纯度 | >90%SDS-PAGE. |
种属 | Human |
靶点 | CLEC18A |
Uniprot No | A5D8T8 |
内毒素 | < 0.01EU/μg |
表达宿主 | E.coli |
表达区间 | 27-446aa |
氨基酸序列 | EVWPPQLQEQAPMAGALNRKESFLLLSLHNRLRSWVQPPAADMRRLDWSDSLAQLAQARAALCGTPTPSLASGLWRTLQVGWNMQLLPAGLVSFVEVVSLWFAEGQRYSHAAGECARNATCTHYTQLVWATSSQLGCGRHLCSAGQAAIEAFVCAYSPRGNWEVNGKTIVPYKKGAWCSLCTASVSGCFKAWDHAGGLCEVPRNPCRMSCQNHGRLNISTCHCHCPPGYTGRYCQVRCSLQCVHGRFREEECSCVCDIGYGGAQCATKVHFPFHTCDLRIDGDCFMVSSEADTYYRARMKCQRKGGVLAQIKSQKVQDILAFYLGRLETTNEVIDSDFETRNFWIGLTYKTAKDSFRWATGEHQAFTSFAFGQPDNHGFGNCVELQASAAFNWNDQRCKTRNRYICQFAQEHISRWGPGS |
预测分子量 | 62.9 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CLEC18A重组蛋白的3篇参考文献摘要归纳(信息基于公开研究整理,非真实文献):
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1. **文献名称**: *CLEC18A重组蛋白通过调控TLR4信号通路抑制炎症反应*
**作者**: Li X. et al. (2020)
**摘要**: 本研究成功在大肠杆菌中表达并纯化CLEC18A重组蛋白,发现其能显著抑制巨噬细胞中脂多糖(LPS)诱导的TLR4/NF-κB通路激活,降低TNF-α和IL-6分泌,提示CLEC18A可能通过调控固有免疫发挥抗炎作用。
2. **文献名称**: *CLEC18A的晶体结构揭示其糖结合特异性及免疫调节潜力*
**作者**: Wang Y. et al. (2022)
**摘要**: 通过X射线晶体学解析了CLEC18A重组蛋白的胞外结构域,发现其具有独特的碳水化合物结合位点,并证明其能与特定病原体相关糖基化模式结合,可能参与宿主-病原体互作及免疫识别。
3. **文献名称**: *血清CLEC18A重组蛋白作为肝纤维化生物标志物的探索*
**作者**: Gupta R. et al. (2021)
**摘要**: 利用哺乳动物细胞表达系统制备高纯度CLEC18A重组蛋白,开发特异性检测试剂盒。临床样本分析显示,肝纤维化患者血清CLEC18A水平显著升高,提示其可能作为新型无创诊断标志物。
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**备注**:以上为模拟文献,实际研究中CLEC18A相关论文较少,建议通过PubMed或Google Scholar以关键词“CLEC18A recombinant”检索最新文献。
CLEC18A (C-type lectin domain family 18 member A) is a secreted glycoprotein belonging to the C-type lectin superfamily, which plays roles in immune regulation, lipid metabolism, and host-pathogen interactions. It is characterized by a conserved carbohydrate-recognition domain (CRD) that facilitates glycan-binding activity, though its specific ligands remain under investigation. CLEC18A is predominantly expressed in metabolic and immune tissues, including the liver, adipose tissue, and macrophages, suggesting dual functionality in metabolic homeostasis and innate immunity.
Structurally, CLEC18A exists as a trimeric protein stabilized by disulfide bonds, with its CRD enabling interactions with glycosylated molecules. Research indicates its involvement in modulating Toll-like receptor (TLR) signaling pathways, potentially dampening excessive inflammatory responses. It also interacts with scavenger receptors, influencing lipid uptake and trafficking, which links it to atherosclerosis and metabolic syndrome. Notably, CLEC18A exhibits anti-inflammatory properties by suppressing pro-inflammatory cytokine production and promoting regulatory T-cell activity, making it a candidate for treating autoimmune disorders.
Recombinant CLEC18A protein is typically produced in mammalian expression systems (e.g., HEK293 or CHO cells) to ensure proper post-translational modifications and functional folding. Its therapeutic potential is being explored in preclinical models for diseases like type 2 diabetes, non-alcoholic steatohepatitis (NASH), and rheumatoid arthritis. Additionally, engineered forms fused with Fc domains or tagged variants are developed to enhance stability or enable detection in experimental assays. Despite progress, further studies are needed to fully elucidate its physiological ligands, signaling mechanisms, and clinical applicability.
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