| 纯度 | >90%SDS-PAGE. |
| 种属 | E.coli |
| 靶点 | mglB |
| Uniprot No | P0AEE5 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-332aa |
| 氨基酸序列 | MNKKVLTLSAVMASMLFGAAAHAADTRIGVTIYKYDDNFMSVVRKAIEQDAKAAPDVQLLMNDSQNDQSKQNDQIDVLLAKGVKALAINLVDPAAAGTVIEKARGQNVPVVFFNKEPSRKALDSYDKAYYVGTDSKESGIIQGDLIAKHWAANQGWDLNKDGQIQFVLLKGEPGHPDAEARTTYVIKELNDKGIKTEQLQLDTAMWDTAQAKDKMDAWLSGPNANKIEVVIANNDAMAMGAVEALKAHNKSSIPVFGVDALPEALALVKSGALAGTVLNDANNQAKATFDLAKNLADGKGAADGTNWKIDNKVVRVPYVGVDKDNLAEFSKK |
| 预测分子量 | 35,7 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3篇模拟的关于mglB重组蛋白的参考文献(注：文献信息为假设性示例，实际引用请以真实数据库检索结果为准)：
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1. **文献名称**: *Expression and Purification of Recombinant mglB Protein from Escherichia coli*
**作者**: Smith J, et al.
**摘要**: 本研究报道了通过原核表达系统(大肠杆菌BL21)高效表达mglB重组蛋白的优化方法，采用His标签亲和层析技术纯化蛋白，并通过SDS-PAGE和Western blot验证蛋白纯度及抗原性，为后续功能研究提供材料基础。
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2. **文献名称**: *Structural Insights into mglB-mediated Galactose Transport in Bacterial Systems*
**作者**: Zhang L, Wang H.
**摘要**: 通过X射线晶体学解析了重组mglB蛋白与半乳糖结合的复合物三维结构，揭示了其底物结合域的关键氨基酸残基及构象变化机制，为理解细菌糖转运的分子机制提供了结构生物学证据。
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3. **文献名称**: *Functional Characterization of a Mutant mglB Recombinant Protein in ATP-binding Capacity*
**作者**: Tanaka K, et al.
**摘要**: 构建了mglB基因的ATP结合位点突变体，并在体外实验中比较野生型与突变体重组蛋白的ATP水解活性，证明该位点对mglB介导的能量耦合转运过程具有决定性作用。
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如需真实文献，建议在PubMed或Web of Science中检索关键词："mglB recombinant protein", "mglB galactose-binding", 或结合具体研究方向补充筛选条件。
**Background of mglB Recombinant Protein**
The *mglB* gene encodes a periplasmic D-galactose-binding protein in *Escherichia coli*, a critical component of the methyl-galactose (mgl) ABC transporter system. This system facilitates the high-affinity uptake of galactose and related carbohydrates, supporting bacterial metabolism under nutrient-limited conditions. MglB functions as a solute receptor, binding extracellular substrates and delivering them to the transmembrane transporter complex for ATP-dependent import. Its role in nutrient scavenging highlights its importance in bacterial survival, particularly in competitive environments.
Recombinant MglB protein is engineered via heterologous expression, typically in *E. coli* expression systems, to produce purified protein for structural and functional studies. The protein’s high solubility and stability make it a model for investigating ligand-receptor interactions and conformational changes in ABC transporters. Structural studies using X-ray crystallography and cryo-EM have revealed its unique bilobate architecture, with ligand binding inducing a "closed" conformation that triggers downstream transport signaling.
Research on MglB has broader implications. Its substrate-binding specificity has been exploited in biosensor development, leveraging ligand-induced conformational shifts for signal transduction. Additionally, understanding MglB’s role in bacterial metabolism informs antimicrobial strategies targeting nutrient uptake pathways. Recent studies also explore engineered variants for biotechnological applications, such as custom ligand-binding proteins or scaffolds for synthetic biology.
Despite progress, challenges remain in fully elucidating dynamics of MglB-mediated transport and adapting it for industrial use. Ongoing work focuses on optimizing expression systems, improving ligand-binding affinities, and integrating MglB into hybrid bio-nanodevices. Overall, MglB recombinant protein serves as a versatile tool for both basic science and applied research in microbiology and biotechnology.
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