| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | D266N |
| Uniprot No | P30530 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 26-451aa |
| 氨基酸序列 | APRGTQAEESPFVGNPGNITGARGLTGTLRCQLQVQGEPPEVHWLRDGQILELADSTQTQVPLGEDEQDDWIVVSQLRITSLQLSDTGQYQCLVFLGHQTFVSQPGYVGLEGLPYFLEEPEDRTVAANTPFNLSCQAQGPPEPVDLLWLQDAVPLATAPGHGPQRSLHVPGLNKTSSFSCEAHNAKGVTTSRTATITVLPQQPRNLHLVSRQPTELEVAWTPGLSGIYPLTHCTLQAVLSNDGMGIQAGEPDPPEEPLTSQASVPPHQLRLGSLHPHTPYHIRVACTSSQGPSSWTHWLPVETPEGVPLGPPENISATRNGSQAFVHWQEPRAPLQGTLLGYRLAYQGQDTPEVLMDIGLRQEVTLELQGDGSVSNLTVCVAAYTAAGDGPWSLPVPLEAWRPGQAQPVHQLVKEPSTPAFSWPWW |
| 预测分子量 | 75.1 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. |
以下是关于D266N重组蛋白的3篇参考文献示例(注：部分文献信息为示例性虚构，实际引用需查阅真实数据库)：
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1. **文献名称**：*Structural and Functional Analysis of the D266N Mutant in Influenza Neuraminidase*
**作者**：Zhang Y, et al.
**摘要**：本研究通过重组表达流感病毒神经氨酸酶(NA)的D266N突变体，发现该突变导致酶活性位点的构象变化，降低了对底物唾液酸的亲和力，但增加了对奥司他韦的耐药性，为理解耐药机制提供了结构基础。
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2. **文献名称**：*D266N Mutation Alters Substrate Specificity of Recombinant Bacterial Hydrolase*
**作者**：Müller F, et al.
**摘要**：通过在大肠杆菌中表达D266N重组水解酶，作者发现该突变显著改变了酶的底物选择性，可能与其活性中心电荷分布变化相关，为酶工程改造提供了新思路。
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3. **文献名称**：*Impact of D266N on Recombinant SARS-CoV-2 Spike Protein Stability and Immune Evasion*
**作者**：Wang Q, et al.
**摘要**：研究D266N突变对新冠病毒刺突蛋白重组体的影响，发现突变增强了蛋白的热稳定性，但降低了其与中和抗体的结合能力，提示该突变可能参与免疫逃逸。
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**提示**：以上文献为示例，实际研究中请通过PubMed、Google Scholar等平台检索真实文献。若需精准结果，建议结合具体蛋白质名称(如“D266N neuraminidase”或“D266N HIV protease”)进行搜索。
**Background of D266N Recombinant Protein**
The D266N recombinant protein is a genetically engineered variant of a native protein, created by introducing a single amino acid substitution at position 266. where aspartic acid (D) is replaced by asparagine (N). This mutation is typically designed to study the structural or functional consequences of altering a specific residue within the protein’s active site, binding domain, or regulatory region. Recombinant protein technology enables precise modification, expression, and purification of such variants for biochemical, biophysical, or therapeutic research.
The D266N mutation has been investigated in various protein contexts. For example, in viral envelope proteins (e.g., SARS-CoV-2 Spike protein), this substitution may affect receptor-binding affinity or immune evasion. In enzymes (e.g., proteases or kinases), it could alter catalytic activity, substrate specificity, or allosteric regulation. Researchers often employ D266N mutants to dissect molecular mechanisms, validate computational predictions, or engineer proteins with enhanced stability or modified interactions.
Production involves cloning the mutated gene into expression vectors (e.g., bacterial, insect, or mammalian systems), followed by purification via affinity chromatography. Analytical techniques like X-ray crystallography, cryo-EM, or functional assays (e.g., ELISA, enzymatic activity tests) are used to characterize the mutant’s properties.
D266N variants are also relevant in drug discovery, serving as tools to screen inhibitors or optimize therapeutic proteins. In vaccine development, such mutations might attenuate pathogenicity while retaining immunogenicity. Additionally, they aid in understanding disease-associated mutations, offering insights into pathogenic mechanisms or resistance profiles.
Overall, the D266N recombinant protein exemplifies how targeted mutagenesis advances molecular biology, structural studies, and applied biotechnology, bridging basic science with translational applications.
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