抗人 TLR1 抗体对
01AB01383
Toll like receptor 1 (TLR1) is a type I transmembrane glycoprotein characterized by an extracellular domain containing leucine-rich repeat (LRR) motifs, which are essential for recognizing pathogen-associated molecular patterns (PAMPs), and an intracellular toll/interleukin-1 receptor (TIR) domain that initiates downstream signaling cascades. TLR1 typically forms heterodimers with TLR2, enabling the recognition of triacylated lipopeptides from bacteria, and this interaction is crucial for the activation of innate immune responses, including the production of proinflammatory cytokines and the bridging of innate and adaptive immunity. Structurally, the LRR domains in TLR1's extracellular region are divided into N-terminal, central, and C-terminal subdomains, with the central region displaying notable variability and unique structural features such as extra alpha helices, which influence ligand binding. Dysfunction or genetic variation in TLR1 has been associated with altered susceptibility to infectious and inflammatory diseases, as impaired TLR1 signaling can compromise immune responses to specific bacterial components.
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技术参数
- 靶点基因名
- TLR1
- 基因别名
- KIAA0012
- 蛋白别名
- toll like receptor 1; TLR1
- UniProt
- Q15399
- 物种
- Human
产品详情
- 靶点名称
- TLR1
- 蛋白名称
- toll like receptor 1
- 蛋白别名
- Toll-like receptor 1; Toll/interleukin-1 receptor-like protein; TIL; CD antigen CD281
- 靶点基因名
- TLR1
- 基因别名
- KIAA0012
- UniProt
- Q15399
- 来源物种
- Homo sapiens (Human)
- 物种反应性
- Human
背景介绍
Toll like receptor 1 (TLR1) is a type I transmembrane glycoprotein characterized by an extracellular domain containing leucine-rich repeat (LRR) motifs, which are essential for recognizing pathogen-associated molecular patterns (PAMPs), and an intracellular toll/interleukin-1 receptor (TIR) domain that initiates downstream signaling cascades. TLR1 typically forms heterodimers with TLR2, enabling the recognition of triacylated lipopeptides from bacteria, and this interaction is crucial for the activation of innate immune responses, including the production of proinflammatory cytokines and the bridging of innate and adaptive immunity. Structurally, the LRR domains in TLR1's extracellular region are divided into N-terminal, central, and C-terminal subdomains, with the central region displaying notable variability and unique structural features such as extra alpha helices, which influence ligand binding. Dysfunction or genetic variation in TLR1 has been associated with altered susceptibility to infectious and inflammatory diseases, as impaired TLR1 signaling can compromise immune responses to specific bacterial components.