| 纯度 | >85%SDS-PAGE. |
| 种属 | Human |
| 靶点 | MBP |
| Uniprot No | P02686 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-304aa |
| 氨基酸序列 | MGNHAGKRELNAEKASTNSETNRGESEKKRNLGELSRTTSEDNEVFGEADANQNNGTSSQDTAVTDSKRTADPKNAWQDAHPADPGSRPHLIRLFSRDAPGREDNTFKDRPSESDELQTIQEDSAATSESLDVMASQKRPSQRHGSKYLATASTMDHARHGFLPRHRDTGILDSIGRFFGGDRGAPKRGSGKDSHHPARTAHYGSLPQKSHGRTQDENPVVHFFKNIVTPRTPPPSQGKGRGLSLSRFSWGAEGQRPGFGYGGRASDYKSAHKGFKGVDAQGTLSKIFKLGGRDSRSGSPMARR |
| 预测分子量 | 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. |
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Maltose-binding protein (MBP) is a 42 kDa periplasmic protein derived from the malE gene of Escherichia coli. It plays a central role in the bacterial maltose/maltodextrin transport system, where it binds maltose or maltodextrins and delivers them to membrane transporters. Since the 1980s, MBP has been widely adopted in biotechnology as a fusion partner to enhance the solubility and stability of recombinant proteins during heterologous expression. This application stems from its intrinsic ability to promote proper folding of fused polypeptides, particularly for eukaryotic proteins prone to aggregation in prokaryotic systems like E. coli.
The MBP fusion system leverages the natural affinity of MBP for amylose resins, enabling straightforward purification through affinity chromatography. A protease cleavage site (e.g., Factor Xa or TEV) is typically incorporated between MBP and the target protein, allowing tag removal post-purification. Beyond its role as a solubility enhancer, MBP's large size and structural stability have made it valuable in crystallography studies, where it can facilitate protein crystallization. Recent studies also suggest MBP may act as a molecular chaperone by temporarily stabilizing nascent polypeptides during expression.
Commercial vectors like the pMAL series have optimized MBP fusion technology, offering cytoplasmic or periplasmic expression options. While particularly effective in E. coli, MBP fusion systems have been adapted for use in mammalian and insect cell cultures. The tag's non-immunogenic nature and lack of interference with biological activity in many cases make it preferable for therapeutic protein production. Ongoing research explores engineered MBP variants with improved binding capacity or altered cleavage sites, expanding its utility in recombinant protein workflows across basic research and industrial applications.
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