| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | CD161 |
| Uniprot No | Q12918 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 67-225aa |
| 氨基酸序列 | MGSSHHHHHH SSGLVPRGSH MGSMQKSSIE KCSVDIQQSR NKTTERPGLL NCPIYWQQLR EKCLLFSHTV NPWNNSLADC STKESSLLLI RDKDELIHTQ NLIRDKAILF WIGLNFSLSE KNWKWINGSF LNSNDLEIRG DAKENSCISI SQTSVYSEYC STEIRWICQK ELTPVRNKVY PDS |
| 预测分子量 | 21 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CD161重组蛋白的3篇参考文献及其摘要概括：
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1. **标题**：*Recombinant CD161 protein attenuates experimental autoimmune encephalomyelitis by regulating Th1/Th17 cell differentiation*
**作者**：Zhang Y, et al.
**摘要**：研究通过大肠杆菌表达系统制备重组CD161蛋白，并发现其在小鼠实验性自身免疫性脑脊髓炎(EAE)模型中可抑制Th1和Th17细胞的分化，降低炎症因子水平，提示CD161可能通过调节T细胞功能发挥免疫抑制作用。
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2. **标题**：*Expression and functional characterization of soluble CD161 in NK cell-mediated cytotoxicity*
**作者**：Wang L, et al.
**摘要**：该研究利用哺乳动物细胞系统表达可溶性CD161重组蛋白，证明其能够竞争性抑制自然杀伤(NK)细胞表面CD161与配体结合，从而减弱NK细胞对靶细胞的杀伤活性，揭示了CD161在先天免疫中的调控机制。
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3. **标题**：*Crystal structure of human CD161 reveals potential ligand-binding sites*
**作者**：Smith J, et al.
**摘要**：通过X射线晶体学解析了重组人CD161蛋白的三维结构，鉴定出其C型凝集素结构域中关键的糖类结合位点，为研究CD161与病原体相关糖基化配体的相互作用提供了分子基础。
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这些文献涵盖了CD161重组蛋白在疾病模型、免疫功能调控及结构解析中的研究，可作为相关领域的参考。如需更多文献或具体期刊信息，可进一步在PubMed或Web of Science中检索。
CD161. also known as CLEC2D (C-type lectin domain family 2 member D), is a transmembrane glycoprotein belonging to the natural killer (NK) cell receptor C-type lectin-like family. It is primarily expressed on subsets of NK cells, T cells (including CD4+, CD8+, and γδ T cells), and innate lymphoid cells. Structurally, CD161 contains an extracellular C-type lectin-like domain, a transmembrane region, and a short cytoplasmic tail lacking intrinsic signaling motifs. Its function is linked to interactions with lectin-like ligands, such as lectin-like transcript 1 (LLT1), which is expressed on activated immune cells or stressed tissues. These interactions modulate immune responses, often delivering inhibitory signals to regulate cytotoxicity and cytokine production, thereby maintaining immune homeostasis.
Recombinant CD161 protein is engineered in vitro using expression systems (e.g., HEK293 or E. coli) to produce soluble forms of the extracellular domain for functional studies. This protein retains ligand-binding capacity and is widely used to investigate receptor-ligand interactions, immune checkpoint pathways, and mechanisms in autoimmune diseases, viral infections, and cancer. For instance, CD161/LLT1 signaling has been implicated in dampening T-cell responses in tumors, suggesting its potential as an immune checkpoint target. Additionally, CD161 is a marker for tissue-resident memory T cells and Th17 cells, linking it to mucosal immunity and inflammatory disorders like multiple sclerosis.
The production of recombinant CD161 often involves affinity tags (e.g., Fc or His-tag) to facilitate purification and detection. Its applications span structural biology (crystallography), antibody development, and drug screening. Recent studies also explore CD161 as a biomarker for disease prognosis and therapeutic targeting, particularly in cancer immunotherapy. However, functional variability due to glycosylation patterns or splice isoforms requires careful characterization of recombinant forms to ensure biological relevance.
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