Anti-hTLR5 Detection and Neutralizing mAb

Human TLR5 Detection and Neutralizing Antibody - Monoclonal Human IgA2

Neutralizing activity of Anti-hTLR5-IgA

Anti-hTLR5-IgA (clone Q2G4) is a chimeric monoclonal antibody specific for human Toll-like receptor 5 (hTLR5). This antibody was generated by combining the constant domains of the human IgA molecule with the murine variable regions. It was produced in Chinese hamster ovary (CHO) cells and purified by affinity chromatography.

Anti-hTLR5-IgA has been selected for its ability to efficiently neutralize the biological activity of hTLR5. The neutralizing activity was determined using HEK-Blue™ TLR5 cells. This antibody can also be used to detect hTLR5 using flow cytometry. TLR5 recognizes flagellin from Gram-positive and Gram-negative bacteria. Activation of the receptor stimulates the production of proinflammatory cytokines through signaling via the adaptor protein MyD88.

More details

Key features:

• Reacts with human TLR5
• Provided azide-free
• Each lot is functionally tested

Read our review on Toll-Like Receptors.

Figures

Anti-hTLR5-IgA2 is a potent neutralization antibody. Increasing concentrations of Anti-hTLR5-IgA2 were incubated for 1 hour with HEK‑Blue™ hTLR5 cells prior to the addition of FLA-ST Ultrapure (1 ng/ml). After overnight incubation, secreted embryonic alkaline phosphatase (SEAP) activity in the cell culture supernatant was assessed using QUANTI-Blue™ Solution. Data are shown in percentage (%) of neutralization (mean ± SEM).

Specifications

Target: Human TLR5 (hTLR5)

Specificity: No cross-reactivity with murine TLR5

Clonality: Monoclonal antibody

Clone: Q2G4

Isotype: Human IgA2, kappa

Control: Human IgA2 Control

Source: CHO cells

Formulation: 0.2 μm filtered solution in TRIS with glycine, saccharose, and stabilizing agents

Applications: Neutralizing hTLR5-induced cellular activation. This antibody can also be used for detection using flow cytometry

Quality control:

• This product has been validated for neutralization using cellular assays.
• The absence of bacterial contamination (e.g. lipoproteins and endotoxins) has been confirmed using HEK-Blue™ TLR2 and HEK‑Blue™ TLR4 cells.

Contents

• 2 x 100 μg purified anti-hTLR5-IgA antibody, provided azide-free and lyophilized.

Product is shipped at room temperature.

Upon receipt, store lyophilized antibody at -20°C.

Details

Toll-like receptors (TLRs) play a critical role in early innate immunity to invading pathogens by sensing microorganisms. These evolutionarily conserved receptors recognize highly conserved structural motifs only expressed by microbial pathogens, called pathogen-associated microbial patterns (PAMPs). Stimulation of TLRs by PAMPs initiates a signaling cascade leading to the secretion of proinflammatory cytokines following NF-κB activation. To date ten human and twelve murine TLRs have been characterized, TLR1 to TLR10 in humans, and TLR1 to TLR9, TLR11, TLR12, and TLR13 in mice, the homolog of TLR10 being a pseudogene.

TLR5 recognizes flagellin from both Gram-positive and Gram-negative bacteria. Activation of the receptor stimulates the production of proinflammatory cytokines, such as TNF-α, through signaling via the adaptor protein MyD88 and the serine kinase IRAK [1-3]. TLR5 can generate a pro-inflammatory signal as a homodimer suggesting that it might be the only TLR participating in flagellin recognition [3]. However, TLR5 may require the presence of a co-receptor or adaptor molecule for efficient ligand recognition and/or signaling [4].

1. Yang J. & Yan H. 2017. TLR5: beyond the recognition of flagellin.Cell Mol Immunol. 14(12):1017-1019.
2. Gewirtz A.T. et al., 2001. Cutting edge: bacterial flagellin activates basolaterally expressed TLR5 to induce epithelial proinflammatory gene expression. J Immunol, 167(4):1882-5.
3. Hayashi F. et al., 2001. The innate immune response to bacterial flagellin is mediated by Toll-like receptor 5. Nature, 410(6832):1099-103.
4. Tallant T. et al., 2004. Flagellin acting via TLR5 is the major activator of key signaling pathways leading to NF-kappa B and proinflammatory gene program activation in intestinal epithelial cells. BMC Microbiol. 4(1):33.