Detects human TLR1 in direct ELISAs and Western blots. In direct ELISAs and Western blots, approximately 15% cross-reactivity with recombinant mouse (rm) TLR1 is observed and less than 5% cross-reactivity with recombinant human (rh) TLR3, rhTLR4, and rmTLR6 is observed.
Polyclonal Goat IgG
Mouse myeloma cell line NS0-derived recombinant human TLR1 Ser22-Asn578 Accession # AAC34137
Supplied in a saline solution containing BSA and Sodium Azide.
10 µL/106 cells
Please Note: Optimal dilutions should be determined by each laboratory for each application. General Protocols are available in the Technical Information section on our website.
Detection of TLR1 in Human Monocytes by Flow Cytometry. Human monocytes were stained with Goat Anti-Human TLR1 PE‑conjugated Antigen Affinity-purified Polyclonal Antibody (Catalog # FAB1484P, filled histogram) or isotype control antibody (Catalog # IC108P, open histogram). View our protocol for Staining Membrane-associated Proteins.
Preparation and Storage
The product is shipped with polar packs. Upon receipt, store it immediately at the temperature recommended below.
Stability & Storage
Protect from light. Do not freeze.
12 months from date of receipt, 2 to 8 °C as supplied.
The Toll-like family of molecules are type I transmembrane proteins that serve as pattern recognition receptors for microbial pathogens. There are at least eleven mouse and ten human TLRs that activate the innate immune system following exposure to a variety of microbial species (1, 2). TLRs contain a large number of leucine-rich repeats (LRRs) and a cytoplasmic tail with one Toll/IL-1 receptor (TIR) domain. Mature human TLR1 consists of a 556 amino acid (aa) extracellular domain (ECD) with 20 LRRs, a 21 aa transmembrane segment, and a 185 aa cytoplasmic domain (3, 4). Within the ECD, human TLR1 shares 63% aa sequence identity with human TLR6 and 20%‑43% aa sequence identitity with human TLR2, -3, -4, -5, -7, -8, -9, and -10. It shares 73% and 71% aa sequence identity with mouse and rat TLR1, respectively. TLR1 is expressed on the surface of macrophages, dendritic cells, and tonsillar epithelial cells in ligand-independent association with TLR2 (5‑8). TLR2 additionally associates with TLR6 to form a functional complex with specificity for distinct but related microbial ligands (9‑11). TLR1 and TLR2 cooperate in the recognition of bacterial and protozoal triacylated lipopeptides and glycosylphosphatidylinositols (6, 10‑12). Ligand binding induces TLR1 localization to lipid rafts followed by receptor internalization and activation of NF kappa B (7, 11, 13).
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