| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | SY |
| Uniprot No | P21579 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 99-416aa |
| 氨基酸序列 | KNAINMKDVKDLGKTMKDQALKDDDAETGLTDGEEKEEPKEEEKLGKLQYSLDYDFQNNQLLVGIIQAAELPALDMGGTSDPYVKVFLLPDKKKKFETKVHRKTLNPVFNEQFTFKVPYSELGGKTLVMAVYDFDRFSKHDIIGEFKVPMNTVDFGHVTEEWRDLQSAEKEEQEKLGDICFSLRYVPTAGKLTVVILEAKNLKKMDVGGLSDPYVKIHLMQNGKRLKKKKTTIKKNTLNPYYNESFSFEVPFEQIQKVQVVVTVLDYDKIGKNDAIGKVFVGYNSTGAELRHWSDMLANPRRPIAQWHTLQVEEEVDA |
| 预测分子量 | 40.3 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SY重组蛋白的3篇示例参考文献(内容为虚构，仅用于示例)：
1. **文献名称**：Expression and Purification of SY Recombinant Protein in E. coli
**作者**：Zhang L., et al.
**摘要**：本研究通过优化大肠杆菌表达系统，成功实现了SY重组蛋白的高效可溶性表达，采用亲和层析技术纯化获得高纯度蛋白，为后续功能研究奠定基础。
2. **文献名称**：Functional Analysis of SY Recombinant Protein in Neurodegenerative Disease Models
**作者**：Wang Y., et al.
**摘要**：通过体外细胞实验和小鼠模型，发现SY重组蛋白能够显著抑制β-淀粉样蛋白聚集，缓解神经元损伤，提示其潜在阿尔茨海默病治疗价值。
3. **文献名称**：Structural Characterization of SY Recombinant Protein by Cryo-EM
**作者**：Chen H., et al.
**摘要**：利用冷冻电镜技术解析了SY重组蛋白的3.2Å分辨率三维结构，揭示其与配体结合的关键位点，为基于结构的药物设计提供依据。
(注：以上文献为模拟示例，实际引用需依据具体研究领域检索真实数据库如PubMed、CNKI等。)
SY recombinant proteins are engineered biological molecules produced through advanced genetic engineering techniques, enabling precise manipulation of protein structures for research, therapeutic, and industrial applications. Developed as part of the broader recombinant protein technology boom since the late 20th century, SY variants specifically address challenges in protein stability, solubility, and functional consistency that often limit conventional recombinant systems.
These proteins are typically expressed in optimized host systems (e.g., E. coli, yeast, or mammalian cells) using codon-optimized synthetic genes, ensuring high-yield production while maintaining post-translational modifications critical for biological activity. The "SY" designation often reflects proprietary expression platforms or modification technologies developed by biotech firms or academic institutions to enhance protein performance. Common applications include drug discovery (as targets or therapeutic agents), diagnostic assay components, and tools for structural biology studies.
Recent advancements in SY protein engineering incorporate machine learning-driven design for improved antigen-binding affinity in antibody production or enhanced enzymatic properties for industrial biocatalysis. Quality control protocols for SY proteins typically exceed industry standards, with rigorous characterization using mass spectrometry, circular dichroism, and functional assays. Their growing adoption in personalized medicine and biosimilar development underscores their importance in modern biopharmaceutical pipelines, particularly in oncology and autoimmune disease research where precise protein interactions dictate therapeutic outcomes.
Commercial SY protein platforms often emphasize scalability, with some systems achieving gram-per-liter yields under GMP conditions. Ongoing research focuses on reducing production costs while expanding modification capabilities, such as site-specific PEGylation or fluorescent tagging, to meet evolving demands in both academic and industrial settings.
×
