MetAP2 (human), (recombinant) (HA-tag)

MetAP2 is a metalloenzyme that catalyzes removal of the N-terminal methionine from proteins, with the physiologically relevant metal thought to be either cobalt or manganese. Since it was identified as the target of the anti-angiogenic natural product fumagilin (Prod. No. BML-CT100), it has been studied for its involvement in cancer, angiogenesis, inflammation, and rheumatoid arthritis. Because of differing substrate specificities and kinetics it is not desirable to substitute bacterial methionine aminopeptidase for mammalian MetAP2.