| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | IgG1 |
| Uniprot No | P05112 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 25-153aa |
| 氨基酸序列 | HKCDITLQEI IKTLNSLTEQ KTLCTELTVT DIFAASKNTT EKETFCRAAT VLRQFYSHHE KDTRCLGATA QQFHRHKQLI RFLKRLDRNL WGLAGLNSCP VKEANQSTLE NFLERLKTIM REKYSKCSS |
| 预测分子量 | 15.0 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3-4条关于IgG1重组蛋白的模拟参考文献示例(文献信息为虚构，仅用于示例)：
1. **文献名称**：*Optimization of IgG1 Recombinant Protein Production in CHO Cells*
**作者**：Smith A, et al.
**摘要**：研究通过优化CHO细胞培养条件和载体设计，显著提高了IgG1重组蛋白的产量和糖基化一致性，为规模化生产提供技术参考。
2. **文献名称**：*Structural and Functional Analysis of Engineered IgG1 Fc Domains*
**作者**：Johnson R, et al.
**摘要**：通过定点突变改造IgG1的Fc区域，增强其与Fcγ受体的结合能力，从而提升抗体依赖性细胞毒性(ADCC)效应，拓展治疗性抗体的应用潜力。
3. **文献名称**：*Stability Profiling of IgG1 Recombinant Antibodies under Stress Conditions*
**作者**：Lee H, et al.
**摘要**：系统评估了IgG1重组蛋白在不同pH、温度和储存条件下的稳定性，提出降解机制及制剂配方改进策略。
4. **文献名称**：*IgG1-Based Bispecific Antibodies: Design and Preclinical Efficacy*
**作者**：Wang Y, et al.
**摘要**：开发了一种基于IgG1的双特异性抗体平台，验证其在肿瘤模型中的靶向性和免疫激活功能，为癌症免疫治疗提供新思路。
(注：以上文献为模拟生成，实际引用需检索PubMed、Google Scholar等数据库获取真实文献。)
**Background of IgG1 Recombinant Proteins**
Immunoglobulin G1 (IgG1) is the most abundant antibody subclass in human serum, playing a central role in adaptive immunity. As a recombinant protein, IgG1 is engineered using biotechnological platforms, such as mammalian cell cultures (e.g., CHO or HEK293 cells), to mimic natural antibodies with high specificity and functionality. Structurally, recombinant IgG1 consists of two heavy chains and two light chains linked by disulfide bonds, forming a Y-shaped structure. The fragment crystallizable (Fc) region mediates effector functions, including antibody-dependent cellular cytotoxicity (ADCC) and complement-dependent cytotoxicity (CDC), while the antigen-binding fragment (Fab) recognizes specific epitopes.
Recombinant IgG1 antibodies have revolutionized therapeutic applications, particularly in oncology, autoimmune diseases, and infectious diseases. Their ability to target disease-specific antigens with precision has led to blockbuster drugs like trastuzumab (HER2-positive cancer) and rituximab (CD20-positive lymphomas). Additionally, IgG1’s Fc region can be engineered to enhance or silence effector functions, enabling tailored therapies. For example, afucosylation boosts ADCC activity, while amino acid mutations in the Fc domain can reduce inflammatory responses.
Production involves advanced bioprocessing to ensure proper folding, glycosylation (e.g., N-linked glycans at Asn297), and homogeneity. Quality control assays (e.g., mass spectrometry, HPLC) are critical to verify structural integrity and bioactivity. Challenges include minimizing aggregation, optimizing yield, and controlling post-translational modifications.
Beyond therapeutics, IgG1 recombinant proteins are vital tools in diagnostics, research, and biotechnology, serving as standards in immunoassays or probes for target validation. Their versatility, scalability, and well-characterized structure make IgG1 a cornerstone of modern biologics development. Ongoing innovations in protein engineering and manufacturing continue to expand their clinical and industrial potential.
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