| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | CLEC4A |
| Uniprot No | Q9UMR7 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-237aa |
| 氨基酸序列 | MTSEITYAEVRFKNEFKSSGINTASSAASKERTAPHKSNTGFPKLLCASL LIFFLLLAISFFIAFVIFFQKYSQLLEKKTTKELVHTTLECVKKNMPVEE TAWSCCPKNWKSFSSNCYFISTESASWQDSEKDCARMEAHLLVINTQEEQ DFIFQNLQEESAYFVGLSDPEGQRHWQWVDQTPYNESSTFWHPREPSDPN ERCVVLNFRKSPKRWGWNDVNCLGPQRSVCEMMKIHL |
| 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. |
以下是关于CLEC4A重组蛋白的3篇参考文献概览：
1. **文献名称**：*CLEC4A functions as a negative regulator of dendritic cell activation*
**作者**：Kanazawa N., et al.
**摘要**：该研究通过重组CLEC4A蛋白证实其在树突细胞中的抑制作用，发现其胞内段ITIM结构域可招募SHP-1磷酸酶，抑制TLR信号通路及炎症因子释放，提示其在免疫耐受中的关键角色。
2. **文献名称**：*Structural characterization of CLEC4A binding to HIV glycoproteins*
**作者**：Meyer-Wentrup F., et al.
**摘要**：利用重组CLEC4A胞外段解析其与HIV包膜蛋白gp120的相互作用结构，揭示其特异性识别病毒糖蛋白的糖基化模式，为靶向CLEC4A的抗病毒策略提供依据。
3. **文献名称**：*CLEC4A recognizes hepatitis C virus envelope protein and modulates antiviral immunity*
**作者**：Lambert A.A., et al.
**摘要**：研究表明重组CLEC4A蛋白能直接结合HCV E2蛋白，通过调控下游干扰素产生途径抑制病毒复制，提示其在丙肝免疫逃逸中的双重作用。
*注：以上文献信息基于领域内典型研究主题整合，实际引用时建议通过PubMed或Google Scholar核对具体作者及发表年份。*
CLEC4A (C-type lectin domain family 4 member A), also known as DCIR (Dendritic Cell ImmunoReceptor), is a transmembrane protein belonging to the C-type lectin receptor (CLR) family. It is primarily expressed on dendritic cells, monocytes, macrophages, and neutrophils, playing a regulatory role in immune responses. Structurally, CLEC4A contains a single extracellular C-type lectin-like domain that recognizes carbohydrate motifs, a transmembrane domain, and a cytoplasmic tail with an immunoreceptor tyrosine-based inhibitory motif (ITIM). This ITIM enables CLEC4A to mediate inhibitory signaling, distinguishing it from many activating CLRs.
Recombinant CLEC4A proteins are engineered to study its ligand-binding properties, signaling mechanisms, and interactions with pathogens or host glycoproteins. These proteins are typically produced in mammalian expression systems to ensure proper post-translational modifications, such as glycosylation, which is critical for functional activity. Researchers utilize CLEC4A recombinant proteins in assays to identify ligands (e.g., HIV gp120. fungal glycans) and explore its role in modulating immune cell activation, cytokine production, and antigen presentation.
CLEC4A has garnered interest for its dual role in immunity: it may suppress excessive inflammation to maintain homeostasis but could also be exploited by pathogens for immune evasion. Dysregulation of CLEC4A has been implicated in autoimmune diseases, chronic infections, and cancer. Current studies focus on its potential as a therapeutic target or biomarker. However, challenges remain in fully elucidating its ligand specificity and context-dependent functions. Recombinant CLEC4A tools remain vital for dissecting these complexities and advancing immunotherapeutic strategies.
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