| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | IgG |
| Uniprot No | P55899 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 24-297aa |
| 氨基酸序列 | AESHLSLLYHLTAVSSPAPGTPAFWVSGWLGPQQYLSYNSLRGEAEPCGAWVWENQVSWYWEKETTDLRIKEKLFLEAFKALGGKGPYTLQGLLGCELGPDNTSVPTAKFALNGEEFMNFDLKQGTWGGDWPEALAISQRWQQQDKAANKELTFLLFSCPHRLREHLERGRGNLEWKEPPSMRLKARPSSPGFSVLTCSAFSFYPPELQLRFLRNGLAAGTGQGDFGPNSDGSFHASSSLTVKSGDEHHYCCIVQHAGLAQPLRVELESPAKSS |
| 预测分子量 | 57.4 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3条关于IgG重组蛋白的示例文献概要(虚构内容，供参考)：
1. **文献名称**: *Optimization of Recombinant IgG Production in Mammalian Cell Systems*
**作者**: Smith J. et al.
**摘要**: 研究通过优化CHO细胞培养条件和载体设计，显著提高重组IgG的产量和稳定性，为规模化生产单克隆抗体提供新策略。
2. **文献名称**: *Engineering IgG Antibodies for Enhanced Therapeutic Efficacy*
**作者**: Lee H. et al.
**摘要**: 探讨通过基因工程改造IgG的Fc区域和抗原结合位点，增强其靶向性和半衰期，在肿瘤治疗模型中显示显著疗效提升。
3. **文献名称**: *High-throughput Screening of Recombinant IgG Expression in Yeast*
**作者**: Zhang Y. et al.
**摘要**: 开发基于酵母表达系统的高通量筛选平台，实现快速筛选高表达重组IgG的菌株，降低生产成本并缩短研发周期。
4. **文献名称**: *Quality Control of Recombinant IgG: Challenges and Solutions*
**作者**: Patel R. et al.
**摘要**: 分析重组IgG生产中糖基化异质性和聚集问题，提出基于质谱和色谱技术的质量控制方法，确保临床级抗体的批次一致性。
(注：以上文献及作者为示例性内容，非真实存在)
**Background of Recombinant IgG Proteins**
Immunoglobulin G (IgG), the most abundant antibody in human serum, plays a central role in adaptive immunity by neutralizing pathogens, activating complement systems, and mediating effector cell responses. Structurally, IgG consists of two heavy and two light chains forming a Y-shaped molecule with antigen-binding (Fab) and crystallizable (Fc) regions. Its four subclasses (IgG1–4) exhibit distinct biological functions, such as varying half-lives and Fc-mediated effector activities.
The development of recombinant IgG technology emerged alongside advances in genetic engineering and biomanufacturing. Traditional antibody production relied on animal immunization or hybridoma techniques, but these methods faced limitations in scalability, batch consistency, and ethical concerns. Recombinant DNA technology enabled the precise engineering of IgG molecules by cloning antibody genes into expression vectors, followed by production in host systems like mammalian cells (e.g., CHO or HEK293), yeast, or bacteria. Mammalian systems remain dominant due to their ability to perform proper post-translational modifications, such as glycosylation, critical for IgG stability and function.
Recombinant IgG production typically involves gene synthesis, vector construction, host cell transfection, and purification using Protein A/G affinity chromatography. Innovations like transient expression systems and CRISPR-edited cell lines have enhanced yield and reduced timelines.
Applications of recombinant IgG span therapeutics, diagnostics, and research. Therapeutic monoclonal antibodies (e.g., rituximab, trastuzumab) target cancers, autoimmune diseases, and infections. In diagnostics, recombinant IgG serves as standardized reagents for assays, improving reproducibility. Researchers also engineer IgG variants (e.g., Fc-silenced or bispecific formats) to tailor immune responses.
Challenges include optimizing glycosylation patterns, ensuring stability, and reducing production costs. Nonetheless, recombinant IgG remains a cornerstone of biologics, with ongoing advancements in AI-driven design and alternative expression platforms (e.g., plant cells) promising to expand its therapeutic potential.
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