Myeloperoxidase (human) Rabbit Monoclonal Antibody (Clone RM407)

Myeloperoxidase (MPO) is a heme-containing enzyme and the most abundant protein in polymorphonuclear leukocytes (PMNs). It is composed of two subunits linked by a disulfide bridge with each subunit containing a light and a heavy polypeptide chain. It can oxidize a variety of substrates and catalyzes the formation of highly reactive (pseudo)hypohalous acids and radicals including hypochlorous acid. MPO is stored in azurophilic granules of PMNs and is released from activated or necrotic PMNs, after which it can bind to and modify acidic serum proteins, as well as recruit additional PMNs. MPO also has roles in PMN apoptosis and antimicrobial defense systems, including neutrophil extracellular traps (NETs). MPO-deficient mice exhibit reduced survival in a polymicrobial sepsis model, increased susceptibility to experimental autoimmune encephalomyelitis (EAE), and increased atherosclerosis in mice also deficient in the LDL receptor and fed an atherogenic diet.