Human MPO Knockout Cell Line - MOLM-13

Myeloperoxidase (MPO) is located on human chromosome 17 and contains multiple exons and introns. The protein product of the MPO gene is initially synthesized as an inactive precursor called preproMPO, which undergoes several post-translational modifications to become the active enzyme found in the azurophilic granules of neutrophils. These modifications include cleavage of the signal peptide, glycosylation, and subsequent conversion to a mature tetramer consisting of two heavy chains and two light chains. Myeloperoxidase catalyzes the production of hypochlorous acid (HOCl) and other reactive oxygen species during the respiratory burst, which are potent antimicrobial agents capable of destroying a wide range of pathogens, including bacteria, viruses, and fungi. Mutations and polymorphisms in the MPO gene can have significant effects on human health. For example, certain single nucleotide polymorphisms (SNPs) in the MPO gene have been associated with various diseases, including cardiovascular disease, inflammatory diseases, and certain types of cancer. Although rare, a lack of MPO enzyme activity results in a condition called myeloperoxidase deficiency, which impairs the immune system's ability to fight off infection.