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Recombinant Mouse Myeloperoxidase/MPO

Recombinant Mouse Myeloperoxidase/MPO Recombinant Mouse Myeloperoxidase/MPO

Instruction Manual!

Product name: Recombinant Mouse Myeloperoxidase/MPO
Source:Human Cells
Purity:Greater than 95% as determined by reducing SDS-PAGE.
Buffer Formulation:Lyophilized from a 0.2 μm filtered solution of PBS, pH7.4.
Applications:Applications:SDS-PAGE; WB; ELISA; IP.
Storage:Avoid repeated freeze/thaw cycles. Store at 2-8 oC for one month. Aliquot and store at -80 oC for 12 months.
UOM:100ug/50ug/200ug/1mg/1g
Source Human Cells
Description Recombinant Mouse Myeloperoxidase is produced by our Mammalian expression system and the target gene encoding Met16-Thr718 is expressed with a 10His tag at the C-terminus.
Names Myeloperoxidase; MPO
Accession # P11247
Formulation Lyophilized from a 0.2 μm filtered solution of PBS, pH7.4.
Shipping The product is shipped at ambient temperature.
Reconstitution Always centrifuge tubes before opening. Do not mix by vortex or pipetting.
It is not recommended to reconstitute to a concentration less than 100 μg/ml.
Dissolve the lyophilized protein in ddH2O.
Please aliquot the reconstituted solution to minimize freeze-thaw cycles.
Storage Lyophilized protein should be stored at < -20°C, though stable at room temperature for 3 weeks.
Reconstituted protein solution can be stored at 4-7°C for 2-7 days.
Aliquots of reconstituted samples are stable at < -20°C for 3 months.
Purity Greater than 95% as determined by reducing SDS-PAGE.
Endotoxin Less than 0.1 ng/µg (1 IEU/µg) as determined by LAL test.
Amino Acid Sequence
MLQTSNGATPALLGEVENSVVLSCMEEAKQLVDRAYKERRESIKRSLQSGSASPTELLFYFKQPV AGTRTAVRAADYLHVALDLLKRKLQPLWPRPFNVTDVLTPAQLNLLSVSSGCAYQDVRVTCPPND KYRTITGHCNNRRSPTLGASNRAFVRWLPAEYEDGVSMPFGWTPGVNRNGFKVPLARQVSNAIVR FPNDQLTKDQERALMFMQWGQFLDHDITLTPEPATRFSFFTGLNCETSCLQQPPCFPLKIPPNDP RIKNQKDCIPFFRSCPACTRNNITIRNQINALTSFVDASGVYGSEDPLARKLRNLTNQLGLLAIN TRFQDNGRALMPFDSLHDDPCLLTNRSARIPCFLAGDMRSSEMPELTSMHTLFVREHNRLATQLK RLNPRWNGEKLYQEARKIVGAMVQIITYRDYLPLVLGPAAMKKYLPQYRSYNDSVDPRIANVFTN AFRYGHTLIQPFMFRLNNQYRPTGPNPRVPLSKVFFASWRVVLEGGIDPILRGLMATPAKLNRQN QIVVDEIRERLFEQVMRIGLDLPALNMQRSRDHGLPGYNAWRRFCGLPQPSTVGELGTVLKNLEL ARKLMAQYGTPNNIDIWMGGVSEPLEPNGRVGQLLACLIGTQFRKLRDGDRFWWENPGVFSKQQR QALASISLPRIICDNTGITTVSKNNIFMSNTYPRDFVSCNTLPKLNLTSWKETHHHHHHHHHH
Background Myeloperoxidase (MPO) is a hemecontaining enzyme belonging to the XPO subfamily of peroxidases. It is an abundant neutrophil and monocyte glycoprotein that catalyzes the hydrogen peroxidedependent conversion of chloride, bromide, and iodide to multiple reactive species. MPO activity results in protein nitrosylation and the formation of 3-chlorotyrosine and dityrosine crosslinks. Modification of ApoB100, as well as the lipid and cholesterol components of LDL and HDL, promotes the development of atherosclerosis. 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 pathogencontaining phagosomes. While mice lacking MPO are impaired in clearing select microbial infections,MPO deficiency in humans does not necessarily result in heightened susceptibility to infections.

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