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Oxidation kinetics for roGFP2 WT -PfGrx fusion constructs The in vivo oxidation kinetics from fusion constructs between roGFP2 WT and a variety of glutaredoxins and mutants thereof were shown to correlate very well with the rate constants for the oxidative half-reaction from GSSCys assays in vitro, suggesting that the glutathionylation of the glutaredoxin and not the transfer of oxidation to the fused roGFP2 moiety was rate-limiting under the chosen conditions 15,34,35

Here we show that glutaryllipoyl adducts (Lp glu ) are constantly formed on ketoacid dehydrogenases and that the serine hydrolase ABHD11 acts as a glutaryllipoyl thioesterase that removes these lipoyl adducts

All compounds are intended strictly for laboratory research use and are not approved for human consumption.

Perform a patch test on a small area of skin before full application to identify any hypersensitivity reaction