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| 纯度 | >90%SDS-PAGE. |
| 种属 | E.coli |
| 靶点 | gam |
| Uniprot No | P03702 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-138aa |
| 氨基酸序列 | MDINTETEIKQKHSLTPFPVFLISPAFRGRYFHSYFRSSAMNAYYIQDRLEAQSWARHYQQLAREEKEAELADDMEKGLPQHLFESLCIDHLQRHGASKKSITRAFDDDVEFQERMAEHIRYMVETIAHHQVDIDSEV |
| 预测分子量 | 23.8 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GAM重组蛋白的3篇参考文献示例(注：内容为模拟概括，非真实文献)：
1. **文献名称**：*"Recombinant M protein-based vaccine against Group A Streptococcus"*
**作者**：Dale, J.B. et al.
**摘要**：研究利用重组GAM蛋白(A族链球菌M蛋白)开发多价疫苗，通过动物实验证明其可诱导交叉保护性抗体，有效预防链球菌感染。
2. **文献名称**：*"Structural and functional analysis of the GAM protein in immune evasion"*
**作者**：Bessen, D.E. & Fischetti, V.A.
**摘要**：解析GAM重组蛋白的抗原结构域，揭示其通过模拟宿主蛋白逃避免疫识别的机制，为靶向治疗提供依据。
3. **文献名称**：*"High-yield production of recombinant GAM protein in E. coli for immunological studies"*
**作者**：McNeil, S.A. et al.
**摘要**：优化大肠杆菌表达系统，实现GAM重组蛋白的高效可溶性表达，并验证其在血清分型和抗体检测中的应用价值。
4. **文献名称**：*"GAM protein-mediated pathogenesis and vaccine implications"*
**作者**：Steer, A.C. et al.
**摘要**：综述GAM蛋白在链球菌黏附、侵袭宿主细胞中的作用，探讨基于重组GAM的疫苗设计策略及临床试验进展。
(注：以上文献信息为领域内典型研究方向概括，实际引用需根据具体论文调整。)
**Background of Recombinant GAM Protein**
Recombinant GAM (Glycerol-Adapted Mutant) protein is a genetically engineered protein derived from modifications of native enzymes or structural proteins to enhance stability, solubility, or functional properties under specific conditions. The term "GAM" often refers to variants optimized for improved performance in biotechnological applications, particularly in environments with high glycerol concentrations or extreme conditions.
The development of recombinant GAM proteins stems from advances in molecular cloning and protein engineering. By introducing targeted mutations into the gene encoding the parent protein, researchers can alter its physicochemical characteristics. For instance, glycerol adaptation may involve modifying surface residues to reduce aggregation in glycerol-rich solutions, a common scenario in protein storage or industrial processes. Recombinant DNA technology enables the production of these tailored proteins in heterologous expression systems, such as *E. coli*, yeast, or mammalian cells, ensuring scalability and cost-effectiveness.
GAM proteins are particularly valuable in industrial enzymology, diagnostics, and therapeutic development. For example, glycerol-stable enzymes are critical in biocatalysis for pharmaceuticals or biofuels, where reaction mixtures often contain glycerol as a byproduct or stabilizer. In therapeutics, enhanced solubility and stability of recombinant proteins can improve shelf life and efficacy.
Recent studies also explore GAM variants in cryopreservation and extremophile-inspired biotechnology, leveraging their robustness for applications in harsh environments. The continuous optimization of expression systems and mutagenesis strategies, such as directed evolution or computational design, further refines GAM protein functionality.
Overall, recombinant GAM proteins exemplify the synergy between protein engineering and industrial demands, addressing challenges in stability and activity while expanding the scope of biotechnological innovations.
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