Myeloperoxidase from human leukocytes

Source material tested and found negative for antibody to HIV and for HBSAG.

Myeloperoxidase (MPO) from human leukocytes has been used in MPO assay.

Myeloperoxidase from human leukocytes has been used:

• as a standard to quantify the neutrophil (polymorphonuclear cell [PMN]) infiltration in lung tissue
• as a neutrophil extracelullar trap (NET) component to stimulate 10⁶ dendritic cells or 10⁶ macrophages
• as a standard in myeloperoxidase (MPO) assay to measure pancreatic MPO

Myeloperoxidase (MPO) has a crucial role to play in destruction of various microorganisms and foreign cells, such as bacteria, fungi, viruses, red cells and malignant and nonmalignant nucleated cells. MPO catalyzes the production of number of reactive oxidant species (ROS) that influence tissue damage during inflammation. MPO and its downstream inflammatory pathways function as a potent therapeutic target for prophylaxis of atherosclerotic cardiovascular disease. MPO catalyze the synthesis of polychlorinated dibenzo(p)dioxins and furans (PCDD/F) from precursor such as chlorophenols in presence of hydrogen peroxide (H₂O₂).

Myeloperoxidase (MPO) is encoded by the gene mapped to human chromosome 17q22-24. The encoded protein is a leukocyte-derived enzyme and is an integral constituent of the innate immune response. MPO belongs to the heme peroxidase superfamily. MPO is a heme protein containing iron and is highly expressed in leukocytes, neutrophils, monocytes and some subtypes of tissue macrophages.

Lysosomal heme-containing protein.

One unit of myeloperoxidase will catalyze the consumption of one micromole of hydrogen peroxide and the production of ¹/₄ micromole of tetraguaiacol per minute at pH 7.0 and 25 °C

Lyophilized from 50 mM sodium acetate buffer, pH 6.0, 0.1 M sodium chloride