L-Phenylalanine-13C6 is a stable isotope-labeled variant of the essential amino acid L-Phenylalanine. As a competitive antagonist of the glycine- and glutamate-binding sites on N-methyl-D-aspartate receptors (NMDARs), it exhibits a binding affinity (KB) of 573 μM. Additionally, it targets the α2δ subunit of voltage-dependent calcium channels with a Ki of 980 nM. This reagent is valuable in biochemical research, particularly in metabolic studies and the synthesis of pharmaceuticals and food flavorings.
L-Phenylalanine-13C6 is a stable isotope-labeled variant of the essential amino acid L-Phenylalanine. As a competitive antagonist of the glycine- and glutamate-binding sites on N-methyl-D-aspartate receptors (NMDARs), it exhibits a binding affinity (KB) of 573 μM. Additionally, it targets the α2δ subunit of voltage-dependent calcium channels with a Ki of 980 nM. This reagent is valuable in biochemical research, particularly in metabolic studies and the synthesis of pharmaceuticals and food flavorings.
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