TLR2-TLR1 & TLR2-TLR6 agonists
Toll-like receptor 2 (TLR2) plays an essential role in detecting a diverse range of microbial pathogen-associated molecular patterns (PAMPs) such as bacterial lipoproteins [1]. TLR2 alone can not activate downstream signaling and thus, forms a functional heterodimer at the cell surface with either TLR1 or TLR6 [1]. The TLR2‑TLR6 and TLR2‑TLR1 heterodimers are known to bind specific bacterial lipoproteins depending on whether they are di- or triacylated, respectively [2, 3]. Synthetic ‘mimics’ of di- or triacylated lipoproteins, such as FSL-1 and Pam3CSK4 are commonly used to activate and study TLR2-dependent signaling and immune responses.
Importantly, the activation of TLR2-TLR1 and TLR2-TLR6 results in differing immune responses [1], and currently, activation of a specific TLR2 heterodimer cannot be selectively achieved with most known TLR2 agonists. Therefore, to further understand the specific mechanisms behind the varying heterodimer signaling pathways, the development of selective small molecules (i.e. CU-T12-9) is essential [4].
Key features of InvivoGen’s synthetic TLR2 agonists:
- Potent activators of the TLR2-TLR1 or TLR2-TLR6 heterodimer
- Functionally validated using InvivoGen’s HEK-Blue™ hTLR2 cellular assay
- Each lot is highly pure and free of microbial contaminants
References:
1. Oliveira-Nascimento, L. et al. 2012. The Role of TLR2 in Infection and Immunity. Front Immunol 3, 79.
2. Takeuchi, O. et al. 2001. Discrimination of bacterial lipoproteins by Toll-like receptor 6. Int Immunol 13, 933-940.
3. Takeuchi, O. et al. 2002. Cutting edge: role of Toll-like receptor 1 in mediating immune response to microbial lipoproteins. J Immunol 169, 10‑14.
4. Cheng, K. et al. 2015. Specific activation of the TLR1-TLR2 heterodimer by small-molecule agonists. Sci Adv 1
