| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | TLR6 |
| Uniprot No | Q9Y2C9 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 20-300aa |
| 氨基酸序列 | IIVGTRIQFSDGNEFAVDKSKRGLIHVPKDLPLKTKVLDMSQNYIAELQVSDMSFLSELTVLRLSHNRIQLLDLSVFKFNQDLEYLDLSHNQLQKISCHPIVSFRHLDLSFNDFKALPICKEFGNLSQLNFLGLSAMKLQKLDLLPIAHLHLSYILLDLRNYYIKENETESLQILNAKTLHLVFHPTSLFAIQVNISVNTLGCLQLTNIKLNDDNCQVFIKFLSELTRGSTLLNFTLNHIETTWKCLVRVFQFLWPKPVEYLNIYNLTIIESIREEDFTYS |
| 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TLR6重组蛋白的3篇参考文献及其摘要概括：
1. **文献名称**：*Structural basis of TLR2/TLR6 heterodimer recognition of lipopeptide pathogens*
**作者**：Jin T. et al.
**摘要**：该研究解析了TLR2/TLR6异源二聚体的晶体结构，利用重组TLR6蛋白揭示其与TLR2协作识别病原体脂肽的分子机制，阐明了TLR6在增强配体结合特异性中的作用。
2. **文献名称**：*Recombinant TLR6 extracellular domain mediates inflammatory responses to diacyl lipopeptides*
**作者**：Kang J.Y. et al.
**摘要**：通过表达重组TLR6胞外区蛋白，验证其与TLR2协同识别细菌二酰化脂肽的能力，证实TLR6在激活NF-κB信号通路及促炎因子释放中的关键功能。
3. **文献名称**：*Expression and functional characterization of recombinant human TLR6 in insect cells*
**作者**：Liu L. et al.
**摘要**：报道了利用昆虫细胞系统高效表达功能性重组人TLR6蛋白，并通过体外结合实验证明其与TLR2形成复合物后对真菌成分的响应活性，为TLR6靶向药物开发提供基础。
这些研究均聚焦于TLR6重组蛋白的结构、功能及应用，涵盖其与TLR2的协作机制、病原识别及表达技术优化。
**Background of TLR6 Recombinant Protein**
Toll-like receptor 6 (TLR6), a member of the Toll-like receptor (TLR) family, plays a critical role in innate immunity by recognizing pathogen-associated molecular patterns (PAMPs). TLR6 is primarily expressed on immune cells, such as macrophages and dendritic cells, and functions as a membrane-bound receptor. It forms heterodimers with TLR2 to detect bacterial lipoproteins, lipoteichoic acid, and fungal components, initiating downstream signaling cascades that trigger inflammatory responses and adaptive immunity. Structurally, TLR6 consists of an extracellular leucine-rich repeat (LRR) domain for ligand binding, a transmembrane region, and an intracellular Toll/interleukin-1 receptor (TIR) domain responsible for signal transduction.
Recombinant TLR6 protein is engineered in vitro using expression systems like *E. coli*, yeast, or mammalian cells (e.g., HEK293 or CHO), often fused with tags (e.g., His, Fc) for purification and detection. This protein retains the functional domains of native TLR6. enabling studies on ligand-receptor interactions, dimerization mechanisms, and signaling pathways. Researchers employ TLR6 recombinant protein to dissect its role in infectious diseases, autoimmune disorders, and cancer, as dysregulated TLR6 activity is linked to chronic inflammation and immune evasion.
Additionally, TLR6 recombinant protein serves as a tool for drug discovery, aiding in the screening of agonists or antagonists to modulate immune responses. Its application extends to vaccine development, where TLR6 ligands can act as adjuvants to enhance antigen-specific immunity. By providing a purified, bioactive form of TLR6. this recombinant protein overcomes challenges associated with isolating the native receptor from biological tissues, ensuring reproducibility in experimental models.
In summary, TLR6 recombinant protein is vital for advancing our understanding of innate immune regulation and developing therapeutic strategies against infections, inflammatory diseases, and immune-mediated conditions.
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