Recombinant Mouse Myeloperoxidase (Mpo)

Code CSB-YP014757MO
MSDS
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Source Yeast
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Code CSB-EP014757MO
MSDS
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Source E.coli
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Code CSB-EP014757MO-B
MSDS
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Source E.coli
Conjugate Avi-tag Biotinylated
E. coli biotin ligase (BirA) is highly specific in covalently attaching biotin to the 15 amino acid AviTag peptide. This recombinant protein was biotinylated in vivo by AviTag-BirA technology, which method is BriA catalyzes amide linkage between the biotin and the specific lysine of the AviTag.
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Code CSB-BP014757MO
MSDS
Size Pls inquire
Source Baculovirus
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Code CSB-MP014757MO
MSDS
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Source Mammalian cell
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Product Details

Purity
>85% (SDS-PAGE)
Target Names
Mpo
Uniprot No.
Alternative Names
Mpo; Myeloperoxidase; MPO; EC 1.11.2.2) [Cleaved into: Myeloperoxidase light chain; Myeloperoxidase heavy chain]
Species
Mus musculus (Mouse)
Expression Region
139-718
Target Protein Sequence
VT CPPNDKYRTI TGHCNNRRSP TLGASNRAFV RWLPAEYEDG VSMPFGWTPG VNRNGFKVPL ARQVSNAIVR FPNDQLTKDQ ERALMFMQWG QFLDHDITLT PEPATRFSFF TGLNCETSCL QQPPCFPLKI PPNDPRIKNQ KDCIPFFRSC PACTRNNITI RNQINALTSF VDASGVYGSE DPLARKLRNL TNQLGLLAIN TRFQDNGRAL MPFDSLHDDP CLLTNRSARI PCFLAGDMRS SEMPELTSMH TLFVREHNRL ATQLKRLNPR WNGEKLYQEA RKIVGAMVQI ITYRDYLPLV LGPAAMKKYL PQYRSYNDSV DPRIANVFTN AFRYGHTLIQ PFMFRLNNQY RPTGPNPRVP LSKVFFASWR VVLEGGIDPI LRGLMATPAK LNRQNQIVVD EIRERLFEQV MRIGLDLPAL NMQRSRDHGL PGYNAWRRFC GLPQPSTVGE LGTVLKNLEL ARKLMAQYGT PNNIDIWMGG VSEPLEPNGR VGQLLACLIG TQFRKLRDGD RFWWENPGVF SKQQRQALAS ISLPRIICDN TGITTVSKNN IFMSNTYPRD FVSCNTLPKL NLTSWKET
Protein Length
Full Length of Mature Protein
Tag Info
Tag type will be determined during the manufacturing process.
The tag type will be determined during production process. If you have specified tag type, please tell us and we will develop the specified tag preferentially.
Form
Lyophilized powder
Note: We will preferentially ship the format that we have in stock, however, if you have any special requirement for the format, please remark your requirement when placing the order, we will prepare according to your demand.
Buffer before Lyophilization
Tris/PBS-based buffer, 6% Trehalose, pH 8.0
Reconstitution
We recommend that this vial be briefly centrifuged prior to opening to bring the contents to the bottom. Please reconstitute protein in deionized sterile water to a concentration of 0.1-1.0 mg/mL.We recommend to add 5-50% of glycerol (final concentration) and aliquot for long-term storage at -20℃/-80℃. Our default final concentration of glycerol is 50%. Customers could use it as reference.
Troubleshooting and FAQs
Storage Condition
Store at -20°C/-80°C upon receipt, aliquoting is necessary for mutiple use. Avoid repeated freeze-thaw cycles.
Shelf Life
The shelf life is related to many factors, storage state, buffer ingredients, storage temperature and the stability of the protein itself.
Generally, the shelf life of liquid form is 6 months at -20°C/-80°C. The shelf life of lyophilized form is 12 months at -20°C/-80°C.
Lead Time
Delivery time may differ from different purchasing way or location, please kindly consult your local distributors for specific delivery time.
Note: All of our proteins are default shipped with normal blue ice packs, if you request to ship with dry ice, please communicate with us in advance and extra fees will be charged.
Notes
Repeated freezing and thawing is not recommended. Store working aliquots at 4°C for up to one week.
Datasheet
Please contact us to get it.

