Recombinant Human Myeloperoxidase/MPO Protein (His Tag)

Cat. No : CDRP-00375

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Target Information
Target Name	Myeloperoxidase/MPO
Synonyms	Myeloperoxidase; MPO
UniProt ID	P09237
Accession	P05164

Product Details
Expression Host	Human Cells
Species	Human
Tag	C-10His
Molar Mass	80.3 kDa
Sequence	Gln 29-Leu 360

Background
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. 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. This results in a disulfide-linked dimer composed of a 60 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 bond between 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 of the signal sequence and part of the propeptide. Human and mouse MPO share 87% aa sequence identity. MPO activity results in protein nitrosylation and the formation of 3-chlorotyrosine and dityrosine crosslinks. MPO is also associated with a variety of other diseases, and inhibits vasodilation in inflammation by depleting the levels of NO. Serum albumin functions as a carrier protein during MPO movement to the basolateral side of epithelial cells. MPO is stored in neutrophil azurophilic granules. Upon cellular activation, it is deposited into pathogen-containing phagosomes.

Background

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. 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. This results in a disulfide-linked dimer composed of a 60 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 bond between 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 of the signal sequence and part of the propeptide. Human and mouse MPO share 87% aa sequence identity. MPO activity results in protein nitrosylation and the formation of 3-chlorotyrosine and dityrosine crosslinks. MPO is also associated with a variety of other diseases, and inhibits vasodilation in inflammation by depleting the levels of NO. Serum albumin functions as a carrier protein during MPO movement to the basolateral side of epithelial cells. MPO is stored in neutrophil azurophilic granules. Upon cellular activation, it is deposited into pathogen-containing phagosomes.

Properties
Purity	>90% as determined by reducing SDS-PAGE.
Formulation	Lyophilized from a 0.2 μm filtered solution of 20 mM Tris, 150 mM NaCl, pH8.0.
Reconstitution	Please refer to the printed manual for detailed information.
Shipping	This product is provided as lyophilized powder which is shipped with ice packs.
Storage	Generally, lyophilized proteins are stable for up to 12 months when stored at -20 to -80 °C. Reconstituted protein solution can be stored at 4-8 °C for 2-7 days. Aliquots of reconstituted samples are stable at < -20 °C for 3 months.

! For research use only. Not intended for any clinical use.