| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | IgG2 |
| Uniprot No | P01859 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 99-326aa |
| 氨基酸序列 | ERKCCVECPPCPAPPVAGPSVFLFPPKPKDTLMISRTPEVTCVVVDVSHE DPEVQFNWYVDGVEVHNAKTKPREEQFNSTFRVVSVLTVVHQDWLNGKEY KCKVSNKGLPAPIEKTISKTKGQPREPQVYTLPPSREEMTKNQVSLTCLV KGFYPSDISVEWESNGQPENNYKTTPPMLDSDGSFFLYSKLTVDKSRWQQ GNVFSCSVMHEALHNHYTQKSLSLSPGK |
| 预测分子量 | 26 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篇与IgG2重组蛋白相关的文献摘要概括(虚构示例，供参考)：
1. **标题**：Structural Characterization of Recombinant IgG2 Variants with Altered Hinge Disulfide Bonding
**作者**：Zhang Y. et al.
**摘要**：研究利用质谱和X射线晶体学分析了重组IgG2抗体不同铰链区二硫键异构体的结构差异，发现异构化影响Fab段柔韧性和抗原结合活性，为IgG2类药物的质量控制提供依据。
2. **标题**：Expression Optimization of IgG2 in CHO Cells: Impact of Glycosylation Patterns on Stability
**作者**：King L.M. et al.
**摘要**：通过优化CHO细胞培养条件调控IgG2的糖基化修饰，发现甘露糖含量降低可显著提高重组蛋白的热稳定性，同时不影响其Fcγ受体结合能力。
3. **标题**：Comparative Analysis of IgG1 vs. IgG2 in Tumor Targeting: Pharmacokinetics and Efficacy
**作者**：Chao H. et al.
**摘要**：比较IgG1和IgG2重组抗体在荷瘤小鼠中的表现，发现IgG2因较低的Fc介导的免疫清除作用，显示出更长的半衰期和增强的实体瘤穿透能力。
注：以上为模拟内容，实际文献需通过PubMed/Google Scholar检索关键词(如"recombinant IgG2 production"、"IgG2 structure-function")。真实文献可参考期刊如《mAbs》《Journal of Biological Chemistry》等。
**Background of Recombinant IgG2 Protein**
Immunoglobulin G (IgG) is the most abundant antibody class in human serum, playing a central role in adaptive immunity. Among its four subtypes (IgG1. IgG2. IgG3. IgG4), IgG2 is distinguished by its unique structural and functional properties. IgG2 antibodies are primarily involved in responses to polysaccharide antigens, such as those found in bacterial capsules, and exhibit reduced effector functions compared to IgG1. This lower affinity for activating Fcγ receptors (FcγR) and complement proteins (C1q) makes IgG2 less potent in triggering inflammatory responses, which can be advantageous in therapeutic contexts where excessive immune activation is undesirable.
Recombinant IgG2 proteins are engineered using biotechnological platforms, often through mammalian cell expression systems (e.g., CHO cells). The production involves cloning the heavy and light chain genes into expression vectors, followed by transfection, protein secretion, and purification via techniques like Protein A/G chromatography. The IgG2 subclass features a shorter hinge region and distinct disulfide bonding patterns, contributing to its rigid structure and reduced flexibility. These structural traits influence antigen binding and stability, necessitating careful optimization during manufacturing to ensure proper folding and post-translational modifications.
Therapeutic applications of recombinant IgG2 include treatments for infectious diseases, autoimmune disorders, and cancer. For instance, IgG2-based biologics may offer targeted neutralization of pathogens or cytokines with minimized off-target inflammation. However, challenges persist in balancing efficacy and manufacturability, as IgG2's limited effector functions may require engineering (e.g., Fc domain modifications) for specific use cases. Analytical characterization—such as SEC-HPLC, mass spectrometry, and binding assays—is critical to verify purity, stability, and functionality. Overall, recombinant IgG2 represents a versatile tool in both therapeutic development and biomedical research, bridging specificity with controlled immune modulation.
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