Date published: 2025-12-24

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EG215895 Inhibitors

Sult3a2, a gene predicted to enable sulfotransferase activity, plays a pivotal role in the complex landscape of cellular sulfate conjugation processes. As a member of the sulfotransferase family, Sult3a2 is anticipated to be involved in the transfer of sulfate groups to various substrates within the cytoplasm, contributing to the modification of biomolecules essential for cellular functions. The prediction of sulfotransferase activity implies that Sult3a2 is intricately linked to the sulfation of diverse molecules, including proteins, lipids, and small molecules. This enzymatic activity is integral to the formation of sulfated biomolecules, which are crucial for signal transduction, metabolism, and the structural integrity of various cellular components.

The cytoplasmic localization of Sult3a2 further emphasizes its active engagement in cellular processes, signifying its role in the initial steps of sulfation reactions. Sulfation, as facilitated by Sult3a2, is essential for the regulation of biological activities, including the modulation of signaling pathways and the fine-tuning of cellular responses. The prediction of its involvement in sulfation processes highlights its significance in the dynamic interplay of cellular events. Inhibition of Sult3a2 encompasses a multifaceted approach, targeting both direct and indirect mechanisms to modulate its sulfotransferase activity. Various inhibitors disrupt the availability of sulfate co-substrates, interfere with sulfate activation processes, or directly interact with sulfuryl groups, thereby hindering the enzymatic function of Sult3a2. This broad spectrum of inhibitory strategies reveals the intricate nature of controlling Sult3a2-mediated sulfation reactions, providing insights into potential avenues for influencing cellular processes reliant on sulfate conjugation. Overall, understanding the functional significance of Sult3a2 and its intricate inhibition mechanisms contributes to unraveling the complexities of cellular sulfation and opens avenues for further exploration of its regulatory role in cellular physiology.

SEE ALSO...

Product NameCAS #Catalog #QUANTITYPriceCitationsRATING

RO-3306

872573-93-8sc-358700
sc-358700A
sc-358700B
1 mg
5 mg
25 mg
$65.00
$160.00
$320.00
37
(1)

RO-3306 disrupts sulfotransferase activity by inhibiting the production of 3'-phosphoadenosine-5'-phosphosulfate (PAPS), a crucial co-substrate. This inhibition leads to a reduction in sulfation processes, impacting Sult3a2 enzymatic activity in the cytoplasm.

Sodium sulfate anhydrous

7757-82-6sc-212945
sc-212945A
500 g
1 kg
$62.00
$89.00
(1)

Sodium Sulfate, when present in excess, competes with sulfate donors for sulfotransferase binding sites, leading to reduced sulfotransferase activity. This competition impedes Sult3a2-mediated sulfation processes, influencing its predicted enzymatic function in the cytoplasm.

Thiourea

62-56-6sc-213038
50 g
$37.00
(1)

Thiourea inhibits sulfotransferase activity indirectly by scavenging sulfate ions. This competition for sulfate ions diminishes the substrate pool for sulfotransferase reactions, influencing Sult3a2-mediated sulfation processes in the cytoplasm and reducing its enzymatic activity.

Dextran Sulfate, Sodium Salt MW ~500,000

9011-18-1sc-203917
sc-203917A
sc-203917B
sc-203917C
10 g
50 g
100 g
1 kg
$56.00
$163.00
$367.00
$3070.00
7
(2)

Dextran Sulfate inhibits sulfotransferase activity by interacting with sulfated biomolecules. Its competition with endogenous substrates hinders the enzymatic function of Sult3a2, influencing cytoplasmic sulfation processes and impeding its predicted role in sulfuryl group transfer.

2,4-Dinitrophenol, wetted

51-28-5sc-238345
250 mg
$58.00
2
(1)

2,4-Dinitrophenol disrupts sulfotransferase activity by covalently modifying sulfuryl groups. This direct interaction with the catalytic site of Sult3a2 inhibits its enzymatic function, influencing cytoplasmic sulfation processes and impairing its role in sulfuryl group transfer.