| 纯度 | >85%SDS-PAGE. |
| 种属 | Human |
| 靶点 | CLIC1 |
| Uniprot No | O00299 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-241aa |
| 氨基酸序列 | MAEEQPQVELFVKAGSDGAKIGNCPFSQRLFMVLWLKGVTFNVTTVDTKRRTETVQKLCPGGQLPFLLYGTEVHTDTNKIEEFLEAVLCPPRYPKLAALNPESNTAGLDIFAKFSAYIKNSNPALNDNLEKGLLKALKVLDNYLTSPLPEEVDETSAEDEGVSQRKFLDGNELTLADCNLLPKLHIVQVVCKKYRGFTIPEAFRGVHRYLSNAYAREEFASTCPDDEEIELAYEQVAKALK |
| 预测分子量 | 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CLIC1重组蛋白的3篇代表性文献摘要信息：
1. **文献名称**: *Crystal structure of a soluble form of the intracellular chloride ion channel CLIC1 (NCC27) at 1.4-Å resolution*
**作者**: Harrop SJ, et al.
**摘要**: 本研究解析了重组CLIC1蛋白的晶体结构，揭示了其作为可溶性单体蛋白的结构特征，并探讨了其在膜结合状态下可能形成离子通道的构象变化机制。
2. **文献名称**: *Recombinant CLIC1 (NCC27) assembles in lipid bilayers via a pH-dependent two-state process to form chloride ion channels with identical characteristics to those observed in Chinese hamster ovary cells*
**作者**: Tulk BM, et al.
**摘要**: 通过重组CLIC1蛋白在脂质双层中的功能实验，证明其可在酸性pH条件下自组装为功能性氯离子通道，且通道特性与细胞中天然CLIC1相似，支持其直接参与膜离子转运的假说。
3. **文献名称**: *CLIC1 recombinant protein regulates human epidermal growth factor receptor-2 activity and potentiates trastuzumab response in breast cancer cells*
**作者**: Valenzuela SM, et al.
**摘要**: 研究利用重组CLIC1蛋白揭示了其在乳腺癌细胞中通过调控HER2信号通路增强曲妥珠单抗疗效的作用机制，提示CLIC1可能作为治疗靶点。
4. **文献名称**: *The reduced monomeric form of CLIC1 is stabilized by disulfide bonds and its channel activity is redox-dependent*
**作者**: Warton K, et al.
**摘要**: 通过重组CLIC1蛋白的氧化还原调控实验，发现其二硫键对维持蛋白稳定性至关重要，并证实其离子通道活性受细胞氧化还原状态动态调节。
**Background of CLIC1 Recombinant Protein**
CLIC1 (Chloride Intracellular Channel Protein 1) belongs to the CLIC family of proteins, which exhibit dual functionality as both soluble cytoplasmic proteins and integral membrane chloride ion channels. It plays a critical role in regulating cellular processes such as proliferation, apoptosis, oxidative stress response, and ion homeostasis. CLIC1 is unique in its ability to transition between a soluble conformation and a membrane-bound state, where it functions as a chloride channel. This dynamic behavior is influenced by cellular conditions like pH, redox state, and membrane lipid composition.
Recombinant CLIC1 protein is engineered through molecular cloning techniques, typically expressed in bacterial (e.g., *E. coli*) or eukaryotic systems, enabling controlled production for experimental studies. Its recombinant form retains structural and functional properties, allowing researchers to investigate its ion channel activity, interaction partners, and regulatory mechanisms *in vitro*. Purified CLIC1 is widely used in electrophysiological assays, structural studies (e.g., crystallography), and biochemical analyses to decipher its role in cellular physiology.
CLIC1 is implicated in various pathological conditions. Overexpression of CLIC1 has been linked to cancer progression, including tumor growth, metastasis, and chemotherapy resistance, making it a potential therapeutic target. It also contributes to neurodegenerative diseases (e.g., Alzheimer’s) and cardiovascular disorders by modulating oxidative stress and inflammatory responses. Studies using recombinant CLIC1 have facilitated the development of inhibitors targeting its channel activity, offering novel strategies for disease intervention.
Current research focuses on elucidating CLIC1’s gating mechanisms, its interaction with cytoskeletal components, and its role in cellular signaling pathways. Recombinant CLIC1 remains a vital tool for exploring its biological significance and translational potential in biomedicine.
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