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Recombinant E.coli phrB protein

  • 中文名: 脱氧核糖二嘧啶光裂解酶(phrB)重组蛋白
  • 别    名: phrB;(6-4) photolyase
货号: PA2000-2829
Price: ¥询价
数量:
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产品详情

纯度>90%SDS-PAGE.
种属E.coli
靶点phrB
Uniprot NoP00914
内毒素< 0.01EU/μg
表达宿主E.coli
表达区间1-472aa
氨基酸序列MGSSHHHHHHSSGLVPRGSHMGSMTTHLVWFRQDLRLHDNLALAAACRNS SARVLALYIATPRQWATHNMSPRQAELINAQLNGLQIALAEKGIPLLFRE VDDFVASVEIVKQVCAENSVTHLFYNYQYEVNERARDVEVERALRNVVCE GFDDSVILPPGAVMTGNHEMYKVFTPFKNAWLKRLREGMPECVAAPKVRS SGSIEPSPSITLNYPRQSFDTAHFPVEEKAAIAQLRQFCQNGAGEYEQQR DFPAVEGTSRLSASLATGGLSPRQCLHRLLAEQPQALDGGAGSVWLNELI WREFYRHLITYHPSLCKHRPFIAWTDRVQWQSNPAHLQAWQEGKTGYPIV DAAMRQLNSTGWMHNRLRMITASFLVKDLLIDWREGERYFMSQLIDGDLA ANNGGWQWAASTGTDAAPYFRIFNPTTQGEKFDHEGEFIRQWLPELRDVP GKVVHEPWKWAQKAGVTLDYPQPIVEHKEARVQTLAAYEAARKGK
预测分子量56 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 **phrB 重组蛋白** 的3篇参考文献(基于领域知识模拟,具体文献需结合实际数据库检索验证):

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1. **文献名称**: *Molecular cloning and functional analysis of the phrB gene encoding a photolyase from Synechocystis sp. PCC 6803*

**作者**: Kaneko T., Tabata S.

**摘要**: 本研究克隆了蓝藻 *Synechocystis* 中的 **phrB** 基因,并通过大肠杆菌表达系统成功获得重组蛋白。功能实验表明,phrB 编码的光裂解酶能特异性修复紫外线引起的环丁烷嘧啶二聚体(CPD),证实其在DNA损伤修复中的作用。

2. **文献名称**: *Heterologous expression and purification of phrB photolyase: Role in UV resistance*

**作者**: Takeuchi I., Yamamoto K.

**摘要**: 作者构建了带有His标签的phrB重组蛋白表达载体,通过亲和层析纯化获得高纯度蛋白。体外活性实验显示,重组phrB显著增强UV损伤的DNA修复效率,为光复活机制研究提供了工具。

3. **文献名称**: *Structural and biochemical characterization of phrB in cyanobacterial photoprotection*

**作者**: de Marsac N.T., Houmard J.

**摘要**: 通过X射线晶体学解析了重组phrB蛋白的三维结构,揭示了其结合FAD辅因子的活性位点。生化实验证明,phrB的活性依赖于蓝光激发,为光依赖型修复酶的机理提供了依据。

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**注**:以上为模拟示例,实际文献需通过PubMed/Google Scholar等平台以“phrB recombinant protein”“photolyase phrB”等关键词检索。建议结合具体研究需求筛选近年文献。

背景信息

**Background of PhrB Recombinant Protein**

PhrB is a protein encoded by the *phrB* gene, initially identified in *Bacillus subtilis* and related bacterial species. It plays a role in the DNA damage response and repair mechanisms, particularly within the *phr* (photoreactivation) operon. This operon is associated with light-dependent DNA repair processes, where photolyases reverse UV-induced thymine dimers. PhrB, however, is distinct from photolyases and is proposed to function as a regulatory or accessory protein in stress adaptation or repair pathways. Its exact molecular mechanism remains under investigation, but studies suggest potential involvement in nucleotide excision repair or modulation of repair enzyme activity.

Recombinant PhrB protein is produced via genetic engineering, typically by cloning the *phrB* gene into expression vectors (e.g., plasmid systems) and expressing it in heterologous hosts like *Escherichia coli*. This approach enables large-scale production of purified PhrB for functional and structural studies. Recombinant technology allows modifications such as affinity tags (e.g., His-tag) to facilitate purification and detection.

Research on PhrB recombinant protein focuses on elucidating its role in bacterial stress responses, interactions with DNA repair machinery, and potential applications in biotechnology. For instance, understanding PhrB’s function could aid in developing UV-resistant bacterial strains or novel biocatalysts. Additionally, structural analysis of recombinant PhrB (via X-ray crystallography or cryo-EM) provides insights into its 3D conformation and active sites, which may inform drug design targeting bacterial repair systems.

Overall, PhrB recombinant protein serves as a critical tool for dissecting microbial DNA repair mechanisms and exploring biotechnological innovations tied to stress adaptation.

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