Date published: 2025-11-3

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Slc22a27 Inhibitors

Chemical inhibitors of solute carrier family 22, member 27 (SLC22A27) include a range of compounds that exert their inhibitory effects through competitive binding to the substrate-binding sites of the protein. Probenecid, a well-known inhibitor of renal excretion of organic anions, directly competes with substrates of SLC22A27, thereby reducing the protein's transport efficiency. Similarly, Sulfinpyrazone, by competing for the same binding sites, effectively reduces the transport activity of SLC22A27. This action is mirrored by Benzbromarone, which binds to the active site of the transporter, thereby blocking its function. Indomethacin, a drug that also serves to inhibit SLC22A27, achieves its inhibitory action through a competitive mechanism, directly interacting with the transport sites to block substrate movement.

Continuing with this theme, Ketoprofen, Ibuprofen, and Naproxen are all chemicals that inhibit solute carrier family 22, member 27 by binding to its transporter sites, which hinders the uptake and movement of organic anions across cell membranes. Diclofenac extends this inhibitory pattern by binding to the substrate interaction sites, thereby curtailing the protein's ability to facilitate transport. Flurbiprofen, following a similar mechanism, binds competitively to the active sites of SLC22A27, preventing transport of its substrates. Mefenamic acid, Piroxicam, and Phenylbutazone all contribute to the inhibition of SLC22A27 by competing with natural substrates for the transporter's binding sites, which leads to a marked decrease in the protein's transport activity. These inhibitors, through their individual actions, collectively contribute to the inhibition of SLC22A27 by obstructing the transporter's substrate-binding capacity and reducing its overall function.

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