| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | N75Q |
| Uniprot No | P31785 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 56-254aa |
| 氨基酸序列 | PLPEVQCFVFNVEYMNCTWQSSSEPQPTNLTLHYWYKNSDNDKVQKCSHYLFSEEITSGCQLQKKEIHLYQTFVVQLQDPREPRRQATQMLKLQNLVIPWAPENLTLHKLSESQLELNWNNRFLNHCLEHLVQYRTDWDHSWTEQSVDYRHKFSLPSVDGQKRYTFRVRSRFNPLCGSAQHWSEWSHPIHWGSNTSKEN |
| 预测分子量 | 25.0 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N75Q重组蛋白的3篇模拟参考文献示例，涵盖不同研究方向：
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1. **文献名称**：*Enhanced Secretion and Stability of N75Q Mutant Recombinant Protein in CHO Cells*
**作者**：Zhang, L., et al.
**摘要**：本研究探讨了在CHO细胞中表达N75Q突变体重组蛋白的效果。结果显示，N75Q突变导致糖基化位点缺失，显著提高了蛋白分泌效率，但热稳定性略有下降，为工业化生产提供了优化策略。
2. **文献名称**：*Structural Insights into N75Q-Modified Protein X: Implications for Ligand Binding*
**作者**：Li, Y., & Wang, H.
**摘要**：通过冷冻电镜和分子动力学模拟，分析N75Q突变对蛋白X结构的影响。突变破坏了原有氢键网络，导致底物结合亲和力降低，但增强了蛋白在酸性环境中的构象稳定性。
3. **文献名称**：*N75Q Recombinant Antigen Elicits Potent Neutralizing Antibodies in Murine Models*
**作者**：Chen, J., et al.
**摘要**：评估N75Q突变体作为疫苗抗原的潜力。糖基化缺失使关键表位暴露，在小鼠模型中诱导的中和抗体滴度较野生型提高3倍，提示其在疫苗开发中的应用前景。
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注：上述文献为模拟内容，实际研究中请通过学术数据库(如PubMed、Web of Science)检索真实文献。
**Background of N75Q Recombinant Protein**
The N75Q recombinant protein is a genetically engineered variant designed to study the role of specific post-translational modifications, particularly *N-linked glycosylation*, in protein structure and function. The "N75Q" designation refers to a point mutation where the asparagine (N) residue at position 75 is replaced with glutamine (Q). This substitution disrupts a conserved *N-X-S/T* glycosylation motif, effectively eliminating glycosylation at this site. Such mutations are critical for investigating how glycosylation impacts protein stability, folding, ligand binding, or cellular localization.
Recombinant proteins like N75Q are typically produced using expression systems such as mammalian cells (e.g., CHO or HEK293), which support proper folding and post-translational modifications. The protein is often purified via affinity chromatography tags (e.g., His-tag or Fc-fusion) followed by rigorous quality assessments, including SDS-PAGE, Western blotting, and mass spectrometry, to confirm the absence of glycosylation and structural integrity.
N75Q variants are widely used in biomedical research to dissect glycosylation-dependent mechanisms in diseases. For example, in therapeutic antibody development, removing glycosylation sites can alter effector functions (e.g., antibody-dependent cellular cytotoxicity) or reduce immunogenicity. Similarly, in enzyme studies, glycosylation-deficient mutants like N75Q help clarify how sugar moieties influence activity, secretion, or half-life *in vivo*.
This protein also serves as a tool in structural biology, enabling comparisons between glycosylated and non-glycosylated forms via techniques like X-ray crystallography or cryo-EM. Such studies provide insights into how glycosylation stabilizes conformations or mediates interactions. Overall, the N75Q recombinant protein exemplifies the intersection of genetic engineering and functional biochemistry, driving advances in both basic science and biopharmaceutical applications.
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