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Usage

Uses

Used in Research and Analysis:
(3beta,4alpha,8alpha,12xi)-4,15-bis(acetyloxy)-3-hydroxy-12,13-epoxytrichothec-9-en-8-yl 3-hydroxy-3-methylbutanoate is used as a research compound for studying the effects of trichothecene mycotoxins on biological systems. Its complex structure and toxic properties make it a valuable subject for investigations into the mechanisms of toxicity and potential countermeasures against mycotoxin exposure.
It is crucial to emphasize that any use of (3beta,4alpha,8alpha,12xi)-4,15-bis(acetyloxy)-3-hydroxy-12,13-epoxytrichothec-9-en-8-yl 3-hydroxy-3-methylbutanoate outside of controlled research environments is strongly discouraged due to the significant risks associated with its toxicity. Proper safety measures, including the use of personal protective equipment and adherence to strict laboratory protocols, must be in place when working with (3beta,4alpha,8alpha,12xi)-4,15-bis(acetyloxy)-3-hydroxy-12,13-epoxytrichothec-9-en-8-yl 3-hydroxy-3-methylbutanoate.

Upstream product

• 21259-20-1 T-2 toxin 
• 108947-28-0 4β,15-diacetoxy-3α-(2-tetrahydropyranyloxy)scirpene-8β-ol 
• 625-08-1 3-Hydroxy-3-methylbutyric acid 

Relevant academic research and scientific papers

Structure-function analysis of porcine cytochrome P450 3A29 in the hydroxylation of T-2 toxin as revealed by docking and mutagenesis studies

T-2 toxin, one of the type A trichothecenes, presents a potential hazard to human and animal health. Our previous work demonstrated that porcine cytochrome P450 3A29 (CYP3A29) played an important role in the hydroxylation of T-2 toxin. To identify amino a

The catalytic activity of cytochrome P450 3A22 is critical for the metabolism of T-2 toxin in porcine reservoirs

Contamination of food by T-2 toxin, a trichothecene mycotoxin, poses a serious threat to human health. We report the identification of cytochrome P450 3A22 (CYP3A22) responsible for 3′-hydroxylation of T-2 and HT-2 in pigs. The present study shows that T-2 toxin significantly induces CYP3A22 expression in primary piglet hepatocytes. Moreover, recombinant pig CYP3A22 converted T-2 toxin into TC-1 (3′-OH-T-2 toxin) and HT-2 toxin into TC-3 (3′-OH-HT-2 toxin) in vitro. These results suggest that pig CYP3A22 primarily eliminates T-2 and HT-2 toxins by 3′-hydroxylation of isovaleryl groups. Therefore, CYP3A22 is critical for xenobiotic metabolism and endogenous biochemical biotransformation of trichothecene mycotoxin in porcine reservoirs.