Date published: 2025-9-14

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OR13A1 Inhibitors

OR13A1 inhibitors are a diverse group of chemical compounds that directly or indirectly impact the functionality of the OR13A1 olfactory receptor through various biochemical mechanisms. Cinnamaldehyde and Eugenol, for example, exert their inhibitory effects by competitively binding to the receptor's active site, blocking interaction with odorant molecules and thus hindering the olfactory signaling process. Similarly, Zinc Sulfate and Copper Sulfate can alter receptor conformation to an inactive state or bind to histidine residues respectively, both resulting in a reduction of OR13A1's ability to bind and respond to its specific ligands. Cholesterol extraction from cell membranes by Methyl-β-cyclodextrin can disrupt lipid rafts which are crucial for receptor localization and signal transduction, indirectly decreasing OR13A1 signaling. Menthol and Quinine can allosterically modulate the receptor leading to an inhibition of the olfactory signaling cascade, while Capsaicin and Icilin may cause desensitization or alter membrane dynamics, thereby indirectly inhibiting the receptor's activity. In addition to competitive and allosteric inhibition, the activity of OR13A1 is also sensitive to changes in cellular energy levels and ionic conditions. Compounds like 2,4-Dinitrophenol disrupt ATP production, a critical energy source for downstream signaling molecules in the OR13A1 pathway, leading to an indirect inhibition of OR13A1 function. Ruthenium Red and Cadmium Chloride, by interfering with calcium channels, can decrease intracellular calcium levels, which are essential for olfactory signal transduction, thus indirectly inhibiting OR13A1's signaling capacity. These inhibitors collectively demonstrate the intricate interplay between OR13A1 receptor activity and various biochemical pathways, showcasing the complexity of modulating olfactory receptor function through chemical means. Each inhibitor, by acting through a unique mechanism, contributes to the understanding of how OR13A1's activity can be selectively downregulated, providing insights into the receptor's role in the broader context of olfactory perception.

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