纯度 | >90%SDS-PAGE. |
种属 | Human |
靶点 | SMT3 |
Uniprot No | Q12306 |
内毒素 | < 0.01EU/μg |
表达宿主 | E.coli |
表达区间 | 2-98aa |
氨基酸序列 | SDSEVNQEAKPEVKPEVKPETHINLKVSDGSSEIFFKIKKTTPLRRLMEA FAKRQGKEMDSLRFLYDGIRIQADQTPEDLDMEDNDIIEAHREQIGG |
预测分子量 | 27 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SMT3重组蛋白的参考文献示例(内容为虚构示例,仅用于演示格式):
1. **《SUMO融合系统在大肠杆菌中高效表达可溶性重组蛋白的应用》**
作者:Zhang L. et al.
摘要:研究利用SMT3(酵母SUMO)作为融合标签,显著提高了目标蛋白在大肠杆菌中的可溶性和稳定性,并通过SUMO蛋白酶实现了标签的高效切除。
2. **《SMT3标签对重组蛋白纯化及功能的影响》**
作者:Wang Y. et al.
摘要:通过比较SMT3与其他亲和标签(如His-tag)发现,SMT3融合不仅能简化镍柱纯化流程,还可减少对靶蛋白活性的干扰,适用于结构生物学研究。
3. **《基于SMT3的重组蛋白表达系统优化及其在酶催化中的应用》**
作者:Chen R. et al.
摘要:开发了一种温度诱导型SMT3融合表达系统,成功应用于工业酶(如脂肪酶)的高效生产,证明其能维持酶活性并降低包涵体形成风险。
4. **《SMT3介导的蛋白质翻译后修饰机制及其在药物开发中的潜力》**
作者:Kimura T. et al.
摘要:探讨了SMT3在哺乳动物细胞中调控重组蛋白修饰的分子机制,并验证其在提高抗体类药物稳定性和半衰期方面的应用价值。
(注:以上文献为模拟内容,实际引用请查询PubMed、Web of Science等数据库获取真实文献。)
**Background of SMT3 Recombinant Protein**
SMT3. a homolog of the **Small Ubiquitin-like Modifier (SUMO)** protein family, is a highly conserved post-translational modification protein originally identified in *Saccharomyces cerevisiae* (yeast). SUMO proteins, including SMT3. play critical roles in regulating cellular processes such as protein localization, stability, and interaction, akin to ubiquitination but without targeting substrates for degradation. SMT3 is covalently attached to lysine residues on target proteins via an enzymatic cascade involving E1 (activating), E2 (conjugating), and E3 (ligating) enzymes, a process termed **SUMOylation**.
In recombinant protein technology, SMT3 is widely utilized as a **fusion tag** to enhance the solubility, stability, and yield of heterologous proteins expressed in bacterial or eukaryotic systems. Its small size (~12 kDa) and robust folding properties minimize interference with the structure or function of the target protein. Additionally, SMT3 fusion improves protein solubility, particularly for targets prone to aggregation, such as membrane proteins or intrinsically disordered regions.
A key advantage of SMT3 lies in its compatibility with **proteolytic cleavage** using SUMO-specific proteases (e.g., Ulp1 in yeast), which recognize the tertiary structure of SMT3 rather than a linear sequence. This enables precise removal of the tag after purification, leaving no residual amino acids on the target protein—crucial for structural and functional studies.
SMT3-tagged systems are integral to structural biology, drug discovery, and industrial enzyme production, offering a reliable method to express challenging proteins. Its applications extend to studying SUMOylation dynamics in disease models, such as cancer and neurodegeneration, where aberrant SUMO signaling is implicated. Overall, SMT3 recombinant technology bridges the gap between protein expression challenges and downstream research or therapeutic needs.
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