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Rat MDHA / MDH1 Protein (His Tag)

MDL1, Mdhl, Mor2

Catalog Number P80232-R08E
Organism Species Rat
Host E. coli
Synonyms MDL1, Mdhl, Mor2
Molecular Weight The recombinant rat MDH1 comprises 345 amino acids and predicts a molecular mass of 38 kDa. The apparent molecular mass of the rat MDH1 is approximately 39 kDa in SDS-PAGE under reducing conditions.
predicted N Met 1
SDS-PAGE
Purity > 90 % as determined by SDS-PAGE
Protein Construction A DNA sequence encoding the rat MDH1 (O88989) (Met 4-Ala 334) was expressed with a polyhistidine tag at the C-terminus.
Bio-activity
Research Area Signaling |Signal Transduction |Metabolism |Types of disease |Metabolism in Cancer
Formulation Lyophilized from sterile 20mM Tris, 10% glycerol, pH 8.0
1. Normally 5 % - 8 % trehalose and mannitol are added as protectants before lyophilization. Specific concentrations are included in the hardcopy of COA.
Background Malate dehydrogenases 1(MDH1 / MDHA) is soluable form of malate dehydrogenases. Malate dehydrogenases (MDH) is a group of multimeric enzymes consisting of identical subunits usually organized as either dimer or tetramers with subunit molecular weights of 30-35 kDa. MDH has been isolated from different sources including archaea, eubacteria, fungi, plant and mammals. MDH catalyzes the NAD/NADH-dependent interconversion of the substrates malate and oxaloacetate. This reaction plays a key part in the malate / aspartate shuttle across the mitochondrial membrane, and in the tricarboxylic acid cycle within the mitochondrial matrix. The enzymes share a common catalytic mechanism and their kinetic properties are similar, which demonstrates a high degree of structural similarity. The three-dimensional structures and elements essential for catalysis are conserved between mitochondrial and cytoplasmic forms of MDH in eukaryotic cells even though these isoenzymes are only marginally related at the level of primary structure. 
Reference
  • Minarik P, et al. (2002) Malate dehydrogenases--structure and function. Gen Physiol Biophys. 21 (3): 257-65.
  • Musrati RA, et al. (1998) Malate dehydrogenase: distribution, function and properties. Gen Physiol Biophys. 17 (3): 193-210.
  • Hall MD, et al. (1992) Crystal structure of Escherichia coli malate dehydrogenase. A complex of the apoenzyme and citrate at 1.87 A resolution. J Mol Biol. 226 (3): 867-82.