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Recombinant E. coli NusA protein

  • 中文名: 大肠杆菌转录终止/抗终止L因子(NusA)重组蛋白
  • 别    名: DMC1;DMC1H;LIM15;Meiotic recombination protein DMC1/LIM15 homolog
货号: PA1000-2226
Price: ¥询价
数量:
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产品详情

纯度>85%SDS-PAGE.
种属Escherichia coli
靶点NusA
Uniprot NoP0AFF6
内毒素< 0.01EU/μg
表达宿主E.coli
表达区间1-495aa
氨基酸序列MNKEILAVVE AVSNEKALPR EKIFEALESA LATATKKKYE QEIDVRVQID RKSGDFDTFR RWLVVDEVTQ PTKEITLEAA RYEDESLNLG DYVEDQIESV TFDRITTQTA KQVIVQKVRE AERAMVVDQF REHEGEIITG VVKKVNRDNI SLDLGNNAEA VILREDMLPR ENFRPGDRVR GVLYSVRPEA RGAQLFVTRS KPEMLIELFR IEVPEIGEEV IEIKAAARDP GSRAKIAVKT NDKRIDPVGA CVGMRGARVQ AVSTELGGER IDIVLWDDNP AQFVINAMAP ADVASIVVDE DKHTMDIAVE AGNLAQAIGR NGQNVRLASQ LSGWELNVMT VDDLQAKHQA EAHAAIDTFT KYLDIDEDFA TVLVEEGFST LEELAYVPMK ELLEIEGLDE PTVEALRERA KNALATIAQA QEESLGDNKP ADDLLNLEGV DRDLAFKLAA RGVCTLEDLA EQGIDDLADI EGLTDEKAGA LIMAARNICW FGDEA
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.

参考文献

以下是关于NusA重组蛋白的3篇示例参考文献(注:以下内容为虚拟生成,仅作格式参考):

1. **标题**: "Functional characterization of recombinant NusA protein in transcription elongation and termination"

**作者**: Roberts JW, et al.

**摘要**: 研究利用重组NusA蛋白分析其与大肠杆菌RNA聚合酶的相互作用,揭示其在转录暂停和终止中的调控机制,证明NusA通过结合RNA发夹结构促进转录终止。

2. **标题**: "Expression and purification of NusA tagged with hexahistidine for structural studies"

**作者**: Zhou Y, et al.

**摘要**: 描述重组NusA蛋白的克隆、表达及镍柱纯化方法,通过X射线晶体学解析其三维结构,揭示其与RNA聚合酶结合的分子基础。

3. **标题**: "NusA modulates the solubility and folding of recombinant proteins in E. coli"

**作者**: Gupta P, et al.

**摘要**: 探讨重组NusA作为分子伴侣辅助其他重组蛋白的可溶性表达,发现其通过减缓转录速率促进蛋白质正确折叠,提升异源蛋白产量。

4. **标题**: "Role of NusA in antitermination complex formation during lambda phage infection"

**作者**: Friedman DI, et al.

**摘要**: 研究重组NusA在λ噬菌体抗终止复合体中的作用,通过体外重组实验证实NusA与N蛋白协同调控宿主转录机制,维持噬菌体基因的持续表达。

背景信息

NusA (N utilization substance A) is a multifunctional transcriptional regulator originally identified in *Escherichia coli*. It plays a central role in modulating RNA polymerase (RNAP) activity during transcription elongation, termination, and anti-termination processes. As an elongation factor, NusA interacts directly with RNAP and nascent RNA to influence transcriptional pausing, fidelity, and termination efficiency. It is also a key component of the anti-termination machinery in phage λ and ribosomal RNA operons, where it collaborates with other factors (e.g., NusB, NusG) to suppress Rho-dependent termination.

Recombinant NusA proteins are engineered versions produced via heterologous expression systems, typically in *E. coli*, for biochemical and structural studies. The nusA gene is cloned into expression vectors under inducible promoters (e.g., T7 or lac), allowing high-yield purification of the protein. Recombinant NusA retains its native functions, including RNA-binding capability via its S1 domain and interaction with RNAP through its AR2 (acidic repeat) domain. These properties make it invaluable for *in vitro* transcription assays, studying transcription-translation coupling, and probing RNA-protein interactions.

In biotechnology, recombinant NusA is often utilized as a solubility enhancer tag for expressing poorly soluble proteins in *E. coli*. Its chaperone-like activity aids in preventing aggregation of fusion partners. Additionally, NusA’s role in stabilizing paused transcription complexes has made it a tool for cryo-EM studies of transcription machinery. Commercial availability of purified recombinant NusA supports diverse applications, from basic research on transcriptional regulation to optimizing protein expression systems. Its structural versatility and functional conservation across bacteria also render it a model for studying transcription mechanisms in pathogens.

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