Description
Product Characteristics: Human myeloperoxidase (MPO) is a dimeric protein composed of two heavy subunits (53 kDa) and two light subunits (15 kDa). Each MPO molecule contains two prosthetic porphyrins which play an important role in the catalytic cycle. Molecular weights for MPO isoforms from pools of normal human samples range from 114,000 to 140,000 daltons reflecting a heterogeneous mixture of isoforms when assayed under non-reducing conditions of SDS-PAGE. Often MPO from a single donor will yield a homogenous preparation reflecting a single isoform. The carbohydrate component of MPO, consisting of mannose, glucose and N-acetylglucosamine residues is 2.5%. MPO is inhibited by azide and other compounds. MPO is stored in primary granules of neutrophils and serves as a bactericidal agent in that MPO catalyzes the production of hypochlorous acid (HOCl), a powerful oxidant. HOCl is derived from chloride ion (Cl-) and hydrogen peroxide (H2O2). In a number of inflammatory situations, MPO is released into the extracellular matrix where its measurement can be used as an indication of neutrophil activation.
Synonyms: EC 1.11.1.7 antibody, MPO antibody
Target Information: Myeloperoxidase (MPO) is a heme protein synthesized during myeloid differentiation that constitutes the major component of neutrophil azurophilic granules. Produced as a single chain precursor, myeloperoxidase is subsequently cleaved into a light and heavy chain. The mature myeloperoxidase is a tetramer composed of 2 light chains and 2 heavy chains. This enzyme produces hypohalous acids central to the microbicidal activity of netrophils. [provided by RefSeq, Jul 2008]