epitope mapping near the C-terminus of ADE2 of human origin
recommended for detection of ADE2 of mouse, rat and human origin by WB, IF and ELISA; also reactive with additional species, including equine, canine, bovine, porcine and avian
ADE2 Background Information Two successive steps in de novo purine biosynthesis are catalyzed by the enzymes 5-aminoimidazole ribonucleotide (AIR) carboxylase and 4-[(N-succinylamino)carbonyl]-5-aminoimidazole ribonucleotide (SAICAR) synthetase. In vertebrates, a bifunctional enzyme, ADE2 ( also designated PurCE/AIRC) catalyzes successive carboxylation and aspartylation steps of AIR to form SAICAR (1-2). ADE2 is transcribed from a 558 bp intergenic promoter region, which is bound by NRF-1 and Sp1 at sites within the 215-260 region (3). The intergenic region is an integrated bidirectional promoter and a novel initiator-like element plays a central role in coordinating expression of the divergently transcribed ADE2 and GPAT genes (4). The ADE2 mRNA levels increase approximately five to six fold in G1/S phase of the cell cycle over those in G0 phase in synchronized rat 3Y1 fibroblasts (2). The ADE2 gene encodes enzyme of AIRC at step 6 and SAICR synthetase at step 7 in de novo purine nucleotide synthesis (5-7). The ADE2 encoded enzyme has no ATP dependence and no common cofactors or metals are required for catalysis (1). Activities of ADE2 enzyme are found in lysates of human erythrocytes, thrombocytes and leukocytes and in homogenate of the stomach biopsy sample, but not in blood plasma and bile (8).
