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  • mProX™ Human TLR1 Stable Cell Line

    [CAT#: S01YF-1023-PY207]
    Product Category:
    Membrane Protein Stable Cell Lines
    Subcategory:
    Immune Checkpoint Cell Lines

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    Product Information

    Target Family
    Immune Checkpoint
    Target Protein Species
    Human
    Host Cell Type
    HEK293;CHO-K1
    Target Classification
    Immune Checkpoint Cell Lines
    Target Research Area
    Infectious Research
    Related Diseases
    Leprosy 5; Rheumatoid Arthritis
    Gene ID
    Human:7096
    UniProt ID
    Human:Q15399

    Product Properties

    Biosafety Level
    Level 1
    Activity
    Yes
    Quantity
    10⁶ cells per vial
    Applications
    Toll-like receptor 1 (TLR1) plays a pivotal role in the innate immune system, recognizing microbial pathogens and initiating inflammatory responses. Recent studies have delved into the intricate mechanisms of TLR1 signaling pathways, revealing its significance in various diseases. For instance, TLR1 has been associated with the pathogenesis of infectious diseases, especially in recognizing bacterial lipoproteins, which are vital for mounting an effective immune response. Furthermore, TLR1 polymorphisms have been linked to susceptibility to infections, emphasizing its genetic influence on immune responses. With the increasing understanding of TLR1's role, potential therapeutic interventions targeting its pathways are being explored, offering promising avenues for treating infectious and inflammatory diseases.

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    FAQ

    chat Taylor Brown (Verified Customer)

    How does TLR1 contribute to the immune response against pathogens? Jun 15 2023

    chat Patrick Liam (Creative Biolabs Scientific Support)

    TLR1, in combination with TLR2, plays a crucial role in initiating proinflammatory responses against pathogens like Borrelia burgdorferi, which can be involved in diseases such as Lyme arthritis. Jun 15 2023

    chat Taylor Johnson (Verified Customer)

    Can TLR1 be targeted for therapeutic interventions in diseases? May 27 2020

    chat Patrick Liam (Creative Biolabs Scientific Support)

    Targeting TLR1, particularly its interaction with other TLRs, has potential in developing therapies for conditions like nasopharyngeal carcinoma, as it is involved in cell proliferation and immune responses. May 27 2020

    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

    Please note: All products are "FOR RESEARCH USE ONLY. NOT FOR USE IN DIAGNOSTIC OR CLINICAL PROCEDURES" For licensing inquiries, please contact
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