Recombinant Human METAP1 protein

**Background of METAP1 Recombinant Protein**

Methionine aminopeptidase 1 (METAP1) is a conserved metalloenzyme critical for post-translational protein modification. It catalyzes the removal of N-terminal methionine residues from nascent polypeptides, a process essential for protein maturation, stability, and functional regulation. By editing protein N-termini, METAP1 influences diverse cellular pathways, including angiogenesis, cell proliferation, and apoptosis. Dysregulation of METAP1 activity has been linked to pathological conditions such as cancer, cardiovascular diseases, and microbial infections, highlighting its potential as a therapeutic target.

Recombinant METAP1 protein is produced via genetic engineering, typically by expressing the METAP1 gene in bacterial (e.g., *E. coli*) or eukaryotic systems, followed by purification using affinity tags like His-tag. This engineered protein retains the enzymatic activity of native METAP1. enabling researchers to study its structural and functional properties in vitro. Its applications span drug discovery, biochemical assays, and structural studies, particularly in screening inhibitors that could modulate METAP1 activity for therapeutic purposes.

Studies using recombinant METAP1 have revealed its dual dependence on divalent metal ions (e.g., Co²⁺, Mn²⁺) for catalysis and provided insights into substrate specificity. Additionally, METAP1's role in regulating eukaryotic initiation factor 2α (eIF2α) phosphorylation underscores its broader impact on cellular stress responses. As research continues, METAP1 recombinant protein remains a vital tool for unraveling its biological significance and developing targeted therapies against METAP1-associated diseases.