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Recombinant Human Myeloperoxidase Protein

Placeholder Recombinant Human Myoglobin Protein
Placeholder Recombinant Human GPBB Protein
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DataSheet   

The recombinant human MPO protein is derived from in vitro expression of human MPO gene in E. coli and purified using his-tag affinity column and can be used in multiple applications such as cell culture, ELISA and western blot.

Alternative names for myeloperoxidase: MPO

This product is for Laboratory Research Use Only not for diagnostic and therapeutic purposes or any other purposes.

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Description

Genorise Recombinant Human Myeloperoxidase Protein Summary

Alternative names for myeloperoxidase: MPO

Product Specifications

Purity > 97%, by SDSPAGE under reducing conditions and visualized by silver stain.
Endotoxin Level < 0.1 EU per 1 μg of the protein by the LAL method.
Activity na
Source E. coli derived human myeloperoxidase.
Accession # P05164
N-Terminal Sequence Analysis Met
Amino Acid Sequence Met 251-Asp 566
Predicted Molecular Mass 35 kDa
SDS-PAGE 35 kDa, reducing conditions

 

Background: 

Myeloperoxidase (MPO) is a member of the XPO subfamily of peroxidase that in humans is encoded by the MPO gene on chromosome 17. MPO is most abundantly expressed in neutrophil granulocytes and is a lysosomal protein stored in azurophilic granules of the neutrophil and released into the extracellular space during degranulation.[1] It produces hypohalous acids to carry out their antimicrobial activity. It requires heme as a cofactor. Furthermore, it oxidizes tyrosine to tyrosyl radical using hydrogen peroxide as an oxidizing agent.[2] Hypochlorous acid and tyrosyl radical are cytotoxic, so they are used by the neutrophil to kill bacteria and other pathogens.[3] However, this hypochlorous acid may also cause oxidative damage in host tissue. Moreover, MPO oxidation of apoA-I reduces HDL-mediated inhibition of apoptosis and inflammation.[4] In addition, MPO mediates protein nitrosylation and the formation of 3-chlorotyrosine and dityrosine crosslinks. Recent studies have reported an association between elevated myeloperoxidase levels and the severity of coronary artery disease.[5] And Heslop et al. reported that elevated MPO levels more than doubled might increase the risk for cardiovascular mortality over a 13-year period.[6] It has also been suggested that myeloperoxidase plays a significant role in the development of the atherosclerotic lesion and rendering plaques unstable.[7] MPO could serve as a sensitive predictor for myocardial infarction in patients presenting with chest pain.[8] The 2010 Heslop et al. study reported that measuring both MPO and CRP provided added benefit for risk prediction than just measuring CRP alone.[6]

References

  1. Kinkade JM, et al. (1983). Biochem Biophys Res Communications. 114 (1): 296–303.
  2. Heinecke JW, et al. (1993). The Journal of Clinical Investigation. 91 (6): 2866–72.
  3. Hampton MB, et al. (1998). Blood. 92 (9): 3007–17.
  4. Shao B, et al. (2010). Chemical Research in Toxicology. 23 (3): 447–54.
  5. Zhang R, et al. (2001). JAMA. 286 (17): 2136–42.
  6. Heslop CL, e tal. (2010). J American College of Cardiology. 55 (11): 1102–9.
  7. Nicholls SJ, et al. (2005). Arteriosclerosis,Thrombosis and Vascular Bio. 25: 1102–11.
  8. Brennan ML, et al. (2003). The New England Journal of Medicine. 349 (17): 1595–604.

 

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