mProX™ Human TLR1 Stable Cell Line
- Product Category:
- Membrane Protein Stable Cell Lines
- Subcategory:
- Immune Checkpoint Cell Lines
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Published Data
Fig.1 Subcellular localization of OnTLR1 in 293T cells.
After the transfection, pcDNA3.1-GFP and pcDNA3.1-TLR1 were introduced into 293T cells. Subsequently, 24 hours later, the cells underwent fixation, and the staining of nuclei was accomplished using 4,6-diamidino-2-phenylindole (DAPI). The fusion protein was denoted by green fluorescence, while the nucleus was characterized by blue fluorescence.
Ref: Gao, Feng-Ying, et al. "TLR1 in Nile tilapia: The conserved receptor cannot interact with MyD88 and TIRAP but can activate NF-κB in vitro." Developmental & Comparative Immunology 127 (2022): 104300.
Pubmed: 34673140
DOI: 10.1016/j.dci.2021.104300
Research Highlights
Bang, Sunghee. et al. "A Cardiolipin from Muribaculum intestinale Induces Antigen-Specific Cytokine Responses." Journal of the American Chemical Society, 2023.
In the present study, a systematic phenotypic screen was conducted on the mouse gut microbiome to identify metabolites with immunomodulatory properties. Through this screen, a collection of immunomodulatory metabolites were identified and their effects were further investigated. The results of this study provide valuable insights into the potential use of gut microbiome-derived metabolites in modulating the immune system. Overall, this research contributes to the growing knowledge of the complex relationship between the gut microbiome and immune system.
Bang, Sunghee. et al. "A Cardiolipin from Muribaculum intestinale Induces Antigen-Specific Cytokine Responses." Journal of the American Chemical Society, 2023.
Pubmed:
37871232
DOI:
10.1021/jacs.3c09734
Jun Park, Beom. et al. "Multiple toll-like receptors (TLRs) display differential bacterial and ligand specificity in the earthworm, Eisenia andrei." Journal of invertebrate pathology, 2023.
The Toll-like receptors (TLRs) are a well-preserved and ancient group of pattern recognition receptors (PRRs) that recognize conserved pathogen-associated molecular patterns. These receptors consist of three domains: the extracellular N-terminal domain, which contains leucine-rich repeats (LRRs) responsible for the recognition and binding of antigens; the type-I transmembrane domain; and the intracellular Toll/Interleukin-1 receptor (TIR) domain, necessary for the downstream signaling pathway. In this study, six new full-length complementary DNA (cDNA) sequences, named Ean-TLR1/2/3/4/5/6, were identified. The deduced amino acid sequences revealed that Ean-TLRs contain a signal peptide, an LRR N-terminal domain (Ean-TLR4/5), varying numbers of LRRs, one (Ean-TLR1/2/3/4/5) or two (Ean-TLR6) LRR C-terminal domains, a type-I transmembrane domain, and a TIR domain. Further analysis showed that three conserved motifs, designated as Box 1, Box 2, and Box 3, contain essential amino acid residues for downstream signaling activity. Phylogenetic analysis of earthworm TLRs revealed two evolutionary branches, representing single (sccTLR) and multiple (mccTLR) cysteine cluster TLRs. Ean-TLR1/2/3/4 (sccTLR type) and Ean-TLR6 (mccTLR type) were clustered with previously reported earthworm TLRs, as well as TLRs from Clitellata and Polychaete. As pattern recognition receptors, earthworm TLRs are believed to have the ability to detect a wide range of pathogens. However, only Ean-TLR3 did not show any response to bacteria. In response to Gram-positive but not Gram-negative bacteria, the expression of earthworm TLRs was significantly increased, indicating the ability to differentiate between different species. The ligand specificity of earthworm TLRs suggests that their pathogen recognition is likely to be as diverse and specific as the mammalian TLR system.
Jun Park, Beom. et al. "Multiple toll-like receptors (TLRs) display differential bacterial and ligand specificity in the earthworm, Eisenia andrei." Journal of invertebrate pathology, 2023.
Pubmed:
37865158
DOI:
10.1016/j.jip.2023.108010