| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | IgM |
| Uniprot No | P01871 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-474aa |
| 氨基酸序列 | MNYYWGQRTLVTVSSGSASAPTLFPLVSCENSPSDTSSVAVGCLAQDFLP DSITFSWKYKNNSDISSTRGFPSVLRGGKYAATSQVLLPSKDVMQGTDEH VVCKVQHPNGNKEKNVPLPVIAELPPKVSVFVPPRDGFFGNPRKSKLICQ ATGFSPRQIQVSWLREGKQVGSGVTTDQVQAEAKESGPTTYKVTSTLTIK ESDWLGQSMFTCRVDHRGLTFQQNASSMCVPDQDTAIRVFAIPPSFASIF LTKSTKLTCLVTDLTTYDSVTISWTRQNGEAVKTHTNISESHPNATFSAV GEASICEDDWNSGERFTCTVTHTDLPSPLKQTISRPKGVALHRPDVYLLP PAREQLNLRESATITCLVTGFSPADVFVQWMQRGQPLSPEKYVTSAPMPE PQAPGRYFAHSILTVSEEEWNTGETYTCVVAHEALPNRVTERTVDKSTEG EVSADEEGFENLWATASTFIVLFLLSLFYSTTVTLFKVK |
| 预测分子量 | 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IgM重组蛋白的3篇示例参考文献(注：文献信息为虚构示例，建议通过学术数据库检索真实文献)：
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1. **文献名称**: *"Efficient Production of Recombinant IgM in Mammalian Expression Systems"*
**作者**: Smith J, et al.
**摘要**: 研究探讨了在HEK293细胞中高效表达功能性IgM五聚体的策略，通过优化载体设计和培养条件，成功实现高产量重组IgM，并验证其与抗原结合及补体激活能力。
2. **文献名称**: *"Engineering IgM Antibodies for Enhanced Pathogen Neutralization"*
**作者**: Lee H, et al.
**摘要**: 报道了一种基因工程技术改造IgM可变区的方法，提升其对流感病毒血凝素蛋白的亲和力，体外实验显示改造后的重组IgM中和病毒效率显著高于天然IgM。
3. **文献名称**: *"Recombinant IgM as a Diagnostic Tool for Early-Stage Cancers"*
**作者**: Chen R, et al.
**摘要**: 开发了基于重组IgM的肿瘤标志物检测平台，利用其多价结合特性提高检测灵敏度，在早期结直肠癌患者血清中成功识别低浓度靶标蛋白。
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**建议**：可通过PubMed、Google Scholar等平台检索关键词“recombinant IgM antibody”、“IgM expression engineering”获取真实文献。
**Background of Recombinant IgM Antibodies**
Immunoglobulin M (IgM), a large pentameric antibody, plays a critical role in the early stages of adaptive immune responses. As the first antibody isotype produced during infection or vaccination, IgM excels in pathogen neutralization and complement activation due to its multivalent structure (10 antigen-binding sites per molecule). However, native IgM’s size (~970 kDa) and complexity (linked by J-chains and stabilized by disulfide bonds) pose challenges for production and therapeutic application.
Recombinant IgM technology emerged to overcome limitations of conventional IgM isolation from plasma or hybridoma cultures, which suffer from low yield, batch variability, and ethical concerns. By leveraging genetic engineering, recombinant IgM is produced in mammalian cell lines (e.g., CHO or HEK293) or alternative systems (insect cells, plants), ensuring controlled glycosylation and scalability. Key innovations include codon-optimized gene constructs, co-expression of J-chain and chaperone proteins, and tailored culture conditions to facilitate proper pentamer assembly.
Therapeutic interest in recombinant IgM stems from its high avidity for repetitive epitopes on viruses, bacteria, or cancer cells, potentially outperforming IgG in targeting membrane-bound antigens or immune evasion mechanisms. Preclinical studies highlight its potential in treating infections (e.g., HIV, SARS-CoV-2), B-cell malignancies, and autoimmune disorders. Additionally, engineered IgM variants with enhanced effector functions or extended half-life are under exploration.
Despite progress, challenges persist, such as maintaining structural stability during purification and minimizing aggregation. Advances in expression systems, glycoengineering, and analytics continue to drive the development of recombinant IgM as a next-generation biologic, bridging the gap between natural immunity and tailored immunotherapy.
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