ME2 Human

ME2 is a homotetrameric protein, meaning it consists of four identical subunits. Each subunit is a non-glycosylated polypeptide chain containing 573 amino acids, resulting in a total molecular mass of approximately 64.4 kDa . The enzyme is characterized by its ability to bind NAD+ (nicotinamide adenine dinucleotide) and catalyze the conversion of malate to pyruvate, releasing carbon dioxide in the process .

The reaction catalyzed by ME2 is as follows:

$$\text{Malate} + \text{NAD}^+ \rightarrow \text{Pyruvate} + \text{CO}_2 + \text{NADH}$$

This reaction is essential for maintaining the balance of NAD+/NADH in the mitochondria and plays a significant role in energy production and metabolic regulation.

Recombinant human ME2 is typically produced in Escherichia coli (E. coli). The recombinant protein is expressed as a single polypeptide chain with a His-tag at the C-terminus to facilitate purification . The protein is then purified using proprietary chromatographic techniques to achieve a purity of over 95%, as determined by SDS-PAGE and HPLC .

Recombinant ME2 is widely used in biochemical and physiological studies to understand its role in metabolism and its potential implications in various diseases. It is also used in drug discovery and development to screen for inhibitors or activators of the enzyme.

The recombinant ME2 protein is typically lyophilized from a concentrated solution in PBS (phosphate-buffered saline) at pH 7.4 and stored at temperatures ranging from -20°C to -70°C . After reconstitution, the protein can be stored at 2-8°C for up to one month or at -20°C to -70°C for long-term storage. It is important to avoid repeated freeze-thaw cycles to maintain the protein’s stability and activity .