纯度 | >90%SDS-PAGE. |
种属 | Human |
靶点 | CLEC13A |
Uniprot No | Q8IX05 |
内毒素 | < 0.01EU/μg |
表达宿主 | E.coli |
表达区间 | 1-232aa |
氨基酸序列 | MLRAALPALLLPLLGLAAAAVADCPSSTWIQFQDSCYIFLQEAIKVESIEDVRNQCTDHGADMISIHNEEENAFILDTLKKQWKGPDDILLGMFYDTDDASFKWFDNSNMTFDKWTDQDDDEDLVDTCAFLHIKTGEWKKGNCEVSSVEGTLCKTAIPYKRKYLSDNHILISALVIASTVILTVLGAIIWFLYKKHSDSRFTTVFSTAPQSPYNEDCVLVVGEENEYPVQFD |
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CLEC13A(C型凝集素家族成员之一)重组蛋白的模拟参考文献示例(请注意,以下内容为基于领域知识的示例,非真实存在的文献,建议通过PubMed或SciFinder查询真实研究):
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1. **文献名称**: *"Recombinant CLEC13A binds to fungal β-glucans and modulates macrophage responses"*
**作者**: Smith J, et al.
**摘要**: 本研究利用哺乳动物表达系统成功表达并纯化CLEC13A重组蛋白,证实其通过C端凝集素结构域特异性识别真菌细胞壁β-葡聚糖,并增强巨噬细胞的吞噬活性和促炎因子释放。
2. **文献名称**: *"Structural characterization of human CLEC13A and its interaction with ligands"*
**作者**: Brown K, et al.
**摘要**: 通过X射线晶体学解析了CLEC13A胞外区的三维结构,发现其钙离子依赖的糖结合特性,重组蛋白实验显示其对高甘露糖结构具有低亲和力,提示其在病原体识别中的潜在作用。
3. **文献名称**: *"CLEC13A recombinant protein as a novel biomarker for dendritic cell activation in cancer"*
**作者**: Zhang L, et al.
**摘要**: 开发了基于CLEC13A重组蛋白的检测体系,证明其在树突状细胞活化过程中表达上调,并与肿瘤抗原呈递效率正相关,为癌症免疫治疗提供新靶点。
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**提示**:实际研究中,CLEC13A(亦称CD302)可能与免疫调节、病原体识别或肿瘤微环境相关。建议通过关键词 **"CLEC13A/CD302 recombinant protein"** 在以下平台检索真实文献:
- PubMed(https://pubmed.ncbi.nlm.nih.gov/)
- Google Scholar(https://scholar.google.com/)
CLEC13A (C-type lectin domain family 13 member A), also known as CD302 or DCL-1. is a type II transmembrane protein belonging to the C-type lectin receptor (CLR) family. It is primarily expressed on immune cells, including macrophages, dendritic cells, and neutrophils, and plays a role in pathogen recognition, immune regulation, and cellular interactions. Structurally, CLEC13A contains an extracellular C-type lectin-like domain (CTLD) that mediates carbohydrate-binding activity, though its calcium-dependent ligand specificity remains less defined compared to other CLRs. Unlike some lectins, CLEC13A lacks a canonical immunoreceptor tyrosine-based activation motif (ITAM), suggesting its signaling mechanisms may involve alternative adaptor proteins or collaborative receptor partnerships.
Recombinant CLEC13A protein is typically produced in mammalian or insect expression systems to ensure proper glycosylation and structural fidelity. It is often engineered with tags (e.g., Fc or His tags) for purification and detection. Research applications include studying receptor-ligand interactions, particularly with pathogen-associated molecules like β-glucans or endogenous glycoproteins. CLEC13A has garnered interest in immunology for its dual roles in promoting phagocytosis of microbial pathogens and modulating inflammatory responses. It is also explored in cancer research due to its altered expression in certain tumors and potential involvement in immune evasion. Additionally, recombinant CLEC13A serves as a tool to develop therapeutic antibodies or decoy receptors targeting immune dysregulation in autoimmune diseases or infections. Ongoing studies aim to clarify its endogenous ligands and downstream signaling pathways to unlock its full therapeutic potential.
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