| 纯度 | >95%SDS-PAGE. |
| 种属 | Human |
| 靶点 | CLEC1A |
| Uniprot No | Q8NC01 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 22-280aa |
| 氨基酸序列 | LHSQGSATTR HPEPRRTEHR APSSTWRPVA LTLLTLCLVL LIGLAALGLL FFQYYQLSNT GQDTISQMEE RLGNTSQELQ SLQVQNIKLA GSLQHVAEKL CRELYNKAGA HRCSPCTEQW KWHGDNCYQF YKDSKSWEDC KYFCLSENST MLKINKQEDL EFAASQSYSE FFYSYWTGLL RPDSGKAWLW MDGTPFTSEL FHIIIDVTSP RSRDCVAILN GMIFSKDCKE LKRCVCERRA GMVKPESLHV PPETLGEGD |
| 预测分子量 | 52 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CLEC1A重组蛋白的3篇代表性文献摘要(注：文献为模拟示例，实际文献需通过学术数据库查询)：
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1. **文献名称**: *Structural Insights into CLEC1A Recognition of Pathogen-Associated Glycans*
**作者**: Smith A, et al.
**摘要**: 本研究解析了CLEC1A重组蛋白的晶体结构，揭示了其C型凝集素结构域特异性结合病原体表面甘露糖化多糖的分子机制，为开发靶向CLEC1A的免疫调节剂提供结构基础。
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2. **文献名称**: *CLEC1A Modulates Dendritic Cell Function in Antiviral Immunity*
**作者**: Tanaka K, et al.
**摘要**: 通过表达CLEC1A重组蛋白，研究发现其可增强树突状细胞对流感病毒的吞噬能力，并促进I型干扰素分泌，表明CLEC1A在抗病毒天然免疫中的关键作用。
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3. **文献名称**: *CLEC1A Recombinant Protein Suppresses Tumor Growth via NK Cell Activation*
**作者**: Chen L, et al.
**摘要**: 实验证明，CLEC1A重组蛋白通过结合自然杀伤细胞(NK)表面受体，激活细胞毒性信号通路，抑制小鼠黑色素瘤模型的肿瘤生长，提示其潜在抗癌应用价值。
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如需具体文献，建议在PubMed或Google Scholar中检索关键词“CLEC1A recombinant protein”或“CLEC1A function”。
CLEC1A (C-type lectin domain family 1 member A) is a transmembrane protein belonging to the C-type lectin receptor (CLR) family, which plays critical roles in immune recognition and response. It is characterized by a conserved carbohydrate-recognition domain (CRD) that binds specific glycan structures, enabling interactions with pathogens or endogenous ligands. CLEC1A is primarily expressed on immune cells, including dendritic cells and macrophages, suggesting its involvement in pathogen sensing, antigen presentation, and immune modulation. However, its precise biological functions and ligands remain less defined compared to other CLRs like Dectin-1 or DC-SIGN.
Recombinant CLEC1A protein is engineered to study its structure-function relationships, ligand specificity, and signaling mechanisms. Typically produced in mammalian expression systems (e.g., HEK293 cells), the recombinant protein retains the extracellular domain, often fused with tags (e.g., Fc or His-tag) for purification and detection. This tool enables in vitro binding assays, receptor-ligand interaction studies, and exploration of its role in immune pathways, such as NF-κB activation or cytokine production.
Research on CLEC1A has gained interest due to potential links to autoimmune diseases, cancer immunity, and infectious responses. For example, it may recognize fungal or viral glycans, triggering anti-pathogen immune responses. Conversely, aberrant CLEC1A signaling has been implicated in immune evasion by tumors. Despite progress, challenges persist in elucidating its physiological ligands and downstream signaling cascades. Recombinant CLEC1A serves as a vital reagent to address these gaps, offering insights into its therapeutic potential as a drug target or immunomodulatory agent. Ongoing studies aim to clarify its role in health and disease, bridging molecular biology with clinical applications.
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