Anti-mTLR5 Neutralizing mAb

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Murine TLR5 Neutralizing antibody (clone Q23D11) - Monoclonal Rat IgG2a

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2 x 100 µg

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Murine TLR5 Neutralizing antibody - Monoclonal Rat IgG2a

Neutralizing activity of Anti-mTLR5-IgG
Neutralizing activity of Anti-mTLR5-IgG

Anti-mTLR5-IgG (clone Q23D11) is a monoclonal antibody specific for murine Toll-like receptor 5 (mTLR5). This monoclonal antibody was produced in hybridoma cells and purified by affinity chromatography.

Anti-mTLR5-IgG has been selected for its ability to efficiently neutralize the biological activity of mTLR5. The neutralizing activity was determined using HEK-Blue™ TLR5 cells. 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.

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Key features:

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


Read our review Read our review on Toll-Like Receptors.



Evaluation of mTLR5 inhibition
Evaluation of mTLR5 inhibition

Anti-mTLR5-IgG is a potent neutralization antibody. Increasing concentrations of Anti-mTLR5-IgG were incubated for 30 minutes with RecFLA-ST (30 pg/ml) prior to the addition of HEK‑Blue™ mTLR5 cells. 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.

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Target: Murine TLR5 (mTLR5)

Specificity: No cross-reactivity with human TLR5

Clonality: Monoclonal antibody

Clone: Q23D11

Isotype: Rat IgG2a, kappa

Control: Rat Control IgG2a

Source: Hybridoma cells

Formulation: 0.2 µm filtered solution in a sodium phosphate buffer with saccharose, glycine, and stabilizing agents

Purity: Purified by affinity chromatography with protein G

Applications: Neutralization of murine TLR5-induced cellular activation. 

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.
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  • 2 x 100 µg of purified Anti-mTLR5 IgG monoclonal antibody, provided lyophilized.

room temperature Product is shipped at room temperature.

store Upon receipt, store at -20°C.

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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 AT. 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.

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