Date published: 2025-12-24

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OR10G7 Inhibitors

Chemical inhibitors of OR10G7 exert their effects by binding to various sites on the protein, thereby blocking the actions of natural ligands and preventing downstream signaling. For instance, Benzethonium chloride can occupy the odorant binding site of OR10G7, preventing the natural odorant ligands from initiating a signaling cascade and effectively inhibiting the receptor's function. Likewise, Methyl anthranilate binds to the ligand-binding domain of OR10G7, obstructing the entry of activating molecules and thus inhibiting the receptor. Naringin and Quinine also inhibit OR10G7 by binding to the receptor in ways that alter its conformation, preventing the usual activation by odorants. Further inhibitory interactions include Cinnamaldehyde, which binds to the active site of OR10G7 and precludes the structural alterations necessary for receptor activation. Capsaicin similarly interacts with OR10G7's binding site, potentially causing conformational changes that inhibit the receptor's activation. Thymol and Eugenol bind to the active site as well, blocking the receptor and disrupting its interaction with activating molecules. Menthol targets the hydrophobic pocket of OR10G7, crucial for the receptor's alignment with odorant molecules, and thus inhibits its function. Triclosan and Camphor bind to the ligand-binding domain, blocking the site from natural inhibitors and impeding the receptor's activation. Lastly, Acesulfame potassium binds to the extracellular domain of OR10G7, which could induce conformational changes that prevent the receptor from being activated by odorants.
Product NameCAS #Catalog #QUANTITYPriceCitationsRATING

Benzethonium chloride

121-54-0sc-239299
sc-239299A
100 g
250 g
$53.00
$105.00
1
(1)

Benzethonium chloride can inhibit OR10G7 by binding to the odorant binding site, preventing the interaction of OR10G7 with its natural odorant ligands, leading to a loss of olfactory signal transduction.

Naringin

10236-47-2sc-203443
sc-203443A
25 g
50 g
$44.00
$99.00
7
(1)

Naringin can inhibit OR10G7 by binding to the protein and altering its conformation, which reduces its ability to interact with its specific odorant molecules.

Quinine

130-95-0sc-212616
sc-212616A
sc-212616B
sc-212616C
sc-212616D
1 g
5 g
10 g
25 g
50 g
$77.00
$102.00
$163.00
$347.00
$561.00
1
(0)

Quinine is known to bind to various olfactory receptors, and it can inhibit OR10G7 by stabilizing a conformation that prevents activation by odorants.

Cinnamic Aldehyde

104-55-2sc-294033
sc-294033A
100 g
500 g
$102.00
$224.00
(0)

Cinnamaldehyde can inhibit OR10G7 by binding to the active site and preventing the structural changes required for the protein to become activated by its natural ligands.

Capsaicin

404-86-4sc-3577
sc-3577C
sc-3577D
sc-3577A
50 mg
250 mg
500 mg
1 g
$94.00
$173.00
$255.00
$423.00
26
(1)

Capsaicin can inhibit OR10G7 by interacting with its binding site, which may alter the protein's conformation and prevent activation by its endogenous odorant molecules.

Thymol

89-83-8sc-215984
sc-215984A
100 g
500 g
$97.00
$193.00
3
(0)

Thymol can inhibit OR10G7 by binding preferentially to the protein's active site, effectively blocking it from being activated by its natural ligands.

Eugenol

97-53-0sc-203043
sc-203043A
sc-203043B
1 g
100 g
500 g
$31.00
$61.00
$214.00
2
(1)

Eugenol inhibits OR10G7 by binding to and altering the conformation of the protein, which disrupts its ability to interact with activating molecules.

(±)-Menthol

89-78-1sc-250299
sc-250299A
100 g
250 g
$38.00
$67.00
(0)

Menthol inhibits OR10G7 by binding to the hydrophobic pocket of the protein, which is necessary for the proper alignment and activation by odorant molecules.

Triclosan

3380-34-5sc-220326
sc-220326A
10 g
100 g
$138.00
$400.00
(1)

Triclosan can inhibit OR10G7 by interacting with the protein's ligand-binding domain, blocking the site and preventing the binding and activation by natural odorants.

Acesulfame Potassium

55589-62-3sc-210736
25 g
$240.00
(0)

Acesulfame potassium can inhibit OR10G7 by binding to the extracellular domain, potentially causing conformational changes that negatively impact the protein's ability to be activated by odorants.