MDH2 Mouse Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 335 amino acids (25-338a.a.) and having a molecular mass of 35.4kDa. MDH2 is fused to a 21 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
MGSSHHHHHH SSGLVPRGSH MAKVAVLGAS GGIGQPLSLL LKNSPLVSRL TLYDIAHTPG VAADLSHIET RANVKGYLGP EQLPDCLKGC DVVVIPAGVP RKPGMTRDDL FNTNATIVAT LTAACAQHCP EAMVCIIANP VNSTIPITAE VFKKHGVYNP NKIFGVTTLD IVRANTFVAE LKGLDPARVN VPVIGGHAGK TIIPLISQCT PKVDFPQDQL ATLTGRIQEA GTEVVKAKAG AGSATLSMAY AGARFVFSLV DAMNGKEGVV ECSFVQSKET ECTYFSTPLL LGKKGLEKNL GIGKITPFEE KMIAEAIPEL KASIKKGEDF VKNMK.
The Mdh2 gene is located on chromosome 5 in mice and is a protein-coding gene . The protein itself is localized to the mitochondria and is involved in the malate-aspartate shuttle, which is essential for metabolic coordination between the cytosol and mitochondria . The recombinant form of this enzyme, often expressed in E. coli, is used for various research purposes.
MDH2 is widely expressed in various tissues, with high expression levels found in the adrenal glands, small intestine, heart, and pancreas . The enzyme’s primary function is to facilitate the conversion of malate to oxaloacetate, a critical step in the citric acid cycle. This cycle is fundamental for cellular respiration, providing energy in the form of ATP by oxidizing acetyl-CoA derived from carbohydrates, fats, and proteins.
Recombinant mouse MDH2 is typically produced in E. coli and purified using conventional chromatography techniques. The recombinant protein often includes a His-tag at the N-terminus to facilitate purification . The molecular weight of the recombinant protein is approximately 35.4 kDa, and it exhibits high purity (>95%) as determined by SDS-PAGE . The specific activity of the enzyme is greater than 800 units/mg, defined as the amount of enzyme that cleaves 1 µmole of oxaloacetate and beta-NADH to L-malate and beta-NAD per minute at pH 8.0 at 37°C .
MDH2 is essential for the proper functioning of the citric acid cycle, which is pivotal for energy production in cells. The enzyme’s activity is crucial for maintaining the balance of NAD+/NADH within the mitochondria, thereby influencing various metabolic pathways. Additionally, the malate-aspartate shuttle, in which MDH2 plays a significant role, is vital for transferring reducing equivalents across the mitochondrial membrane, thus linking cytosolic and mitochondrial metabolism .
Recombinant MDH2 is widely used in biochemical and physiological studies to understand its role in metabolism and energy production. It is also employed in studies investigating mitochondrial function and metabolic disorders. The enzyme’s activity can be measured to assess mitochondrial health and function in various experimental settings.