CL075 (3M002)

CL075 Unit size Cat. code Docs Qty Price
Thiazoloquinoline compound
500 µg
5 mg

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Activation of h/mTLR7 and hTLR8 by CL075 (3M002)
Activation of h/mTLR7 and hTLR8 by CL075 (3M002)

TLR7/8 Agonist - Thiazoquinoline compound

CL075 (3M002) is a thiazoloquinolone derivative that, like the base analog R848 (Resiquimod), induces differential TLR7 and/or TLR8 responses in human and murine immune cells. TLR7 and TLR8 are endosomal pattern recognition receptors that play an important role in the antiviral immune response.

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Mode of action:

CL075 was originally described as a human TLR8 (hTLR8) agonist because it triggers a potent NF-κB activation in hTLR8 reporter cells when compared to hTLR7 reporter cells [1].
In human peripheral blood mononuclear cells (PBMCs), CL075 induces the production of TNF-α and IL-12, and to a lesser extent IFN-α. This cytokine profile is similar to the one induced by the hTLR8 agonist ssRNA40 [1].
CL075 also induces the NF-κB-dependent production of pro-inflammatory cytokines [1]. CL075 efficiently stimulates cytokine production from monocytes and myeloid dendritic cells (DCs) among human PBMCs [1]. This compound has been used to optimize the ex vivo maturation of monocyte-derived DCs for developing DC-based anti-pathogen or anti-tumor vaccines [2].
Using our reporter cell lines HEK-Blue™ hTLR7, HEK-Blue™ hTLR8, HEK-Blue™ mTLR7, and HEK-Blue™ mTLR8, we established that CL075 is a TLR7/8 agonist. CL075 is ~10 times more potent for hTLR8 activation than for hTLR7. It also activates murine TLR7 (mTLR7), but not mTLR8. 


Key features of CL075:

  • Agonist of hTLR7 and hTLR8 with higher potency towards hTLR8
  • Agonist of mTLR7
  • Each lot of CL075 is highly pure (≥95%) and functionally tested


More infoRead our review about TLR7 and TLR8.



1. Gorden K.B. et al., 2005. Synthetic TLR agonists reveal functional differences between human TLR7 and TLR8. J. Immunol. 174(3):1259-68.
2. Spranger S. et al., 2010. Generation of Th1-polarizing dendritic cells using the TLR7/8 agonist CL075. J. Immunol. 185:738-747


Evaluation of CL075 in HEK-Blue™ TLR7 and HEK-Blue™ TLR8 cells
Evaluation of CL075 in HEK-Blue™ TLR7 and HEK-Blue™ TLR8 cells

CL075 induces a dose-dependent response in HEK-Blue™ TLR7 and HEK-Blue™ TLR8 cells. HEK-Blue™ hTLR7, HEK-Blue™ mTLR7, HEK-Blue™ hTLR8, and HEK-Blue™ mTLR8 cells were stimulated with increasing concentrations of CL075. After overnight incubation, CL075‑induced TLR7/TLR8 signaling was assessed by measuring the levels of SEAP using QUANTI‑Blue™ Solution and by reading the optical density (OD) at 630 nm.

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Specificity: human TLR7/8 and mouse TLR7 agonist

CAS number: 256922-53-9

Formula: C13H13N3S 

Molecular weight: 243.33 g/mol

Solubility: 1 mg/ml in water

Working Concentration:

  • 0.1 - 5 μg/ml CL075 for human TLR8 and mouse TLR7 in cell culture assays
  • 0.5 - 5 μg/ml CL075 for human TLR7 in cell culture assays

Quality control:

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CL075 is available in two quantities:


  • 500 µg CL075
  • 1.5 ml of endotoxin-free water


  • 5 mg CL075
  • 10 ml of  endotoxin-free water

room temperature CL075 is provided as a lyophilized powder and shipped at room temperature.

store Upon receipt, store at -20°C.


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TLR7 and TLR8:

TLR7 and TLR8 are endosomal pattern recognition receptors that share structural homology [1]. Both receptors are activated by single-stranded RNA (ssRNA) molecules, however, they exhibit different ligand-binding specificities and cellular expression patterns suggesting that they have nonredundant specialized roles.

TLR7 is essentially expressed by plasmacytoid dendritic cells (pDCs) but is also found in B cells and other myeloid cells [2] while TLR8 is highly expressed by myeloid cells and is absent from pDCs and B cells [2]. 

The endosomal distribution of TLR7 and TLR8 allows them to scan for the presence of microbial RNA in the phagocytic cargo. Their activation leads to NF-κB-, AP1-, and interferon regulatory factor (IRF)-mediated production of type I interferons (IFN-α/β) and pro-inflammatory cytokines [2].

Structural analyses have revealed that both TLR7 and TLR8 possess two binding sites (designated as Site 1 and Site 2) which do not share the same specificities.

Site 1 is highly conserved between TLR7 and TLR8 and binds nucleosides (guanosine (G) for TLR7 and uridine (U) for TLR8) or base analogs. The ligand preference for TLR7 and TLR8 is thus explained by the presence of specific residues in Site 1. Site 1 occupancy allows receptor dimerization and signaling.

Site 2 is less conserved and binds ssRNA with U(U) and U(G) motifs, respectively [3, 4]. Of note, ssRNA-binding to Site 2 is not sufficient for the formation of a signaling-competent TLR dimer but it strongly enhances the binding affinity of Site 1 [3, 4]. Thus, TLR7 and TLR8 appear to sense distinct RNA-degradation products rather than full-length ssRNAs [4].


1. Chuang T.H. & Ulevitch R.J., 2000. Cloning and characterization of a sub-family of human toll-like receptors: hTLR7, hTLR8, and hTLR9. Eur Cytokine Netw, 11:372-8.
2. Georg P. & Sander L.E., 2019. Innate sensors that regulate vaccine responses. Curr. Op. Immunol. 59:31.
3. Zhang Z. et al., 2018. Structural analyses of Toll-like receptor 7 reveal detailed RNA sequence specificity and recognition mechanism of agonistic ligands. Cell Rep. 25:3371.
4. Tanji H. et al., 2015. Toll-like receptor 8 senses degradation products of single-stranded RNA. Nat. Struct. Mol. Biol. 22:109.


Chemical structure of CL075:

Chemical structure of CL075

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