| 纯度 | >95%SDS-PAGE. |
| 种属 | Human |
| 靶点 | CLEC4E |
| Uniprot No | Q9ULY5 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 41-219aa |
| 氨基酸序列 | RCVVTFRIFQTCDEKKFQLPENFTELSCYNYGSGSVKNCCPLNWEYFQSS CYFFSTDTISWALSLKNCSAMGAHLVVINSQEEQEFLSYKKPKMREFFIG LSDQVVEGQWQWVDGTPLTKSLSFWDVGEPNNIATLEDCATMRDSSNPRQ NWNDVTCFLNYFRICEMVGINPLNKGKSLVDHHHHHH |
| 预测分子量 | 22 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篇关于CLEC4E(Mincle)重组蛋白的经典文献摘要概览：
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1. **文献名称**：*C-type lectin Mincle is an activating receptor for pathogenic fungus*
**作者**：Yamasaki S, et al.
**摘要**：本研究首次成功表达并纯化CLEC4E(Mincle)重组蛋白，发现其特异性识别真菌细胞壁成分α-mannose，并通过与Syk激酶偶联的信号通路激活巨噬细胞的炎症反应，揭示了其在先天免疫中的关键作用。(*Immunity*, 2008)
2. **文献名称**：*Direct recognition of the mycobacterial glycolipid trehalose dimycolate by C-type lectin Mincle*
**作者**：Ishikawa E, et al.
**摘要**：通过重组CLEC4E蛋白的体外结合实验，证实其直接结合结核分枝杆菌的糖脂分子TDM(海藻糖二分枝菌酸酯)，并触发NF-κB通路，为CLEC4E在结核病免疫中的作用机制提供证据。(*Nature Immunology*, 2009)
3. **文献名称**：*Structural basis for ligand recognition by the activating C-type lectin receptor Mincle*
**作者**：Furukawa A, et al.
**摘要**：利用重组CLEC4E蛋白的晶体结构解析，揭示其糖识别结构域(CRD)与配体(如TDM)结合的分子机制，阐明关键氨基酸残基在病原体识别中的功能。(*Journal of Biological Chemistry*, 2013)
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**注**：以上文献为CLEC4E功能与结构的经典研究，近年研究可进一步通过PubMed等数据库以“CLEC4E recombinant”为关键词检索获取。
CLEC4E (C-type lectin domain family 4 member E), also known as Clec4e or Mincle (Macrophage-inducible C-type lectin), is a pattern recognition receptor belonging to the C-type lectin receptor (CLR) family. It is primarily expressed on innate immune cells such as macrophages, dendritic cells, and neutrophils. Discovered in the late 1990s, CLEC4E gained attention for its role in detecting pathogen-associated molecular patterns (PAMPs) and damage-associated molecular patterns (DAMPs). It specifically recognizes glycolipids like trehalose dimycolate (TDM) from Mycobacterium tuberculosis and α-mannosyl residues on fungal pathogens, making it critical in antimicrobial immunity.
CLEC4E functions by forming a signaling complex with the Fc receptor γ-chain, activating Syk kinase and downstream NF-κB pathways to trigger pro-inflammatory cytokine production. Beyond infections, it contributes to sterile inflammation by sensing cellular debris, such as SAP130 released during necrosis. Its dual role in pathogen defense and tissue injury response links it to autoimmune diseases, cancer, and vaccine adjuvant research.
Recombinant CLEC4E protein, typically produced in mammalian (e.g., HEK293) or insect expression systems to preserve post-translational modifications, enables structural and functional studies. Purified variants often include tags (e.g., Fc or His-tag) for binding assays, crystallography, or inhibitor screening. Research applications include elucidating ligand interactions, developing immunotherapies, and exploring its modulation in inflammatory disorders. As a therapeutic target, CLEC4E modulation holds potential in balancing antimicrobial responses and controlling inflammation-driven pathologies. Current challenges involve understanding its tissue-specific regulation and crosstalk with other CLRs in immune networks.
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