METAP1 Protein (recombinant human)

Protein Construction: Recombinant Human METAP1 is produced by our E.coli expression system and the target gene encoding Met1-Phe386 is expressed. Sequence: Met1-Phe386. Endotoxin: < 1.0 EU per µg as determined by the LAL method. Apparent Molecular Mass: 38&45-50 kDa. Protein function: Methionine Aminopeptidase 1 is a member of the M24 family of metalloproteases. METAP1 plays an important role in G(2)/M phase regulation of the cell cycle and may serve as a promising target for the discovery and development of new anticancer agents. METAP1 and METAP2 have different substrate specificity due to the differences in both size and shape of the active sites. The proteolytic removal of N-terminal methionine from nascent peptides is catalyzed by a family of enzymes known as methionine aminopeptidases (MetAPs) and is essential for cell growth. Inhibition of METAPs provides a novel strategy in developing anti-cancer drugs. Protein function: Cotranslationally removes the N-terminal methionine from nascent proteins. The N-terminal methionine is often cleaved when the second residue in the primary sequence is small and uncharged (Met- Ala-, Cys, Gly, Pro, Ser, Thr, or Val). Required for normal progression through the cell cycle. [The UniProt Consortium]