Reactivity | MuSpecies Glossary |
Applications | Bioactivity |
Format | Carrier-Free |
Details of Functionality | Measured by its ability to inhibit Flagellin-induced IL-8 secretion in HT‑29 human colon adenocarcinoma cells. The ED50 for this effect is 4-24 ng/mL |
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Source | Chinese Hamster Ovary cell line, CHO-derived mouse TLR5 protein
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Accession # | |||||||
N-terminal Sequence | Ile21 |
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Structure / Form | Disulfide-linked homodimer |
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Protein/Peptide Type | Recombinant Proteins |
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Gene | Tlr5 |
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Purity | >95%, by SDS-PAGE under reducing conditions and visualized by silver stain |
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Endotoxin Note | <0.01 EU per 1 μg of the protein by the LAL method. |
Dilutions |
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Theoretical MW | 97.3 kDa (monomer). Disclaimer note: The observed molecular weight of the protein may vary from the listed predicted molecular weight due to post translational modifications, post translation cleavages, relative charges, and other experimental factors. |
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SDS-PAGE | 100-125 kDa, reducing conditions |
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Publications |
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Storage | Use a manual defrost freezer and avoid repeated freeze-thaw cycles.
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Buffer | Lyophilized from a 0.2 μm filtered solution in PBS. |
Purity | >95%, by SDS-PAGE under reducing conditions and visualized by silver stain |
Reconstitution Instructions | Reconstitute at 100 μg/mL in PBS. |
TLR5 (Toll-like receptor 5) is an approximately 100 kDa cell surface type I transmembrane glycoprotein of the TLR family of pathogen‑associated molecular pattern (PAMP) receptors (1‑3). TLR5 recognizes flagellins, proteins found on flagella of both gram‑positive and gram‑negative pathogenic bacteria (2, 3). The 859 amino acid (aa) mouse TLR5 precursor includes a 21 aa signal sequence, a 621 aa extracellular domain (ECD) with 9 potential N‑glycosylation sites and 16 leucine‑rich repeats (LRR) that contain the flagellin‑binding site, a transmembrane domain, and a 197 aa cytoplasmic region with a TIR (Toll/ IL-1 R) domain (1, 4). The mouse TLR5 ECD shares 84% aa sequence identity with rat and 69‑73% with human, feline, porcine and bovine TLR5. TLR5 is expressed on mucosal epithelia in the gastrointestinal tract, airways, and other areas of potential contact with bacteria, and on alveolar macrophages, monocytes, neutrophils, CD4+ T lymphocytes, and dendritic cell subsets (3‑7). In some portions of the intestine, epithelial TLR5 is expressed only on the basolateral surface (3, 4). Flagellin engagement induces signaling via direct interaction of TLR5 with MyD88, which activates NFkB and stimulates production of inflammatory cytokines such as TNF‑ alpha , IL‑1 beta , IL‑6 and IL‑8, depending on the cell type (2‑6, 8, 9). TLR5 allows recognition of pathogenic bacteria such as Pseudomonas, Salmonella and Listeria, without reaction to non‑flagellated commensal bacteria (3, 4). It stimulates massive neutrophil recruitment and EGF R‑mediated mucus production by airway epithelia (4, 9, 10). It promotes Th2 polarization and IgA secretion, and restrains local regulatory T cell generation (4, 7). Deletion of mouse TLR5 promotes colitis, probably due to TLR4‑mediated inappropriate responses to commensal bacteria (11).
Toll-like receptors in the intestinal epithelial cells By Jamshed Arslan, Pharm. D., PhD. Toll-like receptors (TLRs) are microbe-sensing proteins that act as first responders to danger signals. TLRs help the intestinal epithelial cells (IECs) recognize commensal bacteria ... Read full blog post. |
The role of TLR4 in breast cancer Toll like receptors (TLRs) are highly conserved proteins that are first known for their role in pathogen recognition and immune response activation. In order to elicit the necessary immune response in reaction to a foreign pathogen, TLRs trigger cy... Read full blog post. |
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