Date published: 2025-11-1

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FLJ20433 Inhibitors

The designation FLJ20433 inhibitors would likely refer to a group of compounds designed to specifically inhibit the activity of a protein encoded by a gene initially labeled as FLJ20433. The FLJ prefix typically arises from a gene cataloging system and stands for Full-Length Japanese, indicating that the gene was identified during large-scale cDNA sequencing projects primarily conducted in Japan. These identifiers were often assigned to genes for which little functional information was available at the time of discovery. As such, the FLJ20433 protein would be presumed to have some biological activity or function that could be modulated by small molecules. However, without a clearly established biological role or even a well-understood molecular function, the development of inhibitors targeting such a protein would be in the preliminary stages of research.

In the case that FLJ20433 has been characterized and there is an interest in modulating its activity, the development of inhibitors would begin with a detailed understanding of the protein's structure and function. Researchers would first seek to determine its role within cellular processes, its three-dimensional structure, and the key domains that are critical for its activity. Techniques such as X-ray crystallography, cryo-electron microscopy, or NMR spectroscopy could be used to elucidate the protein's structure, revealing potential binding sites for inhibitors. These sites could include active sites, allosteric sites, or interfaces that are important for the protein's interaction with other cellular components. Once potential binding sites have been identified, the process of inhibitor design can commence, with the goal of producing molecules that can bind to FLJ20433 with high specificity and affinity.

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Product NameCAS #Catalog #QUANTITYPriceCitationsRATING

Etoposide (VP-16)

33419-42-0sc-3512B
sc-3512
sc-3512A
10 mg
100 mg
500 mg
$32.00
$170.00
$385.00
63
(1)

Inhibits topoisomerase II, leading to DNA damage and potential transcriptional arrest.