Myeloperoxidase (MPO) is a highly cationic glycosolated hemoprotein that has a molecular weight of 144kD. The hemoprotein consists of two dimmers linked via a disulfide bridge. Each dimmer is composed of a heavy (53kD) and light (15kD) sub-unit. Each heavy chain contains an independently acting protoporphyrin group containing a central iron (1-5). MPO is present in the azurophilic granules of polymorphonuclear leukocytes (PMNs) and is unique to neutrophils and monocytes. However, monocytes contain only one third of the MPO found in PMN’s. MPO utilizes H202 produced by the neutrophils to oxidize a variety of aromatic compounds to give substrate radicals for bactericidal activity (4 review). This enzyme is unique, however, in that it can oxidize chloride ions to produce a strong nonradical oxidant, HOCl. HOCl is the most powerful bactericidal produced by neutrophils (4 review). Excessive production of these radicals can cause oxidative stress leading to oxidative tissue injury. Fluoro MPOHOCL uses a chlorination activity protocol that utilizes a non-fluorescent detection reagent, APF, which is converted to its fluorescent analog in the presence of HOCl. The kit is used for detection of MPO chlorination activity in neutrophils and macrophages, as well as detection of PMN infiltration in tissue samples (inflammation and innate host defense mechanisms). MPO chlorination activity been implicated in acute and chronic manifestations of cardiovascular disease and acute and chronic inflammatory disorders due to chlorination tissue damage.

Fluorescence plate reader

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