Recombinant Rat MDH1 Protein (His Tag) | PKSR030299

Recombinant Rat MDH1 Protein (His Tag) | PKSR030299 | Gentaur US, UK & Europe Disrtribition

Synonyms: MDL1;Mdhl;Mor2

Active Protein: N/A

Activity: A DNA sequence encoding the rat MDH1 (O88989) (Met 4-Ala 334) was expressed with a polyhistidine tag at the C-terminus.

Protein Construction: A DNA sequence encoding the rat MDH1 (O88989) (Met 4-Ala 334) was expressed with a polyhistidine tag at the C-terminus.

Fusion Tag: C-His

Species: Rat

Expressed Host: E.coli

Shipping: This product is provided as lyophilized powder which is shipped with ice packs.

Purity: > 90 % as determined by reducing SDS-PAGE.

Endotoxin: Please contact us for more information.

Stability and Storage: Generally, lyophilized proteins are stable for up to 12 months when stored at -20 to -80℃. Reconstituted protein solution can be stored at 4-8℃ for 2-7 days. Aliquots of reconstituted samples are stable at < -20℃ for 3 months.

Molecular Mass: 38 kDa

Formulation: Lyophilized from sterile 20mM Tris, 10% glycerol, pH 8.0

Reconstitution: Please refer to the printed manual for detailed information.

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. 

Research Area: N/A