| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | IgA1 |
| Uniprot No | P01876 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-398aa |
| 氨基酸序列 | ASPTSPKVFPLSLCSTQPDGNVVIACLVQGFFPQEPLSVTWSESGQGVTARNFPPSQDASGDLYTTSSQLTLPATQCLAGKSVTCHVKHYTNPSQDVTVPCPVPSTPPTPSPSTPPTPSPSCCHPRLSLHRPALEDLLLGSEANLTCTLTGLRDASGVTFTWTPSSGKSAVQGPPERDLCGCYSVSSVLPGCAEPWNHGKTFTCTAAYPESKTPLTATLSKSGNTFRPEVHLLPPPSEELALNELVTLTCLARGFSPKDVLVRWLQGSQELPREKYLTWASRQEPSQGTTTFAVTSILRVAAEDWKKGDTFSCMVGHEALPLAFTQKTIDRLADWQMPPPYVVLDLPQETLEEETPGANLWPTTITFLTLFLLSLFYSTALTVTSVRGPSGNREGPQY |
| 预测分子量 | 42,8 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IgA1重组蛋白的3篇参考文献及其摘要概括：
1. **文献名称**：Production of recombinant human IgA1 with tailored glycosylation in CHO cells
**作者**：M. W. Steenbakkers et al.
**摘要**：该研究利用CHO细胞表达系统成功重组生产了人源IgA1蛋白，并通过基因编辑技术调控其糖基化模式。实验表明，重组IgA1的糖链结构与其天然形式高度相似，且在体外模型中保留了与Fcα受体(CD89)的结合活性。
2. **文献名称**：Recombinant IgA1 proteases as tools for studying IgA1-related immune complexes in IgA nephropathy
**作者**：J. Novak et al.
**摘要**：作者通过重组技术表达了IgA1蛋白及其蛋白酶，用于研究IgA肾病中异常糖基化IgA1与抗体的免疫复合物形成机制。结果显示，重组IgA1的O-糖基化缺失会显著增强其与自身抗体的结合能力，提示其在疾病病理中的关键作用。
3. **文献名称**：Functional characterization of recombinant human IgA1 antibodies against respiratory pathogens
**作者**：K. E. van Egmond et al.
**摘要**：该研究构建了针对呼吸道病原体的重组IgA1抗体，并验证其在中和病原体及激活黏膜免疫应答中的功能。实验发现，重组IgA1在抑制病毒入侵和促进吞噬细胞清除病原体方面优于IgG抗体，突显其在黏膜免疫治疗中的潜力。
4. **文献名称**：Structural analysis of recombinant IgA1 reveals key determinants of polymer formation
**作者**：S. C. Hitchcock et al.
**摘要**：通过X射线晶体学和质谱技术解析重组IgA1的结构，揭示了其多聚化所需的铰链区特征及糖基化位点。研究为设计稳定且功能优化的重组IgA1抗体药物提供了结构基础。
以上文献聚焦于IgA1重组蛋白的生产、糖基化调控、功能分析及疾病机制研究，覆盖了基础研究和应用方向。
Immunoglobulin A (IgA) is the predominant antibody class in mucosal secretions and plays a critical role in defending mucosal surfaces against pathogens. IgA exists as two subclasses, IgA1 and IgA2. with IgA1 being the major form in serum and upper mucosal tissues. Structurally, IgA1 contains a unique 18-amino acid hinge region between its Fab and Fc domains, which is heavily O-glycosylated. This region confers flexibility for antigen binding but also makes IgA1 susceptible to proteolytic cleavage by bacterial enzymes, a mechanism pathogens exploit to evade immune responses.
Recombinant IgA1 production aims to study its biological functions, therapeutic potential, and role in diseases. Unlike IgG antibodies, IgA1’s complex glycosylation and dimeric/multimeric assembly pose challenges for recombinant expression. Mammalian cell lines (e.g., CHO or HEK293) are typically used to ensure proper post-translational modifications, particularly O-glycosylation in the hinge region. Advances in expression systems now enable scalable production of monomeric or dimeric IgA1 with preserved effector functions, such as binding to FcαRI (CD89) on immune cells.
Research on recombinant IgA1 has shed light on its dual role in immunity and pathology. For instance, in IgA nephropathy (IgAN), the most common glomerulonephritis, galactose-deficient O-glycans in the IgA1 hinge region are recognized as autoantigens, triggering immune complex formation and kidney injury. Recombinant IgA1 variants with engineered glycosylation patterns help dissect these mechanisms. Additionally, IgA1-based therapeutics are being explored for mucosal infections, cancer, and autoimmune diseases, leveraging its ability to recruit neutrophils and mediate phagocytosis or ADCC.
Overall, recombinant IgA1 serves as a vital tool for understanding mucosal immunity, host-pathogen interactions, and autoimmune pathways, while offering a foundation for novel biologic therapies.
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