Malate Dehydrogenase, Recombinant (MDH)

Malate Dehydrogenase is an enzyme that catalyzes the conversion of (S)-malate and NAD+ to oxaloacetate and NADH. Hyperthmophile MDH from Thermus flavus MDH exists as a dimer comprising of identical subunit having 350 amino acid residues. Thermus Flavas MDH has excellent thermal stability and long-term storage stability in liquid. MDH has a lower level of side reaction in serum AST Assay than that of purified bacterial enzyme.\n\nUnit Definition:\nOne unit is defined as 1umol of NAD+ production per minute under the assay conditions (25 degrees C, pH 7.5).\n\nApplication:\nSuitable for use as a calibrator or control serum.\n\nStorage and Stability:\nAliquot to avoid repeated freezing and thawing and store at -70 degrees C. For maximum recovery of product, centrifuge the original vial after thawing and prior to removing the cap. Aliquots are stable for at least 12 months.

Prices direct from United States Biological

Quick response times

Exclusive Biosave savings/discounts

SPECIFICATIONS

Catalog Number

M2115-07B

Size

10KU

Form

Supplied as liquid.

Purity

Purified

References

1. Insertion of transposon Tn5tac1 in the Sinorhizobium meliloti malate dehydrogenase (mdh) gene results in conditional polar effects on downstream TCA cycle genes. Dymov SI, Meek DJ, Driscoll BT, Mol Plant Microbe Interact 2004 Dec;17(12):1318-27 2. Degradation of the gluconeogenic enzymes fructose-1,6-bisphosphatase and malate dehydrogenase is mediated by distinct proteolytic pathways and signaling events. Hung GC, Brown CR, Liu J, J Biol Chem 2004 Nov 19;279(47):49138-50 3. Large improvement in the thermal stability of a tetrameric malate dehydrogenase by single point mutations at the dimer-dimer interface. Bjork A, Dalhus B, Sirevag R, J Mol Biol 2004 Aug 27;341(5):1215-26 4. An alpha-proteobacterial type malate dehydrogenase may complement LDH function in Plasmodium falciparum. Cloning and biochemical characterization of the enzyme. Tripathi AK, Desai PV, Khan SI, Eur J Biochem 2004 Sep;271(17):3488-502 5. Mitochondrial malate dehydrogenase from the thermophilic, filamentous fungus Talaromyces emersonii. Maloney AP, Callan SM, Tuohy MG, Eur J Biochem 2004 Aug;271(15):3115-26 6. Molecular adaptation: the malate dehydrogenase from the extreme halophilic bacterium Salinibacter ruber behaves like a non-halophilic protein. Madern D, Zaccai G, Biochimie 2004 Apr-May;86(4-5):295-303.