| 纯度 | >95%SDS-PAGE. |
| 种属 | Human |
| 靶点 | PTMS |
| Uniprot No | P20962 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-102aa |
| 氨基酸序列 | MGSSHHHHHH SSGLVPRGSH MGSMSEKSVE AAAELSAKDL KEKKEKVEEK ASRKERKKEV VEEEENGAEE EEEETAEDGE EEDEGEEEDE EEEEEDDEGP ALKRAAEEED EADPKRQKTE NGASA |
| 预测分子量 | 14 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. |
1. **"Efficient Production of Glycosylated Recombinant Proteins in Mammalian Cells"**
*作者：Smith A, et al.*
摘要：研究哺乳动物表达系统中重组蛋白的糖基化修饰优化策略，提高蛋白稳定性和生物活性。
2. **"Engineering Phosphorylation Sites in Recombinant Proteins Using Yeast Expression Systems"**
*作者：Zhang L, et al.*
摘要：开发基于酵母的改造技术，在重组蛋白中精准引入磷酸化修饰，用于功能研究与药物开发。
3. **"Mass Spectrometry Analysis of Post-Translational Modifications in Recombinant Therapeutic Proteins"**
*作者：Johnson R, et al.*
摘要：利用质谱技术系统鉴定重组治疗性蛋白(如单克隆抗体)的翻译后修饰(如氧化、脱酰胺)，评估其对药物质量的影响。
4. **"Site-Specific Ubiquitination of Recombinant Proteins for Enhanced Functional Studies"**
*作者：Chen H, et al.*
摘要：通过基因编辑技术在大肠杆菌中实现重组蛋白的位点特异性泛素化修饰，解析其在细胞信号通路中的作用机制。
**Background of PTMS Recombinant Proteins**
Recombinant proteins, engineered through genetic modification, are pivotal in biotechnology, medicine, and research. Post-translational modification systems (PTMS) play a critical role in ensuring these proteins acquire functional maturity. PTMS refers to biochemical alterations—such as glycosylation, phosphorylation, or ubiquitination—that occur after protein synthesis, enabling proper folding, stability, and biological activity. Many therapeutic proteins, including antibodies, hormones, and enzymes, require PTMS to mimic natural human proteins and function effectively.
Historically, recombinant proteins were produced in prokaryotic systems like *E. coli*, which lack PTMS capabilities. This limitation drove the adoption of eukaryotic systems, such as yeast, insect, and mammalian cells (e.g., CHO, HEK293), which naturally perform complex PTMS. Mammalian systems, in particular, became gold standards for producing glycosylated biologics, such as monoclonal antibodies and vaccines, due to their human-like modification patterns.
Advancements in genetic engineering, including CRISPR and site-specific mutagenesis, have enabled precise control over PTMS in recombinant proteins. Innovations like glycoengineering now allow customized glycosylation profiles to enhance drug efficacy, reduce immunogenicity, or tailor pharmacokinetics. Additionally, cell-free protein synthesis and plant-based systems are emerging as scalable, cost-effective alternatives for PTMS-heavy proteins.
PTMS recombinant proteins underpin modern biologics, including cancer therapies, enzyme replacement therapies, and COVID-19 vaccines. Challenges remain in ensuring batch-to-batch consistency and scaling production while maintaining PTMS fidelity. Ongoing research focuses on optimizing expression systems, synthetic biology tools, and AI-driven design to address these hurdles, aiming to expand access to lifesaving biotherapeutics globally.
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