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Recombinant Human Myeloperoxidase/MPO Protein (His Tag)
Recombinant Human Myeloperoxidase/MPO Protein (His Tag)
Artikelnummer
ELSPDMH100014-20
Verpackungseinheit
20 µg
Hersteller
Elabscience Biotechnology
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Abbreviation: Myeloperoxidase;MPO
Target Synonym: Myeloperoxidase;MPO
Target Species: Human
Expression Host: HEK293 Cells
Fusion Tag: C-10His
UNIProt ID: P05164
Background: Myeloperoxidase (MPO) is a heme-containingenzyme belonging to the XPO subfamily of peroxidases. It is an abundant neutrophil and monocyte glycoprotein thatcatalyzes the hydrogen peroxide-dependentconversion of chloride, bromide, and iodide to multiple reactive species. Post-translationalprocessing of MPO involvesthe insertion of a heme moiety and the proteolytic removal of both a propeptide and a 6 aa internal peptide. This results in a disulfide-linkeddimer composed of a60 kDa heavy and 12 kDa light chain that associate into a 150 kDa enzymatically active tetramer. The tetramer contains two heme groups and one disulfide bondbetween the heavy chains. Alternate splicing generates two additional isoforms of MPO, one with a 32 aa insertion in the light chain, and another with a deletion ofthe signal sequence and part of the propeptide. Human and mouse MPO share 87% aa sequence identity. MPO activity results in protein nitrosylation and theformation of 3-chlorotyrosineand dityrosine crosslinks. MPO is also associated with a variety of other diseases, and inhibits vasodilation in inflammation by depleting the levelsof NO. Serum albumin functions as a carrier protein during MPO movement to the basolateral side of epithelial cells. MPO is stored in neutrophil azurophilicgranules. Upon cellular activation, it is deposited into pathogen-containingphagosomes.
Sequence: Ala49-Ser745
Purity: > 95 % as determined by reducing SDS-PAGE.
Formulation: Lyophilized from a 0.2 um filtered solution of 20mM Tris-HCl, 150mM NaCl, pH 8.0.
Normally 5 % - 8 % trehalose, mannitol and 0.01% Tween80 are added as protectants before lyophilization.
Please refer to the specific buffer information in the printed manual.
Endotoxin: < 1.0 EU per ug of the protein as determined by the LAL method.
Target Synonym: Myeloperoxidase;MPO
Target Species: Human
Expression Host: HEK293 Cells
Fusion Tag: C-10His
UNIProt ID: P05164
Background: Myeloperoxidase (MPO) is a heme-containingenzyme belonging to the XPO subfamily of peroxidases. It is an abundant neutrophil and monocyte glycoprotein thatcatalyzes the hydrogen peroxide-dependentconversion of chloride, bromide, and iodide to multiple reactive species. Post-translationalprocessing of MPO involvesthe insertion of a heme moiety and the proteolytic removal of both a propeptide and a 6 aa internal peptide. This results in a disulfide-linkeddimer composed of a60 kDa heavy and 12 kDa light chain that associate into a 150 kDa enzymatically active tetramer. The tetramer contains two heme groups and one disulfide bondbetween the heavy chains. Alternate splicing generates two additional isoforms of MPO, one with a 32 aa insertion in the light chain, and another with a deletion ofthe signal sequence and part of the propeptide. Human and mouse MPO share 87% aa sequence identity. MPO activity results in protein nitrosylation and theformation of 3-chlorotyrosineand dityrosine crosslinks. MPO is also associated with a variety of other diseases, and inhibits vasodilation in inflammation by depleting the levelsof NO. Serum albumin functions as a carrier protein during MPO movement to the basolateral side of epithelial cells. MPO is stored in neutrophil azurophilicgranules. Upon cellular activation, it is deposited into pathogen-containingphagosomes.
Sequence: Ala49-Ser745
Purity: > 95 % as determined by reducing SDS-PAGE.
Formulation: Lyophilized from a 0.2 um filtered solution of 20mM Tris-HCl, 150mM NaCl, pH 8.0.
Normally 5 % - 8 % trehalose, mannitol and 0.01% Tween80 are added as protectants before lyophilization.
Please refer to the specific buffer information in the printed manual.
Endotoxin: < 1.0 EU per ug of the protein as determined by the LAL method.
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