Human Myeloperoxidase, natural protein
Humanmyeloperoxidase (MPO). Isolated from human peripheral blood polymorphonuclearleukocytes.
purity > 80% (SDS-PAGE)
0.4-0.9μg/ml (depending on the type of ELISA plate and coating buffer) Suitable forbiotinylation and iodination.
Ionicstrength between150 and 200mM, neutral to slightly alkaline pH and 20 %glycerol as cryoprotective agent.
2-8°C short term, -20°C long term
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 neutrophils.
Myeloperoxidase(MPO) is a peroxidase enzyme (EC 126.96.36.199) most abundantly present inneutrophil granulocytes (a subtype of white blood cells). It is a lysosomalprotein stored in azurophilic granules of the neutrophil. MPO has a hemepigment, which causes it
MPO; AFBP; IBP1; PP12; IGF-BP25; hIGFBP-1; IGFBP1; insulin-like growth factor-binding protein 1; IBP-1; IGFBP-1; OTTHUMP00000159561; OTTHUMP00000207990; OTTHUMP00000214348; binding protein-25; binding protein-26; binding protein-28; placental protein 12;