Recombinant Human Myeloperoxidase (MPO) Protein

Myeloperoxidase (MPO) is a hemoprotein that is abundantly expressed in polymorphonuclear leukocytes (neutrophils) and secreted during their activation. The presence of a peroxidase in the cytoplasmic granules of leukocytes was suggested at the beginning of 20th century but it was the early 1940s that it was purified for the first time. Native MPO is a covalently bound tetrameric complex of two glycosylated alpha chains (MW 59 – 64 kDa) and two unglycosylated beta chains (MW 14 kDa) with total MW about 150 kDa and theoretical pI 9.2. MPO plays an important role in neutrophil microbicidal action through catalyzing chloride ion oxidation to hypochlorous acid, which is a potent antimicrobial agent.
 

Reconstitute in PBS or others.
 

The thermal stability is described by the loss rate. The loss rate was determined by accelerated thermal degradation test, that is, incubate the protein at 37°C for 48h, and no obvious degradation and precipitation were observed. The loss rate is less than 5% within the expiration date under appropriate storage condition.
 

Store it under sterile conditions at -80°C. It is recommended that the protein be aliquoted for optimal storage. Avoid repeated freeze-thaw cycles. Samples are stable for up to twelve months from date of receipt at -80℃.
 

The protein solution is in 0.05M phosphate buffer containing 0.15M NaCl and 0.09% NaN3 pH 7.5. Filtered through a 0.8μM membrane
 

This product is for research use only, not for diagnostic or therapeutic use.