Rat MDHA / MDH1 Protein (His Tag)

Malate dehydrogenase 1, NAD (soluble) Protein Datasheet

MDHA / MDH1 Protein Product Information

• Synonym: MDL1, Mdhl, Mor2
• Protein Construction: A DNA sequence encoding the rat MDH1 (O88989) (Met 4-Ala 334) was expressed, fused with a polyhistidine tag at the C-terminus.
• Source: Rat
• Expression Host: E.coli

MDHA / MDH1 Protein QC Testing

• Purity: > 95 % as determined by SDS-PAGE.
• Endotoxin: Please contact us for more information.
• Stability: Samples are stable for up to twelve months from date of receipt at -70℃
• Predicted N terminal: Met 1
• Molecular Mass: 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 42 kDa in SDS-PAGE under reducing conditions.
• Formulation: Lyophilized from sterile 20mM Tris, 10%glycerol, pH8.0
  1. Normally 5 % - 8 % trehalose and mannitol are added as protectants before lyophilization. Specific concentrations are included in the hardcopy of COA.
  2. Please contact us for any concerns or special requirements.
• SDS-PAGE: MDHA / MDH1 protein

MDHA / MDH1 Protein Usage Guide

• Storage: Store it under sterile conditions at -70℃. It is recommended that the protein be aliquoted for optimal storage. Avoid repeated freeze-thaw cycles.
• Reconstitution: A hardcopy of COA with reconstitution instruction is sent along with the products. Please refer to it for detailed information.

MDHA / MDH1 Protein Description

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.

References

1. Minarik P. et al., 2002, Gen Physiol Biophys. 21 (3): 257-65.
2. Musrati RA. et al., 1998, Gen Physiol Biophys. 17 (3): 193-210.
3. Hall MD. et al., 1992, J Mol Biol. 226 (3): 867-82.