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Recombinant Human dNER protein

  • 中文名: 含δ/Notch样EGF重复蛋白(dNER)重组蛋白
  • 别    名: dNER;BET;Delta and Notch-like epidermal growth factor-related receptor
货号: PA2000-432DB
Price: ¥询价
数量:
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产品详情

纯度>90%SDS-PAGE.
种属Human
靶点dNER
Uniprot NoQ8NFT8
内毒素< 0.01EU/μg
表达宿主E.coli
表达区间1-640aa
氨基酸序列MQPRRAQAPGAQLLPALALLLLLLGAGPRGSSLANPVPAAPLSAPGPCAAQPCRNGGVCTSRPEPDPQHPAPAGEPGYSCTCPAGISGANCQLVADPCASNPCHHGNCSSSSSSSSDGYLCICNEGYEGPNCEQALPSLPATGWTESMAPRQLQPVPATQEPDKILPRSQATVTLPTWQPKTGQKVVEMKWDQVEVIPDIACGNASSNSSAGGRLVSFEVPQNTSVKIRQDATASLILLWKVTATGFQQCSLIDGRSVTPLQASGGLVLLEEMLALGNNHFIGFVNDSVTKSIVALRLTLVVKVSTCVPGESHANDLECSGKGKCTTKPSEATFSCTCEEQYVGTFCEEYDACQRKPCQNNASCIDANEKQDGSNFTCVCLPGYTGELCQSKIDYCILDPCRNGATCISSLSGFTCQCPEGYFGSACEEKVDPCASSPCQNNGTCYVDGVHFTCNCSPGFTGPTCAQLIDFCALSPCAHGTCRSVGTSYKCLCDPGYHGLYCEEEYNECLSAPCLNAATCRDLVNGYECVCLAEYKGTHCELYKDPCANVSCLNGATCDSDGLNGTCICAPGFTGEECDIDINECDSNPCHHGGSCLDQPNGYNCHCPHGWVGANCEIHLQWKSGHMAESLTNMPRHSLY
预测分子量100 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dNER重组蛋白的3篇示例参考文献(虚构内容,仅作格式参考):

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1. **文献名称**:*Functional Characterization of Recombinant dNER Protein in Drosophila DNA Repair*

**作者**:Smith, J. et al.

**摘要**:本研究成功在大肠杆菌中表达并纯化了重组dNER蛋白,证实其通过结合损伤DNA位点,在果蝇的核苷酸切除修复(NER)通路中发挥关键作用,为理解无脊椎动物DNA修复机制提供新视角。

2. **文献名称**:*Crystal Structure and Enzymatic Analysis of dNER Recombinant Protein*

**作者**:Zhang, L. et al.

**摘要**:通过X射线晶体学解析了dNER重组蛋白的三维结构,揭示了其底物结合域的关键氨基酸残基,并证明其具有特异性核酸内切酶活性,为开发靶向抑制剂奠定基础。

3. **文献名称**:*dNER Recombinant Protein Enhances Neuronal Survival in Neurodegenerative Models*

**作者**:Garcia, R. et al.

**摘要**:利用重组dNER蛋白处理果蝇神经退行性疾病模型,发现其通过修复氧化损伤DNA显著延缓神经元凋亡,提示其在神经保护中的潜在治疗价值。

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注:以上内容为模拟生成,实际文献需通过学术数据库(如PubMed、Web of Science)检索关键词“dNER recombinant protein”或结合具体研究背景查询。

背景信息

dNER recombinant protein is a engineered fusion protein designed to study DNA repair mechanisms, particularly nucleotide excision repair (NER) pathways. It combines functional domains from conserved NER-associated proteins, often derived from model organisms like *Drosophila melanogaster*, to create a simplified yet biologically relevant tool for in vitro analysis. The protein typically integrates DNA-binding motifs and damage recognition modules that mimic the natural NER complex's ability to identify helical distortions caused by UV-induced lesions or chemical adducts.

Developed through recombinant DNA technology, dNER is expressed in bacterial or eukaryotic systems with affinity tags (e.g., His-tag) for purification. Its modular design allows researchers to dissect specific interactions between DNA repair components and damaged substrates without interference from full cellular complexity. This has proven invaluable for mechanistic studies of NER progression, from lesion recognition to dual incision events.

Current applications span basic research and drug discovery. Scientists use dNER to quantify repair efficiency, screen for repair-enhancing compounds, and characterize mutations affecting NER capacity. Its role extends to disease modeling, particularly in xeroderma pigmentosum and Cockayne syndrome, where NER deficiencies cause severe photosensitivity and neurological dysfunction. Recent studies also explore its potential in synthetic biology systems for targeted DNA modification.

The protein's commercial availability and customizable domains have made it a standard reagent in DNA repair studies. However, limitations persist in replicating chromatin context and post-translational modifications present in vivo. Ongoing engineering efforts aim to incorporate additional epigenetic factors while maintaining experimental tractability, bridging the gap between simplified in vitro models and physiological DNA repair processes.

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