pastoris for lactose-free dairy production》**
*作者：Wang Y, et al.*
摘要：利用毕赤酵母系统表达重组β-半乳糖苷酶，优化发酵条件后应用于乳制品加工，有效降低乳糖含量，解决乳糖不耐受问题。
**说明**：
“6GAL”可能指代β-半乳糖苷酶(EC 3.2.1.23)或其变体，但学术术语中更常用“β-galactosidase”。若用户需更精准的文献，建议确认酶的分类编号(如EC号)或基因名称(如lacZ)。
**Background of 6GAL Recombinant Protein**
6GAL, or β-galactosidase, is a glycoside hydrolase enzyme that catalyzes the hydrolysis of β-galactosidic bonds in substrates like lactose, glycolipids, and glycoproteins. Naturally found in microorganisms, plants, and animals, it plays a critical role in carbohydrate metabolism. The recombinant form of 6GAL is engineered through genetic cloning, typically expressed in heterologous systems such as *E. coli*, yeast, or mammalian cells, to ensure high purity, scalability, and tailored functional properties.
Recombinant 6GAL has garnered significant interest in biotechnology and biomedicine. In industrial applications, it is widely used in dairy processing to hydrolyze lactose into glucose and galactose, addressing lactose intolerance and improving product texture. In molecular biology, it serves as a reporter enzyme in assays like the lacZ system (e.g., blue-white screening) to monitor gene expression or cloning efficiency. Structurally, 6GAL is often a tetrameric protein, with its activity dependent on conserved catalytic residues and cofactors like magnesium ions.
Recent advances focus on optimizing thermostability, substrate specificity, and pH tolerance through protein engineering, broadening its utility in extreme industrial conditions. In therapeutics, recombinant 6GAL is explored for enzyme replacement therapy in genetic disorders such as GM1 gangliosidosis, where deficient lysosomal β-galactosidase activity leads to neurodegeneration. Additionally, it is studied in glycobiology for modifying glycan structures on biologics to enhance drug efficacy.
Despite progress, challenges remain in minimizing immunogenicity for clinical use and improving cost-effective production. Ongoing research integrates CRISPR-Cas9. directed evolution, and AI-driven design to refine recombinant 6GAL variants, underscoring its versatility as a biocatalyst and therapeutic agent in evolving biotechnological landscapes.
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