Date published: 2026-5-2

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eIF1AY Inhibitors

eIF1AY inhibitors represent a class of compounds that specifically target and inhibit the activity of the eukaryotic translation initiation factor 1A (eIF1A), which is essential in the initiation phase of protein synthesis. eIF1A plays a crucial role in stabilizing the binding of the initiator tRNA to the small ribosomal subunit and promoting the proper scanning of the messenger RNA (mRNA) for the start codon. By inhibiting eIF1A, these compounds disrupt the normal initiation process, leading to a decrease in overall protein synthesis. This inhibition can have significant effects on cellular processes, as protein synthesis is fundamental to cell growth, division, and response to environmental stimuli.

The mechanism of action of eIF1AY inhibitors involves binding to specific sites on the eIF1A protein, thereby preventing its interaction with the ribosomal subunits and other initiation factors. This binding can induce conformational changes in eIF1A, rendering it incapable of performing its function in the initiation complex. The development and study of eIF1AY inhibitors have provided valuable insights into the molecular dynamics of translation initiation and the regulatory mechanisms controlling protein synthesis. These compounds have also been used as tools in research to dissect the roles of eIF1A in various cellular pathways and to understand the broader implications of translational control in cellular physiology. The study of eIF1AY inhibitors continues to be a dynamic field, contributing to our understanding of the intricate processes that govern gene expression at the translational level.

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Items 1 to 10 of 16 total

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Product NameCAS #Catalog #QUANTITYPriceCitationsRATING

Salubrinal

405060-95-9sc-202332
sc-202332A
1 mg
5 mg
$34.00
$104.00
87
(2)

Salubrinal inhibits eIF2α dephosphorylation, leading to prolonged phosphorylation, which reduces translation initiation.

Guanabenz HCl

23113-43-1sc-507500
100 mg
$246.00
(0)

Guanabenz reduces eIF2α phosphorylation by activating the eIF2α phosphatase, PP1, allowing translation to proceed normally.

GSK 2606414

1337531-36-8sc-490182
sc-490182A
5 mg
25 mg
$163.00
$572.00
(0)

GSK2606414 inhibits the activity of PERK, a kinase that phosphorylates eIF2α, reducing eIF2α phosphorylation levels.

Cisplatin

15663-27-1sc-200896
sc-200896A
100 mg
500 mg
$138.00
$380.00
101
(4)

Cisplatin indirectly affects eIF2α by causing DNA damage, triggering the integrated stress response and eIF2α phosphorylation.

Thapsigargin

67526-95-8sc-24017
sc-24017A
1 mg
5 mg
$136.00
$446.00
114
(2)

Thapsigargin induces ER stress, activating PERK and leading to eIF2α phosphorylation, thereby inhibiting protein synthesis.

Etoposide (VP-16)

33419-42-0sc-3512B
sc-3512
sc-3512A
10 mg
100 mg
500 mg
$51.00
$231.00
$523.00
63
(1)

Etoposide causes DNA damage, which could lead to a cellular stress response, potentially diverting cellular resources from RNAi pathways and thus down-regulating eIF2C2.

Fluorouracil

51-21-8sc-29060
sc-29060A
1 g
5 g
$37.00
$152.00
11
(1)

By acting as a pyrimidine analog, 5-Fluorouracil might disrupt nucleotide metabolism. This disruption could indirectly affect RNAi components by hampering RNA synthesis, leading to decreased eIF2C2 levels.

Bortezomib

179324-69-7sc-217785
sc-217785A
2.5 mg
25 mg
$135.00
$1085.00
115
(2)

Bortezomib inhibits the proteasome, affecting protein turnover. This can disrupt the balance of cellular proteins, potentially decreasing the stability or synthesis of eIF2C2.

Actinomycin D

50-76-0sc-200906
sc-200906A
sc-200906B
sc-200906C
sc-200906D
5 mg
25 mg
100 mg
1 g
10 g
$74.00
$243.00
$731.00
$2572.00
$21848.00
53
(3)

Actinomycin D hinders RNA synthesis by intercalating DNA. This can lead to a general down-regulation of RNA-derived processes, which might include a decrease in eIF2C2 levels.

Cycloheximide

66-81-9sc-3508B
sc-3508
sc-3508A
100 mg
1 g
5 g
$41.00
$84.00
$275.00
127
(6)

By inhibiting protein synthesis, Cycloheximide might halt the production of new eIF2C2 molecules, leading to a net decrease in eIF2C2 as existing proteins degrade.