Anti-Human Methionine Aminopeptidase 2 Antibody Pair

Product Description: Methionyl aminopeptidase 2 (METAP2) is a cytosolic metalloenzyme that catalyzes the hydrolytic removal of N-terminal methionine residues from nascent proteins, playing a critical role in protein maturation and stability. METAP2 is particularly important in endothelial cell growth and proliferation during tumor angiogenesis and tumor cell proliferation, making it a promising target in oncology. The enzyme is also involved in protecting the alpha subunit of eukaryotic initiation factor 2 (eIF2) from inhibitory phosphorylation, thereby regulating protein synthesis. Increased expression of METAP2 is associated with various forms of cancer, and inhibitors such as fumagillin and ovalicin have shown anti-cancer effects by irreversibly binding to the active site of METAP2. 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). The catalytic activity of human METAP2 toward Met-Val peptides is consistently two orders of magnitude higher than that of METAP1, suggesting that it is responsible for processing proteins containing N-terminal Met-Val and Met-Thr sequences in vivo , Protects eukaryotic initiation factor EIF2S1 from translation-inhibiting phosphorylation by inhibitory kinases such as EIF2AK2/PKR and EIF2AK1/HCR. Plays a critical role in the regulation of protein synthesis [The Uniprot Consortium]