Date published: 2026-1-10

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Ribosomal Protein L12P8 Inhibitors

The chemical class denoted as Ribosomal Protein L12P8 Inhibitors comprises a category of compounds intricately designed to selectively target the molecular entity Ribosomal Protein L12P8. As a member of the ribosomal protein family, Ribosomal Protein L12P8 plays an integral role in the structure and function of the ribosome, the cellular machinery responsible for protein synthesis. The detailed understanding of Ribosomal Protein L12P8's functions and interactions within this context remains a subject of active investigation. Inhibitors within the Ribosomal Protein L12P8 Inhibitors class are meticulously engineered molecules with the primary goal of modulating the activity or function of Ribosomal Protein L12P8, thereby inducing an inhibitory effect. Researchers engaged in this field employ a multifaceted approach, combining insights from structural biology, medicinal chemistry, and computational modeling to unravel the complex molecular interactions between the inhibitors and the target Ribosomal Protein L12P8.

Structurally, Ribosomal Protein L12P8 Inhibitors are characterized by specific molecular features designed to facilitate selective binding to Ribosomal Protein L12P8. This selectivity is crucial to minimize unintended effects on other cellular components, ensuring a focused impact on the intended molecular target. The development of inhibitors within this chemical class involves a comprehensive exploration of structure-activity relationships, optimization of pharmacokinetic properties, and a deep understanding of the molecular mechanisms associated with Ribosomal Protein L12P8. As researchers delve deeper into the functional aspects of Ribosomal Protein L12P8 Inhibitors, the knowledge generated contributes not only to deciphering the specific roles of Ribosomal Protein L12P8 but also to advancing our broader comprehension of the intricate processes governing protein synthesis within cells. The exploration of Ribosomal Protein L12P8 Inhibitors stands as a significant avenue for expanding fundamental knowledge in molecular pharmacology and cellular biology.

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Items 1 to 10 of 11 total

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Product NameCAS #Catalog #QUANTITYPriceCitationsRATING

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)

Binds to DNA and inhibits RNA polymerase, which could reduce the transcription of ribosomal protein genes.

Doxorubicin

23214-92-8sc-280681
sc-280681A
1 mg
5 mg
$176.00
$426.00
43
(3)

Intercalates DNA and inhibits topoisomerase II, potentially decreasing ribosomal protein gene transcription.

Fluorouracil

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

A uracil analog that disrupts RNA processing and function, which could affect ribosomal protein synthesis.

Cycloheximide

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

Inhibits eukaryotic protein synthesis by interfering with the translocation step on the ribosome.

α-Amanitin

23109-05-9sc-202440
sc-202440A
1 mg
5 mg
$269.00
$1050.00
26
(2)

Inhibits RNA polymerase II, effectively reducing mRNA synthesis for ribosomal proteins.

Mycophenolic acid

24280-93-1sc-200110
sc-200110A
100 mg
500 mg
$69.00
$266.00
8
(1)

Inhibits inosine monophosphate dehydrogenase, leading to depleted nucleotide pools and reduced RNA synthesis.

Triptolide

38748-32-2sc-200122
sc-200122A
1 mg
5 mg
$90.00
$204.00
13
(1)

Has been shown to inhibit RNA polymerase I, II, and III, which would reduce rRNA and mRNA production for ribosomal proteins.

Anisomycin

22862-76-6sc-3524
sc-3524A
5 mg
50 mg
$99.00
$259.00
36
(2)

Inhibits peptidyl transferase activity of the ribosome, affecting protein elongation.

Puromycin

53-79-2sc-205821
sc-205821A
10 mg
25 mg
$166.00
$322.00
436
(1)

Causes premature chain termination by acting as an analog of aminoacyl-tRNA during translation.

Chloramphenicol

56-75-7sc-3594
25 g
$90.00
10
(1)

Binds to the 50S subunit of the bacterial ribosome and inhibits bacterial protein synthesis.