Use your antibodies-online credentials, if available.
No Products on your Comparison List.
Your basket is empty.
Find out more
Myeloperoxidase (MPO) is a heme protein synthesized during myeloid differentiation that constitutes the major component of neutrophil azurophilic granules. Additionally we are shipping Myeloperoxidase Antibodies (597) and Myeloperoxidase Kits (100) and many more products for this protein.
Showing 10 out of 50 products:
When infiltrated with Candida albicans, smu681 myeloperoxidase-deficient embryos and sibling embryos showed similar survival. Proliferation of C. albicans was more rapid in smu681 embryos than in sibling embryos, although it was eventually suppressed.
mpx expression is controlled differently in the anterior lateral plate mesoderm and posterior lateral plate mesoderm regions and describe novel roles for etv2 (show ETV2 Proteins) and gata1 (show GATA1 Proteins) during primitive neutropoiesis.
myeloperoxidase and H2O2 interact directly within neutrophils at the tissue wound
Study demonstrated the possibility of biodegradation of fullerene molecule using the human neutrophil enzyme myeloperoxidase, which leads to the formation of non-aromatic compounds and to the loss of the fullerene molecule topology
High expression of MPO is associated with cardiovascular complications.
Short-term atorvastatin therapy resulted in lipid lowering and anti-inflammatory activity in patients after AMI (show CFD Proteins), independently of its effect on MPO gene expression
MPO levels were positively associated with obesity. MPO levels were positively associated with obesity indices (BMI z-score, WHtR and %BFM). Higher MPO levels were associated with higher mean arterial pressure, with nondipping and with insulin (show INS Proteins) resistance.
High serum levels of MPO were observed in obese individuals with hs-CRP (show CRP Proteins) above 3 mg/L, which is a classic biomarker for inflammation and cardiovascular risk
Myeloperoxidase gene polymorphism showed protective effect in Russian population diagnosed with essential hypertension.
The investigated MPO gene polymorphism is not associated with risk for the development of cervical intraepithelial neoplasia.
Myeloperoxidase and eosinophil peroxidase (show EPX Proteins) are readily internalized by HUVEC cells where they promote cellular proliferation, migration, invasion, and stimulate angiogenesis both in vitro and in vivo.
People with myeloperoxidase 463G>A polymorphisms (AA genetic type) may have decreased lung cancer risk under dominant genetic model (meta-analysis).
concentrations of the C-reactive protein, myeloperoxidase and soluble CD40 ligand taken from peripheral vein were closely similar to the concentration found in coronary blood of ACS patients
lung MPO activity increased following induction of sepsis with CLP while siRNA treatment significantly reduced MPO activity. Liver and lung cytokine and chemokine levels in CLP-induced sepsis reduced following treatment with siRNA. These findings show a crucial pro-inflammatory role for H2S synthesized by CSE in macrophages in sepsis and suggest CSE gene silencing with siRNA as a potential therapeutic approach for this co
MPO deficiency upregulates the expression of several proinflammatory cytokines and chemokines in mouse neutrophils
Myeloperoxidase may be an important determinant of diet and inflammation on colon cancer risk via its effect on endogenous exposure to oxidants and acrolein.
Alkalinity of neutrophil phagocytic vacuoles is modulated by HVCN1 (show HVCN1 Proteins) and has consequences for myeloperoxidase activity.
ethanol catabolism in renal tubules results in a self-perpetuating cycle of CYP2E1 (show CYP2E1 Proteins) induction, local PTAFR (show PTAFR Proteins) ligand formation, and neutrophil infiltration and activation that leads to myeloperoxidase-dependent oxidation and damage to kidney function.
These findings suggest that myeloperoxidase may contribute importantly to formation and rupture of CA.
Myeloperoxidase binds to RBC (show CACNA1C Proteins) membranes in vitro and in vivo, is transported by RBCs (show SSU1 Proteins) to remote sites, and affects endothelial function as well as systemic vascular resistance.
MPO knockout mice were protected from high fat diet-enhanced body weight gain and insulin (show INS Proteins) resistance. Lack of MPO also attenuated HFD-induced macrophage infiltration and expression of proinflammatory cytokines.
these results demonstrate that MPO deficiency ameliorates renal injury in the renal ablation model of chronic kidney disease in mice.
MPO contributes to the development of arthritis despite suppressing adaptive immunity in secondary lymphoid organs. This suggests distinct effects of local MPO on arthritogenic effector responses.
the role of leukocyte activation, leukocyte-derived MPO and MPO-generated oxidants on BBB function
Cycles presenting hyperedema weren't associated with high concentration of myeloperoxidase, intraluminal fluid, or positive cytology, making it a poor diagnostic tool of endometritis.
The analysis of synovial fluid MPO can be used as a complementary test to aid in the discrimination between infectious and noninfectious joint disease, especially when the white blood cell counts and the total protein level are inconclusive.
Results show the possibility of isolating neutrophil elastase (show ELANE Proteins) and myeloperoxidase from the same blood sample with a sufficient yield and purity for future studies on their implication and interaction during inflammatory diseases.[elastase]
Slight elevation of MPO activity in the synovial fluid of horses with osteoarthritis and chronic non-septic arthritis, but greater elevation in septic arthritis.
Myeloperoxidase (MPO) is a heme protein synthesized during myeloid differentiation that constitutes the major component of neutrophil azurophilic granules. Produced as a single chain precursor, myeloperoxidase is subsequently cleaved into a light and heavy chain. The mature myeloperoxidase is a tetramer composed of 2 light chains and 2 heavy chains. This enzyme produces hypohalous acids central to the microbicidal activity of netrophils.
, eosinophil peroxidase