Mouse Leucine Aminopeptidase (LAP) ELISA Kit-Sandwich

Cytosol aminopeptidase is a cytosolic metallopeptidase responsible for catalyzing the removal of unsubstituted N-terminal hydrophobic amino acids from various peptides. The enzyme's activity depends on the presence of Zn2+ ions, and its substrate specificity can be modulated by interactions with other cofactors. For example, it exhibits specific Cys-Gly hydrolyzing activity for Cys-Gly-S-conjugates in the presence of Mn2+. This enzyme is involved in glutathione metabolism and the degradation of glutathione S-conjugates, potentially contributing to the regulation of cellular redox status. In mice, cytosol aminopeptidase plays crucial roles in protein degradation, metabolic regulation, immune regulation, and autophagy, with their specific functions varying according to cell type, tissue environment, and pathological state.