METAP1 Human

METAP1 is responsible for the cotranslational removal of the N-terminal methionine from nascent proteins. This process is essential because the N-terminal methionine is often cleaved when the second residue in the primary sequence is small and uncharged, such as alanine, cysteine, glycine, proline, serine, threonine, or valine . The removal of the initiator methionine is critical for the proper function and stability of many proteins .

METAP1 is required for normal progression through the cell cycle and is essential for cell growth . It is involved in various cellular pathways, including visual phototransduction and the N-end rule pathway, which is a eukaryotic pathway for protein degradation . The enzyme’s activity is crucial for maintaining cellular homeostasis and proper protein function.

Recombinant Human Methionyl Aminopeptidase 1 is typically produced in Escherichia coli (E. coli) expression systems. The recombinant protein is often tagged with a His-tag at the N-terminus to facilitate purification and is expressed as a full-length protein ranging from 1 to 386 amino acids . The purity of the recombinant protein is usually greater than 90%, making it suitable for various applications such as SDS-PAGE and mass spectrometry (MS) .

Recombinant METAP1 is widely used in biochemical and molecular biology research to study its role in protein maturation and cellular processes. It is also a target for developing novel anti-cancer drugs, as inhibition of METAP1 can disrupt cell growth and proliferation . Understanding the function and regulation of METAP1 can provide insights into various diseases and potential therapeutic strategies.

Mutations or dysregulation of the METAP1 gene have been associated with certain diseases, including granulomatous myositis and autosomal recessive deafness . Research into these associations helps in understanding the broader implications of METAP1 in human health and disease.