Date published: 2025-10-25

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SLC26A10 Inhibitors

Chemical inhibitors of SLC26A10 encompass a range of compounds that impede its anion transport function. DIDS, a known anion exchanger inhibitor, can directly target the anion exchange mechanism of SLC26A10, resulting in a decrease in its ability to transport anions across the cell membrane. This action is shared by CFTR(inh)-172 and GlyH-101, both of which are primarily CFTR inhibitors but can also inhibit SLC26A10 due to the structural and functional similarities they share with CFTR, specifically in regard to anion exchange. Similarly, NPPB, a chloride channel blocker, can bind to SLC26A10 and prevent the transport of chloride ions, which is a primary function of the protein. Tannic acid takes a more general approach by non-specifically binding to and precipitating proteins, including SLC26A10, thus impairing its function. Further, Niflumic acid and Flufenamic acid, known for their inhibitory action on various chloride channels, can prevent the movement of chloride ions by directly obstructing the ion pathways in SLC26A10. Diclofenac, though known as a nonsteroidal anti-inflammatory drug, can inhibit SLC26A10 by interfering with anion transport mechanisms, a secondary action that derives from its possible effects on membrane transporters. Indanyloxyacetic acid targets the chloride/bicarbonate exchanger activity, a crucial function of SLC26A10, thereby impeding its transport capabilities. Talniflumate, by modulating chloride channels, can disrupt the bicarbonate transport function of SLC26A10. Ethacrynic acid, although traditionally used for different purposes, can impede the chloride transport mechanisms that SLC26A10 facilitates. Lastly, Mefenamic acid can act as a blocker of chloride channels, thus interfering with the anion exchange capability of SLC26A10, leading to functional inhibition of the protein's anion transport abilities. Through these mechanisms, each compound contributes to the overall inhibition of SLC26A10's role in cellular anion exchange processes.
Product NameCAS #Catalog #QUANTITYPriceCitationsRATING

CFTR Inhibitor-172

307510-92-5sc-204680
sc-204680A
10 mg
50 mg
$165.00
$510.00
10
(1)

CFTR(inh)-172, though primarily targeting CFTR, can inhibit SLC26A10 by disrupting the anion transport, as both proteins share functional similarities in anion exchange.

KRIBB11

342639-96-7sc-507391
5 mg
$95.00
(0)

GlyH-101 is another CFTR inhibitor that can block SLC26A10 by directly occluding its anion exchange pore due to the structural and functional similarities with CFTR.

Gallotannin

1401-55-4sc-202619
sc-202619A
sc-202619B
sc-202619C
sc-202619D
sc-202619E
sc-202619F
1 g
10 g
100 g
250 g
1 kg
2.5 kg
5 kg
$25.00
$36.00
$66.00
$76.00
$229.00
$525.00
$964.00
12
(1)

Tannic acid can inhibit SLC26A10 by non-specifically binding to and precipitating proteins, including membrane transporters, thus impairing its anion transport function.

Niflumic acid

4394-00-7sc-204820
5 g
$31.00
3
(1)

Niflumic acid, as an inhibitor of various chloride channels, can inhibit SLC26A10 by preventing chloride ion movement across the membrane.

Flufenamic acid

530-78-9sc-205699
sc-205699A
sc-205699B
sc-205699C
10 g
50 g
100 g
250 g
$26.00
$77.00
$151.00
$303.00
1
(1)

Flufenamic acid can inhibit SLC26A10 by blocking its anion transport channels, similarly to its action on other members of the chloride channel family.

Diclofenac acid

15307-86-5sc-357332
sc-357332A
5 g
25 g
$107.00
$292.00
5
(1)

Diclofenac, while primarily an NSAID, can inhibit SLC26A10 on the premise of its ability to interfere with chloride channels and anion transport mechanisms.

Ethacrynic acid

58-54-8sc-257424
sc-257424A
1 g
5 g
$49.00
$229.00
5
(1)

Ethacrynic acid can inhibit SLC26A10 by its general action on chloride transport mechanisms, impeding the movement of chloride/bicarbonate that SLC26A10 facilitates.

Mefenamic acid

61-68-7sc-205380
sc-205380A
25 g
100 g
$104.00
$204.00
6
(0)

Mefenamic acid can inhibit SLC26A10 by acting as a blocker of chloride channels and interfering with the anion exchange capability of the protein.