Date published: 2026-4-24

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U2 snRNP A Activators

U2 snRNP A Activators are a diverse set of chemical entities designed to specifically target and enhance the activity of the U2 small nuclear ribonucleoprotein A (U2 snRNP A), a crucial component of the spliceosome complex involved in pre-mRNA splicing. This complex process is fundamental to the maturation of messenger RNA (mRNA), whereby introns are excised, and exons are ligated to generate a translatable mRNA sequence. The activators of U2 snRNP A exert their influence by binding to, stabilizing, or facilitating the conformational changes necessary for the U2 snRNP A to interact effectively with the pre-mRNA substrate. By enhancing the assembly and stabilization of the U2 snRNP within the spliceosome, these activators directly contribute to the efficiency and fidelity of the splicing process. The chemical activators may also engage in promoting the recruitment of auxiliary splicing factors and snRNPs, thereby potentiating the catalytic steps of splicing. Some may even function to stabilize the U2 snRNP A structure itself, ensuring a more robust interaction with the branch point sequence within the intron, which is a critical step in the splicing reaction.

The specificity of U2 snRNP A Activators lies in their capacity to selectively bind to the U2 snRNP A or its immediate associating factors, enhancing the snRNP's role without altering the broader RNA processing pathways. These compounds can induce conformational changes that increase the affinity of U2 snRNP A for its pre-mRNA targets or enhance the intermolecular interactions within the spliceosome. Additionally, activators may act indirectly by modulating the phosphorylation state of proteins associated with the U2 snRNP, thus influencing the dynamics of spliceosome assembly. The net effect of these molecular interactions is an increase in the precision and rate of intron removal, which is essential for generating mature mRNAs capable of directing the synthesis of functional proteins. This targeted upregulation of U2 snRNP A's activity ensures that the splicing machinery operates at optimal capacity, maintaining the necessary balance of splicing events required for cellular function and gene expression regulation.

SEE ALSO...

Items 1 to 10 of 11 total

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Product NameCAS #Catalog #QUANTITYPriceCitationsRATING

Amiloride • HCl

2016-88-8sc-3578
sc-3578A
25 mg
100 mg
$22.00
$57.00
6
(2)

Amiloride inhibits the Na+/H+ exchangers, leading to alterations in intracellular pH that can affect snRNP assembly and thereby potentially increase the functional activity of U2 snRNP A by promoting its proper complex formation.

Plumbagin

481-42-5sc-253283
sc-253283A
100 mg
250 mg
$52.00
$62.00
6
(1)

Plumbagin modulates the redox state of cells by affecting NAD+/NADH ratios and reactive oxygen species (ROS) levels. Elevated ROS can modify RNA-binding protein structures and interactions, which might enhance the assembly or function of U2 snRNP A-containing complexes.

Ellagic Acid, Dihydrate

476-66-4sc-202598
sc-202598A
sc-202598B
sc-202598C
500 mg
5 g
25 g
100 g
$58.00
$95.00
$245.00
$727.00
8
(1)

Ellagic acid, an antioxidant, can influence RNA-protein interactions by protecting RNA from oxidative damage, potentially facilitating the enhanced function or stability of U2 snRNP A in RNA splicing.

Zinc

7440-66-6sc-213177
100 g
$48.00
(0)

Zinc is a cofactor for RNA-binding proteins and can stabilize RNA-protein complexes. Zinc sulfate supplementation may enhance U2 snRNP A assembly or function by promoting RNA binding.

Retinoic Acid, all trans

302-79-4sc-200898
sc-200898A
sc-200898B
sc-200898C
500 mg
5 g
10 g
100 g
$66.00
$325.00
$587.00
$1018.00
28
(1)

Retinoic acid influences cellular differentiation processes that could lead to changes in RNA splicing patterns. This may indirectly enhance U2 snRNP A activity by increasing its demand and functional participation in alternative splicing during differentiation.

Spermidine

124-20-9sc-215900
sc-215900B
sc-215900A
1 g
25 g
5 g
$57.00
$607.00
$176.00
(2)

Spermidine is a polyamine that stabilizes RNA structures and can enhance the formation of RNA-protein complexes, potentially increasing the functional activity of U2 snRNP A by promoting snRNP assembly and splicing accuracy.

Puromycin dihydrochloride

58-58-2sc-108071
sc-108071B
sc-108071C
sc-108071A
25 mg
250 mg
1 g
50 mg
$42.00
$214.00
$832.00
$66.00
394
(16)

Puromycin, an antibiotic that inhibits protein synthesis, can induce stress granule formation, where snRNPs are known to localize. This stress response may indirectly enhance the activity of U2 snRNP A by promoting its incorporation into active spliceosomes.

Sodium (meta)arsenite

7784-46-5sc-250986
sc-250986A
100 g
1 kg
$108.00
$780.00
3
(2)

Sodium arsenite induces oxidative stress and the formation of stress granules, which can concentrate snRNP proteins, potentially enhancing the activity of U2 snRNP A by promoting its assembly into functional spliceosomes.

Curcumin

458-37-7sc-200509
sc-200509A
sc-200509B
sc-200509C
sc-200509D
sc-200509F
sc-200509E
1 g
5 g
25 g
100 g
250 g
1 kg
2.5 kg
$37.00
$69.00
$109.00
$218.00
$239.00
$879.00
$1968.00
47
(1)

Curcumin affects various signaling pathways and can modulate protein-protein interactions. It may enhance U2 snRNP A function by influencing spliceosomal protein interactions and promoting efficient splicing.

Caffeine

58-08-2sc-202514
sc-202514A
sc-202514B
sc-202514C
sc-202514D
50 g
100 g
250 g
1 kg
5 kg
$33.00
$67.00
$97.00
$192.00
$775.00
13
(1)

Caffeine, a known phosphodiesterase inhibitor, increases intracellular cAMP levels, which can affect numerous cellular processes including RNA splicing. This may lead to enhanced U2 snRNP A activity by affecting spliceosome dynamics and function.