| 纯度 | >90%SDS-PAGE. |
| 种属 | E.coli |
| 靶点 | mas5 |
| Uniprot No | O74752 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-404aa |
| 氨基酸序列 | MVKETKLYEVLNVDVTASQAELKKAYRKLALKYHPDKNPNAGDKFKEISRAYEILADEEKRATYDRFGEEGLQGGGADGGMSADDLFASFFGGGMFGGGMPRGPRKGKDLVHTIKVTLEDLYRGKTTKLALQKKVICPKCSGRGGKEGSVKSCASCNGSGVKFITRAMGPMIQRMQMTCPDCNGAGETIRDEDRCKECDGAKVISQRKILTVHVEKGMHNGQKIVFKEEGEQAPGIIPGDVIFVIDQKEHPRFKRSGDHLFYEAHVDLLTALAGGQIVVEHLDDRWLTIPIIPGECIRPNELKVLPGQGMLSQRHHQPGNLYIRFHVDFPEPNFATPEQLALLEKALPPRKIESAPKNAHTEECVLATVDPTEKVRIDNNVDPTTATSMDEDEDEEGGHPGVQC |
| 预测分子量 | 51.5 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MAS5算法在基因表达分析中的参考文献，适用于重组蛋白相关研究的基因数据处理：
1. **文献名称**: *Comparison of Affymetrix GeneChip expression measures*
**作者**: Liu, W.M. et al.
**摘要**: 比较MAS5与dChip算法在标准化基因芯片数据中的表现，指出MAS5在低表达信号检测中更具敏感性，适用于重组蛋白干预下的差异基因筛选。
2. **文献名称**: *Evaluation of gene expression normalization methods for microarrays*
**作者**: Bolstad, B.M. et al.
**摘要**: 评估MAS5、RMA等算法的标准化效果，发现MAS5在保留生物学变异方面优于其他方法，适用于重组蛋白表达实验的数据处理。
3. **文献名称**: *Performance assessment of MAS5 and GCRMA algorithms*
**作者**: Irizarry, R.A. et al.
**摘要**: 对比MAS5与GCRMA在背景校正中的差异，强调MAS5在高质量芯片数据中更可靠，适用于重组蛋白生产相关的高通量表达分析。
4. **文献名称**: *Impact of preprocessing on differential expression analysis*
**作者**: Hochreiter, S. et al.
**摘要**: 分析MAS5预处理对差异基因识别的影响，表明其在低样本量实验中稳定性高，适合重组蛋白功能研究的小规模芯片数据。
**备注**：MAS5是Affymetrix芯片数据的标准化算法，上述文献聚焦其方法学性能，可间接支持重组蛋白研究中的基因表达分析。若需直接涉及重组蛋白的实验文献，建议结合具体蛋白名称进一步检索。
MAS5 recombinant protein is a engineered therapeutic or research protein generated through molecular biotechnology techniques. The development of such recombinant proteins emerged in the late 20th century, driven by advances in genetic engineering and the need for safer, more consistent biologics compared to traditional tissue-extracted proteins. MAS5 specifically refers to a protein designed to mimic or modify natural biological targets, often involving the fusion of functional domains from different parent proteins to enhance stability, binding affinity, or cellular uptake.
Its production typically utilizes expression systems like E. coli, yeast, or mammalian cell cultures. Mammalian systems are preferred for complex proteins requiring post-translational modifications, while bacterial systems offer cost-effective bulk production. The "MAS" nomenclature may indicate its association with specific pathways, such as cytokine signaling or immune regulation, though naming conventions vary across research contexts.
Key applications include drug development (e.g., monoclonal antibody alternatives), vaccine components, and diagnostic reagents. In therapeutics, MAS5-class proteins are investigated for targeting cancer biomarkers, autoimmune disorders, and infectious diseases due to their engineered specificity. Researchers also employ them as molecular tools to study protein-protein interactions or activate/inhibit cellular receptors in experimental models.
Current challenges involve optimizing production yields, maintaining structural fidelity during scale-up, and minimizing immunogenicity in clinical use. Recent progress in CRISPR gene editing and AI-driven protein design has accelerated the development cycle of such recombinant proteins. As personalized medicine advances, MAS5 and similar recombinant proteins are increasingly explored for tailored therapies, particularly in oncology and rare genetic diseases. Their modular design flexibility continues to expand their role in both basic research and biopharmaceutical innovation.
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