Nicotinamide 1,N6-ethenoadenine dinucleotide (ε-NAD) acts as a fluorescent substrate with significant utility in biochemical research. This analog of NAD can be cleaved by phosphodiesterase I, sourced from C. adamanteus venom, and demonstrates binding affinity to bovine liver glutamate dehydrogenase. It serves as a substrate for G-ADP ribosylation of G proteins, a process facilitated by bacterial toxins, making it valuable for investigating ADP ribosylation reactions. Its fluorescent properties enhance detection and analysis in experimental applications.
Nicotinamide 1,N6-ethenoadenine dinucleotide (ε-NAD) acts as a fluorescent substrate with significant utility in biochemical research. This analog of NAD can be cleaved by phosphodiesterase I, sourced from C. adamanteus venom, and demonstrates binding affinity to bovine liver glutamate dehydrogenase. It serves as a substrate for G-ADP ribosylation of G proteins, a process facilitated by bacterial toxins, making it valuable for investigating ADP ribosylation reactions. Its fluorescent properties enhance detection and analysis in experimental applications.
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