AU017455 inhibitors are a class of chemical compounds specifically designed to inhibit the function of the AU017455 protein, a relatively lesser-known entity in the field of molecular biology. The protein AU017455 is thought to be involved in complex cellular processes such as signal transduction, gene expression regulation, or intracellular protein interactions. These inhibitors typically work by blocking key functional domains of the protein, preventing it from interacting with its associated partners or substrates within the cell. By inhibiting AU017455, these compounds interfere with its normal role in cellular signaling or structural dynamics, which could affect a variety of downstream biological processes.
Researchers use AU017455 inhibitors to explore the functional importance of this protein in various cellular pathways. Blocking AU017455 allows scientists to study how its inhibition impacts cellular homeostasis, signaling networks, or gene regulatory mechanisms. By observing the effects of inhibition, scientists can gain valuable insights into the protein's role within larger molecular complexes or pathways. These inhibitors serve as crucial tools for dissecting the specific functions of AU017455 in relation to cellular architecture or protein-protein interactions. Moreover, AU017455 inhibitors help provide a clearer understanding of how certain proteins coordinate complex biological responses at the molecular level, contributing to the broader knowledge of intracellular regulation and protein function.
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| Product Name | CAS # | Catalog # | QUANTITY | Price | Citations | RATING |
|---|---|---|---|---|---|---|
Disulfiram | 97-77-8 | sc-205654 sc-205654A | 50 g 100 g | $52.00 $87.00 | 7 | |
Disulfiram can inhibit the function of zinc finger proteins by binding to the structural zinc ions, leading to the destabilization of the zinc finger domain structure, which is critical for the DNA-binding capability of zinc finger protein 957. | ||||||
Zinc | 7440-66-6 | sc-213177 | 100 g | $47.00 | ||
Pyrithione zinc acts by chelating zinc ions, which are essential for the structural integrity of the zinc finger motifs in zinc finger protein 957, resulting in the loss of DNA binding affinity and therefore functional inhibition of the protein. | ||||||
Clioquinol | 130-26-7 | sc-201066 sc-201066A | 1 g 5 g | $44.00 $113.00 | 2 | |
Clioquinol operates by chelating zinc ions, which can disrupt the zinc finger structures necessary for zinc finger protein 957 to interact with DNA, thus inhibiting its function. | ||||||
1,10-Phenanthroline | 66-71-7 | sc-255888 sc-255888A | 2.5 g 5 g | $23.00 $31.00 | ||
1,10-Phenanthroline is capable of chelating metal ions, including zinc. By chelating zinc, it can inhibit the proper folding and function of zinc finger domains within zinc finger protein 957, thereby inhibiting its DNA binding activity. | ||||||
TPEN | 16858-02-9 | sc-200131 | 100 mg | $127.00 | 10 | |
TPEN is a zinc chelator that can deplete zinc ions necessary for the structural formation of zinc finger motifs in zinc finger protein 957, which is required for DNA binding and therefore the protein's function. | ||||||
Phenylarsine oxide | 637-03-6 | sc-3521 | 250 mg | $40.00 | 4 | |
Phenylarsine oxide can bind to vicinal thiol groups that may be in proximity to the zinc-finger motifs of zinc finger protein 957, potentially causing protein misfolding or dysfunction, thereby inhibiting its DNA-binding activity. | ||||||
Ebselen | 60940-34-3 | sc-200740B sc-200740 sc-200740A | 1 mg 25 mg 100 mg | $32.00 $133.00 $449.00 | 5 | |
Ebselen, a selenium-based compound, can modify cysteine residues in proteins. By modifying the cysteine residues in zinc finger protein 957 that coordinate the zinc ion, it can disrupt the zinc finger structure and inhibit the protein's DNA-binding activity. | ||||||
Auranofin | 34031-32-8 | sc-202476 sc-202476A sc-202476B | 25 mg 100 mg 2 g | $150.00 $210.00 $1899.00 | 39 | |
Auranofin can inhibit thiol-dependent enzymes and may inhibit zinc finger protein 957 by interacting with cysteine residues involved in maintaining the zinc finger structure, leading to a loss of function. | ||||||