E. coli Methionine Aminopeptidase (aa 2 - 264) [His], recombinant protein from E. coli
Recombinant E. coli Methionine Aminopeptidase antigen, was expressed in E. coli. Ala2-Glu264, with a C-terminal 10-His tag (Accession # NP_414710)
> 95%, by SDS-PAGE under reducing conditions and visualized by silver stain.
2-8°C short term, -20°C long term
Methionine aminopeptidase 2 is an enzyme that in humans is encoded by the METAP2 gene. Methionine aminopeptidase 2, a member of the dimetallohydrolase family, is a cytosolic metalloenzyme that catalyzes the hydrolytic removal of N-terminal methionine residues from nascent proteins. peptide-methionine peptide + methionine. MetAP2 is found in all organisms and is especially important because of its critical role in tissue repair and protein degradation. Furthermore, MetAP2 is of particular interest because the enzyme plays a key role in angiogenesis, the growth of new blood vessels, which is necessary for the progression of diseases including solid tumor cancers and rheumatoid arthritis. MetAP2 is also the target of two groups of anti-angiogenic natural products, ovalicin and fumagillin, and their analogs.
Methionine Aminopeptidase (METAP) carries out the important reaction of removing the initiator Met residue from nascent proteins. There are two types of METAP. Type Ia and type IIa are found in eubacteria and archaea, respectively. Type Ib and type IIb are present in eukaryotes and contain additional N-terminal domains. As a metalloenzyme, METAP activity can be inhibited by EDTA. However, the exact identity of the metal ion remains to be uncovered since several metal ions including cobalt, zinc and iron have been suggested.
AI047573; AL024412; AU014659; MGC102452; A930035J23Rik; Amp2; EIF 2 associated p67 homolog; EIF-2-associated p67; Initiation factor 2 associated 67 kDa glycoprotein; Initiation factor 2-associated 67 kDa glycoprotein; MAP 2; MAP2; MetAP 2; Metap2; Methion