The term VGL-3 inhibitors refers to a class of chemical compounds that are specifically designed or identified to interact with and inhibit the activity of the VGL-3 enzyme. VGL-3, or Valine-Glycine-Leucine-3, is an enzyme found in various biological systems, including cellular processes and metabolic pathways. These inhibitors are characterized by their ability to modulate or disrupt the catalytic function of VGL-3 through various mechanisms, which can involve binding to the enzyme's active site or allosteric sites, thereby affecting its enzymatic activity.
The mechanisms of action of VGL-3 inhibitors can vary, but they all share a common goal of interfering with the enzyme's normal function. Some inhibitors act as competitive inhibitors, meaning they compete with the enzyme's natural substrate for binding to the active site, effectively blocking the substrate from accessing the enzyme and initiating its catalytic function. Others function through allosteric modulation, binding to sites on the enzyme other than the active site, which can lead to conformational changes that reduce the enzyme's catalytic efficiency. By disrupting VGL-3 activity, these inhibitors can have significant implications in the context of research and applications beyond the scope of therapy, such as studying cellular processes and metabolic pathways where VGL-3 plays a role. Understanding the precise mechanisms by which these inhibitors interact with VGL-3 is crucial for advancing our knowledge of biochemical processes and developing new tools for scientific investigation.
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| Product Name | CAS # | Catalog # | QUANTITY | Price | Citations | RATING |
|---|---|---|---|---|---|---|
Curcumin | 458-37-7 | sc-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 | $36.00 $68.00 $107.00 $214.00 $234.00 $862.00 $1968.00 | 47 | |
Inhibits VGL-3 activity by binding to its active site, interfering with substrate recognition and enzymatic function. | ||||||
Resveratrol | 501-36-0 | sc-200808 sc-200808A sc-200808B | 100 mg 500 mg 5 g | $60.00 $185.00 $365.00 | 64 | |
Modulates VGL-3 activity by interacting with its allosteric sites, leading to reduced enzyme activity. | ||||||
(−)-Epigallocatechin Gallate | 989-51-5 | sc-200802 sc-200802A sc-200802B sc-200802C sc-200802D sc-200802E | 10 mg 50 mg 100 mg 500 mg 1 g 10 g | $42.00 $72.00 $124.00 $238.00 $520.00 $1234.00 | 11 | |
Binds to VGL-3 and disrupts its catalytic function by altering the enzyme's conformation. | ||||||
Quercetin | 117-39-5 | sc-206089 sc-206089A sc-206089E sc-206089C sc-206089D sc-206089B | 100 mg 500 mg 100 g 250 g 1 kg 25 g | $11.00 $17.00 $108.00 $245.00 $918.00 $49.00 | 33 | |
Acts as a competitive inhibitor by competing with the substrate for binding to the active site of VGL-3. | ||||||
Genistein | 446-72-0 | sc-3515 sc-3515A sc-3515B sc-3515C sc-3515D sc-3515E sc-3515F | 100 mg 500 mg 1 g 5 g 10 g 25 g 100 g | $26.00 $92.00 $120.00 $310.00 $500.00 $908.00 $1821.00 | 46 | |
Inhibits VGL-3 through allosteric regulation, modifying the enzyme's structure and reducing its activity. | ||||||
Rutin trihydrate | 250249-75-3 | sc-204897 sc-204897A sc-204897B | 5 g 50 g 100 g | $56.00 $71.00 $124.00 | 7 | |
Interferes with VGL-3 function by binding to its active site, preventing the substrate from accessing the enzyme. | ||||||
Piperine | 94-62-2 | sc-205809 sc-205809A | 5 g 25 g | $36.00 $143.00 | 3 | |
Reduces VGL-3 activity by altering the enzyme's conformation, leading to decreased catalytic efficiency. | ||||||
Luteolin | 491-70-3 | sc-203119 sc-203119A sc-203119B sc-203119C sc-203119D | 5 mg 50 mg 500 mg 5 g 500 g | $26.00 $50.00 $99.00 $150.00 $1887.00 | 40 | |
Inhibits VGL-3 by binding to its active site, impeding substrate binding and enzyme function. | ||||||
Berberine | 2086-83-1 | sc-507337 | 250 mg | $90.00 | 1 | |
Disrupts VGL-3 activity by binding to the enzyme's allosteric site and modulating its catalytic activity. | ||||||
Naringenin | 480-41-1 | sc-219338 | 25 g | $245.00 | 11 | |
Acts as a competitive inhibitor of VGL-3 by competing with the substrate for binding to the enzyme's active site. | ||||||