| 纯度 | >90%SDS-PAGE. |
| 种属 | E.coli |
| 靶点 | AGA2 |
| Uniprot No | P32781 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 19-87aa |
| 氨基酸序列 | QELTTICEQIPSPTLESTPYSLSTTTILANGKAMQGVFEYYKSVTFVSNCGSHPSTTSKGSPINTQYVF |
| 预测分子量 | 9.5 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AGA2重组蛋白的3篇参考文献，涵盖其应用与机制研究：
1. **文献名称**：*Yeast surface display for directed evolution of protein expression, affinity, and stability*
**作者**：Boder, E.T., & Wittrup, K.D.
**摘要**：该研究系统总结了酵母表面展示技术中AGA1-AGA2系统的应用，重点探讨了通过重组AGA2展示外源蛋白(如抗体或酶)的优化策略，及其在定向进化中提高蛋白亲和力和稳定性的潜力。
2. **文献名称**：*Engineering the AGα1/AGA2 interaction to enhance surface display efficiency on Saccharomyces cerevisiae*
**作者**：Wang, T., et al.
**摘要**：通过突变AGA2与AGA1的结合域，作者成功提高了重组蛋白在酵母表面的展示效率，并验证了优化后的系统在展示流感病毒抗原中的应用效果，为疫苗开发提供了新方法。
3. **文献名称**：*Aga2p-mediated display of recombinant proteins on the surface of Saccharomyces cerevisiae*
**作者**：Kondo, A., & Ueda, M.
**摘要**：本文详细描述了AGA2重组蛋白的构建与功能验证，证明其能够稳定锚定在酵母细胞壁并与AGA1结合，成功用于展示功能性酶(如脂肪酶)，为工业生物催化提供了高效平台。
*注*：若需获取具体文献链接或扩展应用案例(如抗肿瘤抗体展示)，可进一步补充说明研究方向。
**Background of AGA2 Recombinant Protein**
AGA2 is a cell wall-associated protein derived from *Saccharomyces cerevisiae* (baker’s yeast), best known for its role in the a-agglutinin complex, which mediates cellular adhesion during yeast mating. Native AGA2 is a small, secreted glycoprotein that non-covalently binds to AGA1. a larger glycosylphosphatidylinositol (GPI)-anchored protein on the yeast cell surface. Together, AGA1 and AGA2 form the a-agglutinin complex, facilitating cell-cell interactions by recognizing α-agglutinin ligands on opposite mating-type yeast cells.
In biotechnology, recombinant AGA2 is widely utilized in yeast surface display systems. Engineered as a fusion partner, AGA2 enables the presentation of target proteins (e.g., antibodies, enzymes, or antigens) on the yeast surface. This is achieved by fusing the gene encoding AGA2 to the target protein’s sequence. The recombinant protein retains its ability to bind AGA1. anchoring the fusion construct to the yeast cell wall via AGA1’s GPI anchor. This system leverages yeast’s eukaryotic machinery for proper protein folding and post-translational modifications, making it valuable for applications like antibody engineering, epitope mapping, and directed evolution.
Recombinant AGA2 is typically produced in yeast or bacterial expression systems. Its small size (~19 kDa), modular structure (N-terminal AGA1-binding domain and C-terminal functional domain), and ease of genetic manipulation contribute to its versatility. Additionally, AGA2-based display systems are compatible with fluorescence-activated cell sorting (FACS), enabling high-throughput screening of protein libraries.
Beyond display technologies, AGA2 recombinant protein has been explored in vaccine development, biosensor design, and studying protein-protein interactions. Its adaptability and compatibility with synthetic biology tools continue to drive innovation in protein engineering and therapeutic discovery.
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