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The pGEM-T is 3kb in length, and contains the amplicin resistance gene, conferring selection of the plasmid in E. coli, and the ori site which is the bacterial origin of replication. The plasmid has multiple cloning sites as shown below. The coding sequence was inserted by TA cloning. Many E. coli strains are suitable for the propagation of this vector including JM109, DH5α and TOP10.
The coding sequence can be easily obtained by digesting the vector with proper restriction enzyme(s). The coding sequence can also be amplified by PCR with M13 primers, or primer pair SP6 and T7.
|Cynomolgus monkey MDH1 Gene cDNA Clone (full-length ORF Clone), expression ready, FLAG-tagged||CG90156-G-F|
|Cynomolgus monkey MDH1 Gene cDNA Clone (full-length ORF Clone), expression ready, His-tagged||CG90156-G-H|
|Cynomolgus monkey MDH1 Gene cDNA Clone (full-length ORF Clone), expression ready, Myc-tagged||CG90156-G-M|
|Cynomolgus monkey MDH1 Gene cDNA Clone (full-length ORF Clone), expression ready, untagged||CG90156-G-N|
|Cynomolgus monkey MDH1 Gene cDNA Clone (full-length ORF Clone), expression ready, HA-tagged||CG90156-G-Y|
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.