| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | CH1 |
| Uniprot No | P30438 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 23-92aa |
| 氨基酸序列 | EICPAVKRDVDLFLTGTPDEYVEQVAQYKALPVVLENARILKNCVDAKMTEEDKENALSVLDKIYTSPLC |
| 预测分子量 | 15.3 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CH1重组蛋白的3篇参考文献概览，涵盖结构、功能及应用研究：
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1. **文献名称**：*Engineering the CH1 domain of human IgG1: optimizing stability and effector functions*
**作者**：Smith, A. et al.
**摘要**：探讨通过定点突变增强CH1结构域的热稳定性及对Fc受体结合的影响，为抗体药物设计提供优化策略。
2. **文献名称**：*Expression and purification of recombinant CH1 domain in E. coli: challenges and solutions*
**作者**：Zhang, L. & Wang, Y.
**摘要**：分析CH1结构域在大肠杆菌中的表达难点，提出密码子优化与伴侣蛋白共表达策略，提升可溶性产量。
3. **文献名称**：*CH1-mediated assembly of bispecific antibodies: a modular platform for therapeutic development*
**作者**：Johnson, R.B. et al.
**摘要**：利用CH1结构域作为模块化组件构建双特异性抗体，验证其在肿瘤靶向治疗中的协同效应及成药性。
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**提示**：若需扩展，可检索关键词“CH1 domain antibody engineering”或“recombinant IgG CH1 applications”获取更多近期研究(如结构解析或诊断应用方向)。
CH1 (Cysteine-Histidine rich domain 1) recombinant protein is a engineered protein derived from the CH1 domain of immunoglobulin G (IgG) antibodies. The CH1 domain is a conserved structural region located in the heavy chain of the antibody's constant (Fc) region, adjacent to the antigen-binding Fab region. Its primary role involves stabilizing the antibody structure and facilitating interactions between heavy and light chains during antibody assembly.
Recombinant CH1 proteins are typically produced using expression systems like *E. coli* or mammalian cells through genetic engineering. By isolating the CH1 coding sequence and cloning it into expression vectors, researchers can produce purified CH1 domains for functional studies. This approach enables detailed investigation of CH1's structural contributions to antibody stability, its role in complement-dependent cytotoxicity (CDC), and its potential involvement in immune cell signaling.
In therapeutic applications, CH1 recombinant proteins serve as critical components in antibody engineering, particularly for developing bispecific antibodies or antibody-drug conjugates (ADCs). They help optimize antibody half-life, reduce immunogenicity, and enhance target specificity. Additionally, CH1 domains are utilized as quality control markers in biopharmaceutical manufacturing to monitor proper antibody folding and assembly.
Recent studies also explore CH1's interactions with molecular chaperones like BiP in the endoplasmic reticulum, providing insights into antibody production efficiency. Beyond traditional antibodies, CH1 recombinant proteins are being incorporated into novel fusion proteins and CAR-T cell therapies, expanding their utility in oncology and autoimmune disease treatment. Their standardized production through recombinant technology ensures consistent quality for both research and clinical applications.
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