| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | SN |
| Uniprot No | Q9BZZ2 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-1709aa |
| 氨基酸序列 | MGFLPKLLLLASFFPAGQASWGVSSPQDVQGVKGSCLLIPCIFSFPADVEVPDGITAIWYYDYSGQRQVVSHSADPKLVEARFRGRTEFMGNPEHRVCNLLLKDLQPEDSGSYNFRFEISEVNRWSDVKGTLVTVTEEPRVPTIASPVELLEGTEVDFNCSTPYVCLQEQVRLQWQGQDPARSVTFNSQKFEPTGVGHLETLHMAMSWQDHGRILRCQLSVANHRAQSEIHLQVKYAPKGVKILLSPSGRNILPGELVTLTCQVNSSYPAVSSIKWLKDGVRLQTKTGVLHLPQAAWSDAGVYTCQAENGVGSLVSPPISLHIFMAEVQVSPAGPILENQTVTLVCNTPNEAPSDLRYSWYKNHVLLEDAHSHTLRLHLATRADTGFYFCEVQNVHGSERSGPVSVVVNHPPLTPVLTAFLETQAGLVGILHCSVVSEPLATLVLSHGGHILASTSGDSDHSPRFSGTSGPNSLRLEIRDLEETDSGEYKCSATNSLGNATSTLDFHANAARLLISPAAEVVEGQAVTLSCRSGLSPTPDARFSWYLNGALLHEGPGSSLLLPAASSTDAGSYHCRARDGHSASGPSSPAVLTVLYPPRQPTFTTRLDLDAAGAGAGRRGLLLCRVDSDPPARLQLLHKDRVVATSLPSGGGCSTCGGCSPRMKVTKAPNLLRVEIHNPLLEEEGLYLCEASNALGNASTSATFNGQATVLAIAPSHTLQEGTEANLTCNVSREAAGSPANFSWFRNGVLWAQGPLETVTLLPVARTDAALYACRILTEAGAQLSTPVLLSVLYPPDRPKLSALLDMGQGHMALFICTVDSRPLALLALFHGEHLLATSLGPQVPSHGRFQAKAEANSLKLEVRELGLGDSGSYRCEATNVLGSSNTSLFFQVRGAWVQVSPSPELQEGQAVVLSCQVHTGVPEGTSYRWYRDGQPLQESTSATLRFAAITLTQAGAYHCQAQAPGSATTSLAAPISLHVSYAPRHVTLTTLMDTGPGRLGLLLCRVDSDPPAQLRLLHGDRLVASTLQGVGGPEGSSPRLHVAVAPNTLRLEIHGAMLEDEGVYICEASNTLGQASASADFDAQAVNVQVWPGATVREGQLVNLTCLVWTTHPAQLTYTWYQDGQQRLDAHSIPLPNVTVRDATSYRCGVGPPGRAPRLSRPITLDVLYAPRNLRLTYLLESHGGQLALVLCTVDSRPPAQLALSHAGRLLASSTAASVPNTLRLELRGPQPRDEGFYSCSARSPLGQANTSLELRLEGVRVILAPEAAVPEGAPITVTCADPAAHAPTLYTWYHNGRWLQEGPAASLSFLVATRAHAGAYSCQAQDAQGTRSSRPAALQVLYAPQDAVLSSFRDSRARSMAVIQCTVDSEPPAELALSHDGKVLATSSGVHSLASGTGHVQVARNALRLQVQDVPAGDDTYVCTAQNLLGSISTIGRLQVEGARVVAEPGLDVPEGAALNLSCRLLGGPGPVGNSTFAWFWNDRRLHAEPVPTLAFTHVARAQAGMYHCLAELPTGAAASAPVMLRVLYPPKTPTMMVFVEPEGGLRGILDCRVDSEPLASLTLHLGSRLVASSQPQGAPAEPHIHVLASPNALRVDIEALRPSDQGEYICSASNVLGSASTSTYFGVRALHRLHQFQQLLWVLGLLVGLLLLLLGLGACYTWRRRRVCKQSMGENSVEMAFQKETTQLIDPDAATCETSTCAPPLG |
| 预测分子量 | 182,6 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SN重组蛋白的3篇参考文献示例，供参考：
1. **《高效表达SN重组蛋白的大肠杆菌系统构建及功能验证》**
作者：张伟等
摘要：研究通过优化密码子和表达条件，在大肠杆菌中高效表达SN重组蛋白，经纯化后验证其体外酶活性，证实其具备与天然蛋白相似的生物功能，为工业化生产提供基础。
2. **《SN重组蛋白的晶体结构解析及其底物结合机制》**
作者：Chen J, Smith TL
摘要：采用X射线晶体学解析SN重组蛋白的三维结构，结合分子对接实验揭示其底物结合关键位点，阐明其在信号转导中的分子机制。
3. **《SN重组蛋白在神经退行性疾病模型中的治疗潜力评估》**
作者：Li H et al.
摘要：通过细胞和小鼠模型证实，SN重组蛋白可显著减少β-淀粉样蛋白沉积，改善认知功能，提示其在阿尔茨海默病治疗中的应用前景。
注：以上文献为示例性内容，实际研究中需参考具体领域的最新论文。如需真实文献，建议通过PubMed或Web of Science以“SN recombinant protein”等关键词检索。
**Background of SN Recombinant Proteins**
Recombinant proteins, engineered through genetic modification, have revolutionized biomedical research and therapeutic development. SN recombinant proteins, a specific subclass, are typically designed to mimic or modify naturally occurring proteins involved in critical cellular processes, such as signal transduction, immune response, or enzymatic activity. The "SN" designation often refers to their association with specific structural or functional motifs, such as SNARE (Soluble NSF Attachment Protein Receptor) domains, which mediate membrane fusion in intracellular trafficking, though the exact context may vary based on research focus.
The development of SN recombinant proteins leverages advancements in molecular cloning, expression systems (e.g., *E. coli*, yeast, mammalian cells*), and purification techniques. These proteins are synthesized by inserting target gene sequences into expression vectors, followed by transfection into host cells for large-scale production. Post-translational modifications, such as glycosylation or phosphorylation, are often critical for functionality, necessitating the use of eukaryotic systems for certain SN proteins.
SN recombinant proteins have broad applications. In basic research, they serve as tools to study protein-protein interactions, enzymatic mechanisms, or cellular pathways. Therapeutically, they are explored for treating diseases like cancer, autoimmune disorders, or infectious diseases, where modulating specific pathways can yield clinical benefits. For instance, SN proteins mimicking immune checkpoint regulators are investigated in immunotherapy.
Challenges remain in optimizing yield, stability, and functional fidelity, particularly for complex multidomain proteins. Innovations in protein engineering, such as directed evolution or computational design, aim to address these limitations. Additionally, the rise of mRNA and cell-based platforms may complement traditional recombinant approaches.
Overall, SN recombinant proteins exemplify the intersection of biotechnology and molecular biology, offering tailored solutions for understanding and intervening in biological systems. Their continued refinement underscores their importance in both academic and industrial settings.
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