LAP3 Human

LAP3 is a protein-coding gene that encodes for a protein involved in the metabolism of amino acids, particularly leucine. The enzyme’s primary function is to release an N-terminal amino acid, Xaa-/-Yaa-, where Xaa is preferably leucine but can also be other amino acids such as proline, though not arginine or lysine . The enzyme also hydrolyzes amino acid amides and methyl esters, although its activity on arylamides is exceedingly low .

Human recombinant LAP3 is produced in Escherichia coli (E. coli) as a single, non-glycosylated polypeptide chain containing 539 amino acids. This recombinant protein has a molecular mass of approximately 58.3 kDa and is fused to a 20 amino acid His-tag at the N-terminus . The recombinant production allows for the enzyme to be used in various research applications, providing a consistent and reliable source of the protein.

LAP3 is widely used in research due to its role in protein processing. It is particularly useful in studies involving the metabolism of arginine and proline, as well as general aminopeptidase activity . The enzyme’s ability to remove N-terminal amino acids makes it a valuable tool in the study of protein degradation and turnover.

While LAP3 itself is not directly associated with specific diseases, its activity is relevant in the context of certain conditions. For example, alterations in aminopeptidase activity can be indicative of metabolic disorders or other pathological states. Additionally, LAP3 has been studied in the context of bacterial vaginosis and trichomoniasis, highlighting its broader relevance in medical research .

Recombinant LAP3 is typically stored at -20°C to ensure its stability over long periods. It is recommended to avoid multiple freeze-thaw cycles to maintain the enzyme’s activity. For short-term use, the enzyme can be stored at 4°C .