| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | GA |
| Uniprot No | P24522 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-165aa |
| 氨基酸序列 | MTLEEFSAGEQKTERMDKVGDALEEVLSKALSQRTITVGVYEAAKLLNVDPDNVVLCLLAADEDDDRDVALQIHFTLIQAFCCENDINILRVSNPGRLAELLLLETDAGPAASEGAEQPPDLHCVLVTNPHSSQWKDPALSQLICFCRESRYMDQWVPVINLPER |
| 预测分子量 | 34.3 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GA重组蛋白的参考文献示例(注：以下文献为虚构示例，仅供参考格式)：
1. **文献名称**：High-Yield Expression and Purification of Recombinant GA Protein in Escherichia coli
**作者**：Chen, X., Wang, Y., & Liu, Z.
**摘要**：研究报道了一种优化的大肠杆菌表达系统，用于高效生产重组GA蛋白，并通过亲和层析技术实现了高纯度纯化，为后续功能研究奠定了基础。
2. **文献名称**：Functional Analysis of Recombinant GA Protein in Immune Response Modulation
**作者**：Smith, J.R., et al.
**摘要**：通过体外实验证实重组GA蛋白能够激活树突状细胞的TLR4通路，提示其在疫苗佐剂或免疫治疗中的潜在应用价值。
3. **文献名称**：Crystal Structure of GA Recombinant Protein Reveals Key Functional Domains
**作者**：Tanaka, M., et al.
**摘要**：利用X射线晶体学解析了重组GA蛋白的三维结构，揭示了其与配体结合的关键区域，为靶向药物设计提供结构基础。
4. **文献名称**：Scale-Up Production of Recombinant GA Protein Using Mammalian Cell Culture
**作者**：Zhang, H., et al.
**摘要**：开发了一种基于HEK293细胞的规模化重组GA蛋白生产工艺，并验证其糖基化修饰对蛋白稳定性的影响。
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**建议**：如需真实文献，请通过PubMed、Google Scholar等平台搜索关键词(如“recombinant GA protein expression”或“GA protein application”)，并筛选近年研究以获取最新进展。
**Background of GA Recombinant Proteins**
Recombinant proteins, engineered through genetic modification techniques, have revolutionized biomedical research and therapeutic development since the advent of recombinant DNA technology in the 1970s. GA recombinant proteins, specifically, refer to glycoprotein antigens or engineered variants derived from pathogens, often utilized in vaccine development, diagnostic tools, or therapeutic agents. The "GA" designation may correspond to specific targets, such as viral surface proteins (e.g., influenza hemagglutinin) or bacterial antigens, tailored to enhance immunogenicity or stability.
The production of GA recombinant proteins typically involves inserting pathogen-derived gene sequences into expression systems like *E. coli*, yeast, or mammalian cells (e.g., CHO cells). Mammalian systems are preferred for glycosylation, ensuring proper post-translational modifications critical for protein function and immune recognition. Advances in synthetic biology and protein engineering, such as structure-guided design or codon optimization, have further improved yield, purity, and antigenic fidelity.
GA recombinant proteins gained prominence during the COVID-19 pandemic, underpinning subunit vaccine platforms targeting SARS-CoV-2 spike proteins. Their safety profile—avoiding live pathogens—and scalability make them attractive for rapid response to emerging diseases. Beyond vaccines, they serve as tools for antibody production, epitope mapping, and serological assays. Challenges remain, including optimizing thermostability for global distribution and balancing cost-effectiveness with complex production requirements. Ongoing research focuses on multifunctional GA designs, such as fusion proteins or nanoparticle displays, to broaden immunological efficacy against evolving pathogens.
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