Characterization of flavin binding in oxygen-independent fluorescent reporters was written by Anderson, Nolan T.;Weyant, Kevin B.;Mukherjee, Arnab. And the article was included in AIChE Journal in 2020.SDS of cas: 65-22-5 The following contents are mentioned in the article:
Fluorescent proteins based on light, oxygen, and voltage (LOV) sensing photoreceptors are among the few reporter gene technologies available for studying living systems in oxygen-free environments that render reporters based on the green fluorescent protein nonfluorescent. LOV reporters develop fluorescence by binding FMN (FMN), which they endogenously obtain from cells. As FMN is essential to cell physiol. as well as for determining fluorescence in LOV proteins, it is important to be able to study and characterize flavin binding in LOV reporters. To this end, we report a method for reversibly separating FMN from two commonly used LOV reporters to prepare stable and soluble apoproteins. Using fluorescence titration, we measured the equilibrium dissociation constant for binding with all three cellular flavins: FMN, FAD, and riboflavin. Finally, we exploit the riboflavin affinity of apo LOV reporters, identified in this work, to develop a fluorescence turn-on biosensor for vitamin B2. This study involved multiple reactions and reactants, such as 3-Hydroxy-5-(hydroxymethyl)-2-methylisonicotinaldehyde hydrochloride (cas: 65-22-5SDS of cas: 65-22-5).
3-Hydroxy-5-(hydroxymethyl)-2-methylisonicotinaldehyde hydrochloride (cas: 65-22-5) belongs to alcohols. Alcohols are weak acids. The most acidic simple alcohols (methanol and ethanol) are about as acidic as water, and most other alcohols are somewhat less acidic. The most common reactions of alcohols can be classified as oxidation, dehydration, substitution, esterification, and reactions of alkoxides.SDS of cas: 65-22-5
Referemce:
Alcohol – Wikipedia,
Alcohols – Chemistry LibreTexts