Myeloperoxidase Active Protein | MPO active protein

Myeloperoxidase, Recombinant, Human (MPO, pANCA)

Cat. Num. AAA638041

• Purity: Highly Purified; 90%, as determined by SDS-PAGE and visualized by silver stain. Endotoxin: 1EU/1ug (LAL).
• Synonyms: Myeloperoxidase; Recombinant; Human (MPO; pANCA); MPO active protein

• Purity/Purification: Highly Purified; 90%, as determined by SDS-PAGE and visualized by silver stain. Endotoxin: 1EU/1ug (LAL).
• Form/Format: Supplied as a lyophilized powder from 20mM Tris, 150mM sodium chloride, pH 7.5. Reconstitute with ddH20 and 0.1% BSA or HSA to 0.5-1mg/ml.

• Activity: Measured by its ability to oxidize guaiacol in the presence of hydrogen peroxide (Desser, R.K., et al. 1972 Arch.Biochem. Biophys. 148: 452-65). See Activity Assay Protocol on next page for details. The specific activity of the recombinant human Myeloperoxidase is > 5000 pmoles/min/ug as defined in the assay.
• Preparation and Storage: Lyophilized powder may be stored at -20/-70 degree C. Reconstitute to nominal volume by adding ddH20 and 0.1% BSA or HSA. Aliquot and store at -20/-70 degree C. Reconstituted product is stable for 3 months at -20/-70 degree C. For maximum recovery of product, centrifuge the original vial after thawing and prior to removing the cap. Further dilutions can be made in assay buffer.

Related Product Information for MPO active protein

Myeloperoxidase (MPO) is a heme-containing enzyme belonging to the XPO subfamily of peroxidases. It is an abundant neutrophil and monocyte glycoprotein that catalyzes the hydrogen peroxide-dependent conversion of chloride, bromide, and iodide to multiple reactive species (1). Post-translational processing of MPO involves the insertion of a heme moiety and the proteolytic removal of both a propeptide and a 6 aa internal peptide (2). This results in a disulfide-linked dimer composed of a 60 kD heavy and 12kD light chain that associate into a 150 kD enzymatically active tetramer. The tetramer contains two heme groups and one disulfide bond between the heavy chains (2). Alternate splicing generates two additional isoforms of MPO, one with a 32 aa insertion in the light chain, and another with a deletion of the signal sequence and part of the propeptide (3). Human and mouse MPO share 87% aa sequence identity. MPO activity results in protein nitrosylation and the formation of 3-chlorotyrosine and dityrosine crosslinks (4-6). Modification of ApoB100, as well as the lipid and cholesterol components of LDL and HDL, promotes the development of atherosclerosis (5, 7-9). MPO is also associated with a variety of other diseases (1), and inhibits vasodilation in inflammation by depleting the levels of NO (10). Serum albumin functions as a carrier protein during MPO movement to the basolateral side of epithelial cells (11). MPO is stored in neutrophil azurophilic granules. Upon cellular activation, it is deposited into pathogen-containing phagosomes (2). While mice lacking MPO are impaired in clearing select microbial infections, MPO deficiency in humans does not necessarily result in heightened susceptibility to infections (12, 13).

Product Categories/Family for MPO active protein

Molecular Biology; MB-Enzymes

NCBI and Uniprot Product Information

• NCBI GI #: 188658
• NCBI GeneID: 4353
• UniProt Accession #: P05164; Q14862; Q4PJH5; Q9UCL7; A1L4B8
• Molecular Weight: ~80kD
• NCBI Official Full Name: myeloperoxidase
• NCBI Official Synonym Full Names: myeloperoxidase
• NCBI Official Symbol: MPO
• NCBI Protein Information: myeloperoxidase
• UniProt Protein Name: Myeloperoxidase
• Protein Family: Myeloperoxidase
• UniProt Gene Name: MPO
• UniProt Synonym Gene Names: MPO
• UniProt Entry Name: PERM_HUMAN

NCBI Description

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]

Uniprot Description

MPO: Part of the host defense system of polymorphonuclear leukocytes. It is responsible for microbicidal activity against a wide range of organisms. In the stimulated PMN, MPO catalyzes the production of hypohalous acids, primarily hypochlorous acid in physiologic situations, and other toxic intermediates that greatly enhance PMN microbicidal activity. Homodimer; disulfide-linked. Each monomer consists of a light and a heavy chain. Belongs to the peroxidase family. XPO subfamily. 3 isoforms of the human protein are produced by alternative splicing.

Protein type: EC 1.11.2.2; Oxidoreductase

Chromosomal Location of Human Ortholog: 17q23.1

Cellular Component: extracellular space; azurophil granule; mitochondrion; lysosome; nucleus; secretory granule

Molecular Function: heparin binding; peroxidase activity; metal ion binding; heme binding; chromatin binding

Biological Process: response to food; respiratory burst during defense response; removal of superoxide radicals; hydrogen peroxide catabolic process; response to mechanical stimulus; defense response; response to lipopolysaccharide; response to yeast; response to oxidative stress; defense response to fungus; negative regulation of apoptosis; aging

Disease: Myeloperoxidase Deficiency; Alzheimer Disease