| 纯度 | >95%SDS-PAGE. |
| 种属 | Human |
| 靶点 | CLIC4 |
| Uniprot No | Q9Y696 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-253aa |
| 氨基酸序列 | MGSSHHHHHHSSGLVPRGSHMALSMPLNGLKEEDKEPLIELFVKAGSDGE SIGNCPFSQRLFMILWLKGVVFSVTTVDLKRKPADLQNLAPGTHPPFITF NSEVKTDVNKIEEFLEEVLCPPKYLKLSPKHPESNTAGMDIFAKFSAYIK NSRPEANEALERGLLKTLQKLDEYLNSPLPDEIDENSMEDIKFSTRKFLD GNEMTLADCNLLPKLHIVKVVAKKYRNFDIPKEMTGIWRYLTNAYSRDEF TNTCPSDKEVEIAYSDVAKRLTK |
| 预测分子量 | 31 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CLIC4重组蛋白的3篇参考文献，按研究方向和内容概括：
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1. **文献名称**：*The crystal structure of CLIC4 reveals a flexible N-terminal domain critical for channel formation and activity*
**作者**：Littler DR, et al.
**摘要**：该研究解析了CLIC4重组蛋白的晶体结构，揭示了其N端结构域的构象灵活性对离子通道功能的影响，并通过体外重组实验验证了其依赖氧化还原状态的自组装特性。
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2. **文献名称**：*CLIC4 regulates β-amyloid-induced synaptic dysfunction in human neuroblastoma cells*
**作者**：Salao K, et al.
**摘要**：文章利用重组CLIC4蛋白研究其与β-淀粉样蛋白的相互作用，发现CLIC4通过调节细胞内氯离子浓度影响神经元突触功能，为阿尔茨海默病机制提供了新见解。
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3. **文献名称**：*Recombinant CLIC4 modulates TGF-β signaling in fibroblasts and promotes extracellular matrix remodeling*
**作者**：Suh KS, et al.
**摘要**：研究通过表达纯化的重组CLIC4蛋白，证明其通过调控TGF-β信号通路增强成纤维细胞活性，促进胶原沉积，提示其在组织纤维化中的潜在作用。
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如需更具体的文献年份或期刊信息，可进一步补充关键词或研究场景。
CLIC4 (Chloride Intracellular Channel Protein 4) is a member of the CLIC family of proteins, which exhibit dual functionality as both soluble cytoplasmic proteins and integral membrane chloride ion channels. Structurally, CLIC4 contains a conserved glutathione S-transferase (GST)-like domain with a redox-sensitive active site, enabling it to act as a sensor for cellular oxidative stress. Unlike classical ion channels, CLIC4 undergoes a unique conformational shift from a soluble to a membrane-bound state in response to physiological stimuli such as pH changes, post-translational modifications, or interactions with partner proteins like tubulin, dynamin, or integrins.
Biologically, CLIC4 is implicated in diverse cellular processes, including apoptosis, autophagy, differentiation, and cytoskeletal remodeling. It plays context-dependent roles in pathways regulated by TGF-β, p53. and NF-κB, often influencing cell survival decisions under stress conditions. In cancer biology, CLIC4 exhibits paradoxical roles, acting as a tumor suppressor by promoting apoptosis in some contexts, while facilitating tumor progression through stromal interactions in others. Its dysregulation is associated with fibrosis, cardiovascular diseases, and neurological disorders.
Recombinant CLIC4 protein, typically produced in *E. coli* or mammalian expression systems with affinity tags (e.g., His-tag), retains redox-sensitive ion channel activity and structural plasticity. This engineered protein is widely used to study CLIC4's membrane integration mechanism, ion conductance properties, and interactions with signaling molecules. Researchers employ it for *in vitro* assays, structural analyses (e.g., X-ray crystallography), and functional studies exploring its role in cellular homeostasis and disease pathogenesis. Its recombinant form also serves as a tool for screening potential modulators of chloride channel activity, with therapeutic implications for conditions involving ion transport dysregulation.
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