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Recombinant Mouse Myeloperoxidase protein (His Tag)

Species

Mouse

Purity

>90 %, SDS-PAGE

Tag

His Tag

Activity

not tested

Cat no : Eg0702

Validation Data Gallery

Product Information

Purity >90 %, SDS-PAGE
Endotoxin <1.0 EU/μg protein, LAL method
Activity 
Not tested
Expression HEK293-derived Mouse Myeloperoxidase protein Met16-Thr718(Accession# AAR99349) with a His tag at the C-terminus.
GeneID 17523
Accession AAR99349
PredictedSize 84 kDa
SDS-PAGE
Formulation Lyophilized from sterile PBS, pH 7.4. Normally 5% trehalose and 5% mannitol are added as protectants before lyophilization.
Reconstitution Briefly centrifuge the tube before opening. Reconstitute at 0.1-0.5 mg/mL in sterile water.
Storage Conditions
It is recommended that the protein be aliquoted for optimal storage. Avoid repeated freeze-thaw cycles.
  • Until expiry date, -20℃ to -80℃ as lyophilized proteins.
  • 3 months, -20℃ to -80℃ under sterile conditions after reconstitution.
Shipping The product is shipped at ambient temperature. Upon receipt, store it immediately at the recommended temperature.

Background

Myeloperoxidase (MPO) is a heme-containing enzyme primarily found in neutrophils and certain monocytes, playing a crucial role in the innate immune system. MPO generates reactive oxygen species (ROS), such as hypochlorous acid, which are essential for killing pathogens during phagocytosis. Additionally, MPO is a key component of neutrophil extracellular traps (NETs), which capture and kill extracellular pathogens. However, MPO can also contribute to tissue damage and inflammation when released from activated neutrophils. Elevated MPO levels have been associated with various diseases, including cardiovascular diseases and neurodegenerative disorders like Alzheimer's disease.

References:

1. Wright, Joy R et al. Journal of Alzheimer's disease : JAD vol. 89,4 (2022): 1483-1492.                                                            2. Aratani, Yasuaki. Archives of biochemistry and biophysics vol. 640 (2018): 47-52.                                                                  3. Strzepa, Anna et al. Cellular immunology vol. 317 (2017): 1-8.                                                                                                   4. Jannesar, Kosar, and Hamid Soraya. Biochemical and biophysical research communications vol. 755 (2025): 151578.