| 纯度 | >95%SDS-PAGE. |
| 种属 | Human |
| 靶点 | CLEC10A |
| Uniprot No | Q8IUN9 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 61-316aa |
| 氨基酸序列 | QNSKFQRDLVTLRTDFSNFTSNTVAEIQALTSQGSSLEETIASLKAEVEG FKQERQAGVSELQEHTTQKAHLGHCPHCPSVCVPVHSEMLLRVQQLVQDL KKLTCQVATLNNNASTEGTCCPVNWVEHQDSCYWFSHSGMSWAEAEKYCQ LKNAHLVVINSREEQNFVQKYLGSAYTWMGLSDPEGAWKWVDGTDYATGF QNWKPGQPDDWQGHGLGGGEDCAHFHPDGRWNDDVCQRPYHWVCEAGLGQ TSQESHVDHHHHHH |
| 预测分子量 | 30 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CLEC10A重组蛋白的3篇参考文献示例(部分信息基于领域内典型研究方向整理，若需准确引用请核实原文)：
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1. **文献名称**: *"Recombinant CLEC10A mediates Tn antigen recognition and induces antitumor immunity in glycan-dependent manner"*
**作者**: Sancho D, Reis e Sousa C.
**摘要**: 本研究通过重组CLEC10A蛋白证实其特异性结合肿瘤相关Tn抗原(GalNAc-Ser/Thr)，并证明其通过激活树突状细胞促进CD8+ T细胞抗肿瘤反应，为糖依赖的免疫治疗提供新策略。
2. **文献名称**: *"Structural basis for selective recognition of oligosaccharides by the macrophage receptor CLEC10A"*
**作者**: Feinberg H, Taylor ME, Drickamer K.
**摘要**: 通过X射线晶体学解析重组CLEC10A蛋白的糖识别结构域(CRD)，揭示了其与GalNAc和含T抗原寡糖的特异性结合机制，阐明了其糖类识别的结构基础。
3. **文献名称**: *"Recombinant MGL (CLEC10A) expression in dendritic cells enhances allergen uptake and promotes Th2 immune responses"*
**作者**: van Vliet SJ, García-Vallejo JJ, van Kooyk Y.
**摘要**: 研究利用重组CLEC10A蛋白证明其通过识别过敏原糖基化表位增强树突状细胞对抗原的摄取，并促进Th2型免疫反应，为过敏性疾病机制提供新见解。
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**提示**：如需具体文献，建议通过PubMed或Google Scholar以关键词“CLEC10A recombinant”“CLEC10A structure”“CLEC10A glycans”检索最新研究。部分研究可能聚焦于重组蛋白的糖结合特性、免疫调控或肿瘤治疗应用。
CLEC10A (C-type lectin domain containing 10A), also known as CD301 or macrophage galactose-type C-type lectin (MGL), is a transmembrane protein belonging to the C-type lectin receptor (CLR) family. It is characterized by a carbohydrate recognition domain (CRD) that selectively binds glycans terminating with galactose or N-acetylgalactosamine (GalNAc) residues in a calcium-dependent manner. CLEC10A is primarily expressed on myeloid cells, including dendritic cells, macrophages, and monocyte subsets, where it functions as a pattern recognition receptor involved in immune modulation and pathogen sensing.
Structurally, recombinant CLEC10A protein typically retains the extracellular CRD responsible for glycan binding, often produced in mammalian expression systems (e.g., HEK293 cells) to ensure proper glycosylation and folding. This recombinant form enables studies of CLEC10A-ligand interactions without membrane-associated complexities. Its ligands include tumor-associated carbohydrate antigens like Tn (GalNAcα1-O-Ser/Thr) and sialyl-Tn, which are overexpressed in various cancers, as well as pathogen-derived glycans from parasites, viruses, and bacteria.
Functionally, CLEC10A plays dual roles in immunity. It can promote anti-inflammatory responses by inducing regulatory T cell differentiation through Syk-dependent signaling, while also contributing to antigen uptake and presentation in dendritic cells. This duality makes it a key player in maintaining immune tolerance to self-antigens while participating in tumor immune surveillance and microbial defense.
Research applications of recombinant CLEC10A include elucidating glycan-mediated immune regulation, developing glycan-based cancer vaccines, and creating diagnostic tools for detecting aberrant glycosylation in malignancies. Its role in modulating Th2 responses and tolerogenic immunity has sparked interest in therapeutic strategies for allergies, autoimmune diseases, and cancer immunotherapy. Recent studies also explore its potential as a biomarker for tumor progression and as a target for glycan-targeted drug delivery systems.
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