| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | IgA2 |
| Uniprot No | P0DOX2 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-455aa |
| 氨基酸序列 | EVQLVETGGGLIQPGGSLRLSCAASGFTVSNHSMSWVRQAPGKALEWVSAIYRGGTTYYADSVKGRFTISRDDSRNTVYLQMNSLRAEDTAVYYCARDLAAARLFGKGTTVTVSSASPTSPKVFPLSLDSTPQDGNVVVACLVQGFFPQEPLSVTWSESGQNVTARNFPPSQDASGDLYTTSSQLTLPATQCPDGKSVTCHVKHYTNSSQDVTVPCRVPPPPPCCHPRLSLHRPALEDLLLGSEANLTCTLTGLRDASGATFTWTPSSGKSAVEGPPERDLCGCYSVSSVLPGCAQPWNHGETFTCTAAHPELKTPLTANITKSGNTFRPEVHLLPPPSEELALNELVTLTCLARGFSPKDVLVRWLQGSQELPREKYLTWASRQEPSQGTTTYAVTSILRVAAEDWKKGETFSCMVGHEALPLAFTQKTIDRLAGKPTHINVSVVMAEADGTCY |
| 预测分子量 | 48,9 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IgA2重组蛋白的3篇参考文献的简要概括：
1. **文献名称**：*Recombinant IgA2 antibodies for targeted cancer therapy*
**作者**：Smith A, et al.
**摘要**：研究报道了一种新型重组IgA2抗体的开发，通过哺乳动物表达系统高效生产，并验证其在靶向癌细胞表面的特异性抗原时的增强效应，相比IgG抗体展现出更强的中和活性。
2. **文献名称**：*Structural and functional characterization of recombinant human IgA2*
**作者**：Li Y, et al.
**摘要**：通过X射线晶体学解析重组人IgA2的分子结构，分析其铰链区短、糖基化位点独特的特征，阐明其在黏膜免疫中的作用及与IgA1的功能差异。
3. **文献名称**：*Production of secretory IgA2 in plant-based expression systems*
**作者**：Wang Q, et al.
**摘要**：利用植物表达系统成功生产重组分泌型IgA2.验证其与黏膜病原体结合的能力，为低成本大规模生产治疗性IgA2抗体提供新方法。
注：上述文献为虚拟示例，实际研究中请通过学术数据库(如PubMed、Web of Science)检索具体论文。
Immunoglobulin A (IgA) is a critical antibody class in mucosal immunity, predominantly existing as two subclasses: IgA1 and IgA2. IgA2. particularly the IgA2(m1) and IgA2(m2) allotypes, exhibits structural distinctions from IgA1. including a shorter hinge region and lack of O-glycosylation sites. These features enhance its resistance to bacterial proteases, making it more stable in protease-rich mucosal environments like the gut. IgA2 constitutes up to 30% of total IgA in mucosal secretions, where it neutralizes pathogens, blocks microbial adhesion, and regulates commensal microbiota.
Recombinant IgA2 production addresses challenges in studying and utilizing native IgA, which is difficult to isolate in pure forms due to low serum concentrations and structural complexity. Recombinant technology enables precise engineering of IgA2 molecules with tailored properties, such as improved stability, effector functions, or antigen specificity. Mammalian expression systems (e.g., CHO or HEK293 cells) are typically employed to ensure proper glycosylation and assembly of the tetrameric structure (two heavy chains, two light chains, and a joining chain). However, production hurdles persist, including low yields, aggregation, and the need for co-expression of molecular chaperones.
Research on recombinant IgA2 focuses on its therapeutic potential in mucosal infections (e.g., respiratory viruses, enteric pathogens), inflammatory diseases, and cancer immunotherapy. Unlike IgG, IgA2 engages unique receptors (e.g., FcαRI) on immune cells, promoting phagocytosis and neutrophil recruitment, while minimizing inflammatory cascades. Recent advances in glycoengineering and bispecific formats further expand its applicability. Despite progress, scalable manufacturing and pharmacokinetic optimization remain active areas of development to unlock IgA2’s full clinical potential.
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