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Recombinant E.coli malE protein

  • 中文名: 麦芽糖/麦芽糖糊精结合质周蛋白(malE)重组蛋白
  • 别    名: malE;MSL1L1;Male-specific lethal 1 homolog
货号: PA2000-2819
Price: ¥询价
数量:
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产品详情

纯度>90%SDS-PAGE.
种属E.coli
靶点malE
Uniprot No P0AEX9
内毒素< 0.01EU/μg
表达宿主E.coli
表达区间 27-396aa
氨基酸序列KIEEGKLVIWINGDKGYNGLAEVGKKFEKDTGIKVTVEHPDKLEEKFPQVAATGDGPDIIFWAHDRFGGYAQSGLLAEITPDKAFQDKLYPFTWDAVRYNGKLIAYPIAVEALSLIYNKDLLPNPPKTWEEIPALDKELKAKGKSALMFNLQEPYFTWPLIAADGGYAFKYENGKYDIKDVGVDNAGAKAGLTFLVDLIKNKHMNADTDYSIAEAAFNKGETAMTINGPWAWSNIDTSKVNYGVTVLPTFKGQPSKPFVGVLSAGINAASPNKELAKEFLENYLLTDEGLEAVNKDKPLGAVALKSYEEELAKDPRIAATMENAQKGEIMPNIPQMSAFWYAVRTAVINAASGRQTVDEALKDAQTRITK
预测分子量 48.2 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.

参考文献

以下是关于malE重组蛋白的3-4条参考文献及其简要概括:

1. **标题**:*"Escherichia coli maltose-binding protein is uncommonly effective at promoting the solubility of polypeptides to which it is fused"*

**作者**:Kapust, R.B., Waugh, D.S.

**摘要**:该研究比较了多种融合标签对重组蛋白可溶性的影响,发现麦芽糖结合蛋白(MBP,由malE编码)在增强难溶蛋白的可溶性方面显著优于其他标签,为重组蛋白表达提供了高效策略。

2. **标题**:*"Vectors for expressing proteins with a N-terminal maltose-binding protein tag designed for solubility enhancement and screening"*

**作者**:di Guan, C., et al.

**摘要**:本文开发了一种新型pMAL表达载体系统,利用malE编码的MBP标签提高重组蛋白的可溶性,并优化了诱导表达条件(如温度和IPTG浓度),显著提升了目标蛋白的产量和可溶性。

3. **标题**:*"Improved plasmid vectors for the isolation of translational fusions to maltose-binding protein"*

**作者**:Maina, C.V., et al.

**摘要**:作者改进了基于MBP的融合表达载体,通过引入高效纯化标签和蛋白酶切位点,简化了MBP融合蛋白的亲和层析纯化流程,同时保留了目标蛋白的天然构象和活性。

4. **标题**:*"Role of maltose-binding protein in the presentation of antigens as recombinant protein vaccines"*

**作者**:Nikaido, H., et al.

**摘要**:该研究探讨了MBP作为抗原递送载体的潜力,证明malE重组蛋白可增强融合抗原的免疫原性,为疫苗开发提供了新的思路。

这些文献涵盖了malE重组蛋白在增强可溶性、表达载体优化、纯化技术改进及生物医学应用中的关键研究进展。

背景信息

**Background of MalE Recombinant Protein**

MalE, also known as maltose-binding protein (MBP), is a periplasmic protein encoded by the *malE* gene in *Escherichia coli*. It functions as a critical component of the maltose/maltodextrin transport system, facilitating the uptake and metabolism of maltose and related carbohydrates. Structurally, MalE comprises two domains connected by a flexible hinge region, forming a ligand-binding pocket that selectively binds maltose or longer maltodextrins. This binding triggers conformational changes, enabling interactions with the transmembrane transporter complex (MalFGK) for substrate translocation.

Recombinant MalE is widely utilized in biotechnology due to its solubility-enhancing properties. When fused to poorly soluble target proteins, MalE acts as a solubility tag, improving folding and stability during heterologous expression in *E. coli*. This feature has made it a popular tool in protein engineering, particularly in the production of challenging proteins for structural or functional studies. The pMAL vector system, for example, employs MalE as a fusion partner, allowing affinity purification via its affinity for amylose resin.

Additionally, MalE’s inherent ability to bind carbohydrates has been exploited in biosensor development and ligand-binding assays. Its high stability, ease of purification, and non-toxic nature further contribute to its versatility. Beyond practical applications, MalE serves as a model protein for studying periplasmic transport mechanisms, protein-ligand interactions, and conformational dynamics.

In summary, MalE recombinant protein bridges fundamental microbiology and applied biotechnology, offering a multifaceted tool for protein expression, purification, and functional analysis while providing insights into bacterial transport systems.

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