Myeloperoxidase (MPO) is a glycoprotein with a alpha2beta2 heteromultimer expressed in all
cells of the myeloid linage. MPO is abundantly present in azurophilic granules of
polymorphonuclear neutrophils. It is an important enzyme used during phagocytic lysis of
engulfed foreign particles which takes part in the defense of the organism through production
of hypochlorous acid (HOCl), a potent oxidant. MPO is rapidly released by activated
polymorphonuclear neutrophils. Involvement of MPO has been described in numerous
diseases such as atherosclerosis, lung cancer, Alzheimer’s disease and multiple sclerosis.
Autoimmune antibodies to MPO are involved in Wegener’s disease. Since the discovery of
MPO deficiency, initially regarded as rare and restricted to patients suffering from severe
infections, MPO has attracted more clinical attention.
The classical MPO assay is an enzymatic assay for activity of MPO. This classical MPO
assay is hampered by the presence of inhibitory compounds in tissue homogenates and
plasma. In this type of assays spiking often gives unreliable results. The human MPO ELISA
is not influenced by inhibitors of the enzyme activity.
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