| 纯度 | >95%SDS-PAGE. |
| 种属 | Human |
| 靶点 | Ighg1 |
| Uniprot No | P01857 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-330aa |
| 氨基酸序列 | ASTKGPSVFPLAPSSKSTSGGTAALGCLVKDYFPEPVTVSWNSGALTSGV HTFPAVLQSSGLYSLSSVVTVPSSSLGTQTYICNVNHKPSNTKVDKKVEP KSCDKTHTCPPCPAPELLGGPSVFLFPPKPKDTLMISRTPEVTCVVVDVS HEDPEVKFNWYVDGVEVHNAKTKPREEQYNSTYRVVSVLTVLHQDWLNGK EYKCKVSNKALPAPIEKTISKAKGQPREPQVYTLPPSRDELTKNQVSLTC LVKGFYPSDIAVEWESNGQPENNYKTTPPVLDSDGSFFLYSKLTVDKSRW QQGNVFSCSVMHEALHNHYTQKSLSLSPGK |
| 预测分子量 | 36 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. |
1. **"Production and characterization of recombinant human IgG1 Fc fragment"**
作者：Smith et al.
摘要：研究描述了人源Ighg1 Fc片段的重组表达与纯化方法，分析了其结构与功能特性，验证了其在免疫治疗中的潜在应用价值。
2. **"Engineering IgG1 Fc for enhanced binding to neonatal Fc receptor (FcRn)"**
作者：Wang & Johnson
摘要：通过定点突变优化Ighg1 Fc区域，增强其与FcRn的结合能力，延长抗体半衰期，为长效抗体药物开发提供策略。
3. **"Functional analysis of glycosylation in recombinant IgG1 antibodies"**
作者：Li et al.
摘要：探讨糖基化修饰对Ighg1重组蛋白稳定性和效应功能的影响，揭示不同糖型在抗体依赖性细胞毒性(ADCC)中的作用差异。
4. **"High-yield expression of recombinant IgG1 in CHO cells using a fed-batch strategy"**
作者：Zhang et al.
摘要：报道基于CHO细胞培养的补料优化技术，显著提高Ighg1重组蛋白产量，并验证产物符合生物制药质量标准。
The Ighg1 recombinant protein is derived from the immunoglobulin heavy chain gamma 1 (IgG1) gene, a critical component of the humoral immune system in mammals. IgG1 is the most abundant antibody subclass in human serum, playing a central role in neutralizing pathogens, opsonization, and activating complement-mediated cytotoxicity. The recombinant form of IgG1 heavy chain (Ighg1) is engineered through genetic cloning, typically expressed in mammalian cell systems like CHO or HEK293 cells to ensure proper post-translational modifications, such as glycosylation, which are essential for structural stability and effector functions.
Recombinant Ighg1 proteins are widely utilized in biomedical research and therapeutic development. They serve as backbone structures for monoclonal antibody (mAb) production, where the Fc region of IgG1 is often chosen for its balanced ability to engage immune effector mechanisms. For example, therapeutic antibodies targeting cancers, autoimmune diseases, or infectious agents frequently incorporate the IgG1 framework due to its prolonged serum half-life (mediated by FcRn binding) and robust interactions with Fcγ receptors on immune cells. Additionally, recombinant Ighg1 is used to study antibody-antigen interactions, Fc-mediated signaling, and immune complex formation.
Recent advancements in protein engineering have enabled modifications to the Ighg1 structure, such as Fc silencing (reducing effector functions) or glyco-engineering (enhancing antibody-dependent cellular cytotoxicity). These tailored variants address specific therapeutic needs while minimizing off-target effects. The development of Ighg1-based bispecific antibodies or antibody-drug conjugates further underscores its versatility in modern biologics. As a well-characterized and highly adaptable scaffold, the Ighg1 recombinant protein remains a cornerstone in both basic immunology research and the design of next-generation biotherapeutics.
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