| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | TLR1 |
| Uniprot No | Q15399 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 25-580aa |
| 氨基酸序列 | SEFLVDRSKNGLIHVPKDLSQKTTILNISQNYISELWTSDILSLSKLRILIISHNRIQYLDISVFKFNQELEYLDLSHNKLVKISCHPTVNLKHLDLSFNAFDALPICKEFGNMSQLKFLGLSTTHLEKSSVLPIAHLNISKVLLVLGETYGEKEDPEGLQDFNTESLHIVFPTNKEFHFILDVSVKTVANLELSNIKCVLEDNKCSYFLSILAKLQTNPKLSNLTLNNIETTWNSFIRILQLVWHTTVWYFSISNVKLQGQLDFRDFDYSGTSLKALSIHQVVSDVFGFPQSYIYEIFSNMNIKNFTVSGTRMVHMLCPSKISPFLHLDFSNNLLTDTVFENCGHLTELETLILQMNQLKELSKIAEMTTQMKSLQQLDISQNSVSYDEKKGDCSWTKSLLSLNMSSNILTDTIFRCLPPRIKVLDLHSNKIKSIPKQVVKLEALQELNVAFNSLTDLPGCGSFSSLSVLIIDHNSVSHPSADFFQSCQKMRSIKAGDNPFQCTCELGEFVKNIDQVSSEVLEGWPDSYKCDYPESYRGTLLKDFHMSELSCNIT |
| 预测分子量 | 65.2kDa |
| 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TLR1重组蛋白的3篇参考文献及其简要摘要：
1. **文献名称**：*Structural basis of TLR1/TLR2 heterodimerization and signaling*
**作者**：Jin, M.S., Kim, S.E., Heo, J.Y., et al.
**摘要**：该研究通过X射线晶体学解析了TLR1和TLR2重组蛋白形成的异源二聚体结构，揭示了其识别细菌脂蛋白(如Triacyl lipopeptides)的分子机制，并阐明了其在先天免疫信号转导中的关键作用。
2. **文献名称**：*Expression and functional analysis of recombinant TLR1 in ligand recognition*
**作者**：Omueti, K.O., Mazur, D.J., Thompson, K.S., et al.
**摘要**：研究通过哺乳动物细胞系统表达了重组TLR1蛋白，发现其与TLR2协同作用可增强对病原体相关分子模式(PAMPs)的识别能力，并证实TLR1的胞外域结构对配体特异性结合至关重要。
3. **文献名称**：*TLR1 polymorphisms and recombinant protein activity in modulating immune responses*
**作者**：Barclay, W., Shin, H., Fiorini, R.N., et al.
**摘要**：本文探讨了TLR1基因多态性对其重组蛋白功能的影响，发现某些单核苷酸多态性(SNPs)会改变TLR1重组蛋白的配体结合效率，进而影响下游炎症因子(如TNF-α、IL-6)的产生。
这些研究涵盖了TLR1重组蛋白的结构解析、功能验证及其在免疫调控中的机制，可作为相关领域的核心参考文献。
Toll-like receptor 1 (TLR1) is a transmembrane protein belonging to the Toll-like receptor family, a key component of the innate immune system. It plays a critical role in recognizing pathogen-associated molecular patterns (PAMPs), particularly bacterial lipoproteins, by forming heterodimers with TLR2. This interaction enables the detection of conserved microbial structures, triggering downstream signaling cascades that activate immune responses, including the production of pro-inflammatory cytokines and chemokines.
Recombinant TLR1 proteins are engineered versions of the native receptor, typically produced in vitro using expression systems such as mammalian cells (e.g., HEK293) or insect cells (e.g., baculovirus systems). These systems allow for proper post-translational modifications, ensuring functional similarity to the natural protein. The recombinant protein often includes specific domains, such as the extracellular leucine-rich repeat (LRR) region responsible for ligand binding, or the transmembrane and cytoplasmic Toll/interleukin-1 receptor (TIR) domain involved in signal transduction.
Research on TLR1 recombinant proteins has been pivotal in elucidating structural mechanisms of pathogen recognition, ligand specificity, and receptor dimerization. For instance, studies using purified TLR1/TLR2 complexes have revealed how these receptors discriminate between tri-acylated and di-acylated lipopeptides from Gram-positive and Gram-negative bacteria. Additionally, recombinant TLR1 serves as a tool for developing therapeutic agents, such as vaccine adjuvants or inhibitors targeting excessive inflammation in autoimmune diseases.
Challenges in working with TLR1 include its dependence on TLR2 for functional activity and the need for proper membrane localization in experimental setups. Despite this, recombinant TLR1 remains a valuable resource for advancing immunotherapy, infectious disease research, and understanding immune dysregulation in conditions like sepsis or chronic inflammation. Its applications extend to drug screening platforms and diagnostic assays aimed at modulating innate immune responses.
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