protein

NAD-ME Protein, Human (N-His)

HY-P71918A

5 μg;10 μg;50 μg;100 μg

118;200;559;950 USD

NAD-ME Protein, Human (N-His)

proteins

E. coli

5 μg;10 μg;50 μg;100 μg

118;200;559;950 USD

NAD-ME, a mitochondrial malic enzyme, relies on NAD and catalyzes the oxidative decarboxylation of malate to pyruvate within the mitochondria. Essential for cellular energy metabolism and the tricarboxylic acid (TCA) cycle, NAD-ME links metabolic pathways, influencing energy production and precursor molecule generation. Its enzymatic role is pivotal for balancing cellular redox reactions and meeting the cell's metabolic demands. NAD-ME Protein, Human (N-His) is the recombinant human-derived NAD-ME protein, expressed by E. coli , with C-6*His labeled tag.

Human

NAD-ME is a mitochondrial malic enzyme characterized by its dependence on NAD and its role in catalyzing the oxidative decarboxylation of malate to pyruvate. This enzymatic activity takes place within the mitochondria, contributing to cellular energy metabolism and the tricarboxylic acid (TCA) cycle. By facilitating the conversion of malate to pyruvate, NAD-ME plays a crucial role in linking various metabolic pathways, impacting both energy production and the generation of precursor molecules. This enzymatic function is integral to maintaining the balance of cellular redox reactions and supporting the metabolic demands of the cell.

Malate dehydrogenase; Malic enzyme 2; Malic enzyme 2 mitochondrial; Malic enzyme 2 NAD+; dependent mitochondrial; Malic enzyme mitochondrial; Malic enzyme NAD+; dependent mitochondrial; MAOM_HUMAN; ME 2; ME2; mitochondrial; NAD dependent malic enzyme mitochondrial; NAD ME; NAD-dependent malic enzyme; NAD-ME; ODS1; Pyruvic malic carboxylase

Greater than 95% as determined by reducing SDS-PAGE

Lyophilized from a 0.2 μm filtered solution of 50 mM Tris-HCL, 300 mM NaCl, pH 7.4.

Room temperature in continental US; may vary elsewhere.