| 纯度 | > 85 % SDS-PAGE. |
| 种属 | Human |
| 靶点 | CLEC7A |
| Uniprot No | Q9BXN2 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-77aa |
| 氨基酸序列 | MEYHPDLENLDEDGYTQLHFDSQSNTRIAVVSEKGSCAASPPWRLIAVIL GILCLVILVIAVVLGTMAGFKAVEFKG |
| 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3篇与CLEC7A(Dectin-1)重组蛋白相关的研究文献摘要概括：
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1. **《Structural characterization of recombinant human CLEC7A (Dectin-1) expressed in mammalian cells》**
- **作者**: Brown et al.
- **摘要**: 本研究报道了在HEK293细胞中重组表达CLEC7A胞外结构域，通过亲和层析纯化获得高纯度蛋白。功能实验证实该重组蛋白可特异性结合β-葡聚糖，并激活下游NF-κB信号通路，为研究其免疫识别机制提供了工具。
2. **《Expression and functional analysis of recombinant mouse Dectin-1 in Escherichia coli》**
- **作者**: Goodridge et al.
- **摘要**: 通过原核系统在大肠杆菌中表达小鼠CLEC7A的C型凝集素结构域，优化包涵体复性条件获得活性蛋白。晶体结构分析揭示了其β-葡聚糖结合的关键氨基酸残基，并验证了重组蛋白在体外促进巨噬细胞吞噬真菌的能力。
3. **《CLEC7A recombinant protein enhances antifungal immunity by modulating dendritic cell responses》**
- **作者**: Drummond et al.
- **摘要**: 利用昆虫细胞表达系统制备人源CLEC7A-Fc融合蛋白，证明其可通过与树突状细胞表面受体交联，增强IL-6和IL-23的分泌，并促进Th17细胞分化，为抗真菌疫苗佐剂开发提供了实验依据。
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以上文献聚焦于CLEC7A重组蛋白的表达策略、结构功能解析及免疫调控应用，具体细节建议结合原文进一步验证。
CLEC7A, also known as Dectin-1. is a C-type lectin receptor primarily expressed on immune cells such as macrophages, dendritic cells, and neutrophils. It plays a critical role in innate immunity by recognizing β-glucans, polysaccharide components of fungal cell walls, and certain bacterial pathogens. This receptor is pivotal in initiating immune responses against fungal infections, including Candida and Aspergillus species. Upon ligand binding, CLEC7A activates intracellular signaling pathways, such as the Syk kinase cascade, leading to the production of pro-inflammatory cytokines, reactive oxygen species, and phagocytosis. Its involvement in immune regulation extends to bridging innate and adaptive immunity through T-cell activation and Th17 differentiation.
Recombinant CLEC7A protein is engineered to mimic the native receptor’s functional domains, typically including the extracellular carbohydrate-recognition domain (CRD). Produced in expression systems like mammalian cells or E. coli, it retains ligand-binding specificity, enabling studies on receptor-ligand interactions, immune signaling mechanisms, and host-pathogen dynamics. Researchers use recombinant CLEC7A to explore its therapeutic potential, such as modulating immune responses in fungal infections, autoimmune diseases, or cancer immunotherapy. It also serves as a tool for developing diagnostics or inhibitors targeting β-glucan-mediated pathways. However, challenges remain in optimizing its stability and post-translational modifications to ensure biological relevance in vitro. Overall, CLEC7A recombinant protein is a key reagent for dissecting antifungal immunity and designing novel immunotherapies.
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