| 纯度 | > 95 % SDS-PAGE. |
| 种属 | Human |
| 靶点 | CLEC2C |
| Uniprot No | Q07108 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 62-199aa |
| 氨基酸序列 | SVGQYNCPG QYTFSMPSDS HVSSCSEDWV GYQRKCYFIS TVKRSWTSAQ NACSEHGATL AVIDSEKDMN FLKRYAGREE HWVGLKKEPG HPWKWSNGKE FNNWFNVTGS DKCVFLKNTE VSSMECEKNL YWICNKPYK |
| 预测分子量 | 17 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CLEC2C重组蛋白的示例参考文献(部分内容基于相关研究领域推断，供参考)：
1. **文献名称**: "Characterization of CLEC2C as a novel C-type lectin involved in NK cell activation"
**作者**: Smith A, et al.
**摘要**: 本研究首次成功重组表达CLEC2C蛋白，证实其通过结合细胞表面糖基化配体激活NK细胞的细胞毒性，揭示了其在天然免疫中的潜在调控作用。
2. **文献名称**: "Structural and functional analysis of recombinant CLEC2C in platelet signaling"
**作者**: Zhang L, et al.
**摘要**: 通过晶体学解析CLEC2C重组蛋白结构，发现其与血小板受体CLEC-2存在交叉反应，可能参与血栓形成调节，为抗凝药物开发提供新靶点。
3. **文献名称**: "CLEC2C recombinant protein binds viral glycoproteins and inhibits HIV-1 entry"
**作者**: Gupta R, et al.
**摘要**: 体外实验表明重组CLEC2C蛋白可特异性结合HIV包膜蛋白gp120.阻断病毒与宿主细胞融合，提示其抗病毒治疗应用潜力。
4. **文献名称**: "Expression and purification of functional CLEC2C in a mammalian system for ligand screening"
**作者**: Tanaka K, et al.
**摘要**: 开发哺乳动物细胞表达体系制备高纯度CLEC2C重组蛋白，并建立基于该蛋白的配体筛选平台，鉴定出多个潜在相互作用分子。
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**注意**：CLEC2C研究相对较少，上述文献为模拟示例。实际研究中建议通过PubMed/Google Scholar以“CLEC2C recombinant protein”为关键词检索最新文献，或关注C型凝集素家族(如CLEC2D、CLEC5A)相关研究作为扩展。
CLEC2C (C-type lectin domain family 2 member C) is a transmembrane protein belonging to the C-type lectin-like receptor family, which plays diverse roles in immune regulation and cellular interactions. Initially identified as a natural killer (NK) cell receptor, CLEC2C is expressed on immune cells such as NK cells, dendritic cells, and T lymphocytes. It features a conserved C-type lectin-like extracellular domain, a transmembrane region, and a cytoplasmic tail containing immunoreceptor tyrosine-based inhibitory motifs (ITIMs), suggesting its involvement in inhibitory signaling pathways. CLEC2C interacts with ligands like LLT1 (CLEC2D) to modulate immune responses, including NK cell cytotoxicity and cytokine production, balancing immune activation and tolerance.
Recombinant CLEC2C protein is engineered using biotechnological methods, typically through cloning the CLEC2C gene into expression vectors (e.g., mammalian or bacterial systems) to produce soluble or membrane-bound forms. This protein retains functional domains critical for ligand binding and signaling studies. Researchers utilize it to explore its immunological roles, such as its suppressive effects on NK cell activity or its potential in regulating autoimmune diseases and cancer immunity. For instance, CLEC2C-ligand interactions may dampen excessive immune activation, making it a therapeutic target for inflammatory disorders. Structural studies of recombinant CLEC2C also aid in mapping binding interfaces for drug design.
Current research focuses on clarifying its physiological ligands, signaling mechanisms, and therapeutic applications. Challenges include understanding tissue-specific expression patterns and reconciling conflicting data on its pro- or anti-inflammatory roles. As interest grows in immunomodulatory therapies, recombinant CLEC2C serves as a vital tool for deciphering immune checkpoint biology and developing targeted interventions.
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