Customer Reviews and Q&A

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Target Background

Function
Part of the host defense system of polymorphonuclear leukocytes. It is responsible for microbicidal activity against a wide range of organisms. In the stimulated PMN, MPO catalyzes the production of hypohalous acids, primarily hypochlorous acid in physiologic situations, and other toxic intermediates that greatly enhance PMN microbicidal activity.
Gene References into Functions
  1. Severe clinical and pathological disease is associated with the induction of anti-MPO IgG/LPS-mediated glomerulonephritis. PMID: 28186568
  2. These studies further support involvement of MPO-catalyzed oxidative processes in both the development of atherosclerosis and diabetes risk PMID: 28069522
  3. Neutrophils are abundant in abdominal aortic aneurysm (AAA), and myeloperoxidase (MPO), prominently expressed in neutrophils, is associated with AAA. taurine, which can scavenge MPO-generated oxidants, can prevent AAA formation. PMID: 28971841
  4. PTX3 attenuates the production of murine myeloperoxidase-anti-neutrophil cytoplasmic antibody induced by aluminum salt adjuvant. PMID: 28850023
  5. There is a smaller number of MPO positive neutrophils in the inflammatory infiltrate of a resistant model of amoebic liver abscess. PMID: 28796788
  6. thisa study shows that neutrophil myeloperoxidase plays a paradoxical role in bacterial clearance and tissue damage in pneumococcal acute otitis media PMID: 28359218
  7. 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 PMID: 26949091
  8. MPO deficiency upregulates the expression of several proinflammatory cytokines and chemokines in mouse neutrophils PMID: 26573963
  9. Myeloperoxidase may be an important determinant of diet and inflammation on colon cancer risk via its effect on endogenous exposure to oxidants and acrolein. PMID: 26262998
  10. Alkalinity of neutrophil phagocytic vacuoles is modulated by HVCN1 and has consequences for myeloperoxidase activity. PMID: 25885273
  11. ethanol catabolism in renal tubules results in a self-perpetuating cycle of CYP2E1 induction, local PTAFR ligand formation, and neutrophil infiltration and activation that leads to myeloperoxidase-dependent oxidation and damage to kidney function. PMID: 26003521
  12. These findings suggest that myeloperoxidase may contribute importantly to formation and rupture of CA. PMID: 25922506
  13. Myeloperoxidase binds to RBC membranes in vitro and in vivo, is transported by RBCs to remote sites, and affects endothelial function as well as systemic vascular resistance. PMID: 24976018
  14. MPO knockout mice were protected from high fat diet-enhanced body weight gain and insulin resistance. Lack of MPO also attenuated HFD-induced macrophage infiltration and expression of proinflammatory cytokines. PMID: 25024373
  15. these results demonstrate that MPO deficiency ameliorates renal injury in the renal ablation model of chronic kidney disease in mice. PMID: 24990898
  16. 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. PMID: 24757143
  17. data suggest that the conversion of exogenous HE to 2-Cl-E(+) may be a useful selective and sensitive marker for MPO activity in addition to 3-Cl-Tyr. PMID: 24436331
  18. the role of leukocyte activation, leukocyte-derived MPO and MPO-generated oxidants on BBB function PMID: 23691142
  19. Data suggest that expression of Mpo in kidney is significantly correlated with severity of kidney damage in a mouse model of type 2 diabetes. PMID: 23268804
  20. Neu-164 and Neu-107, two novel antioxidant and anti-myeloperoxidase compounds, inhibit acute cigarette smoke-induced lung inflammation. PMID: 23686858
  21. Data indicate that myeloperoxidase-specific anti-neutrophil cytoplasmic antibodies (MPO-ANCA) induces injury via both humoral and cell mediated immune mechanisms. PMID: 23665205
  22. The role of genetics in myeloperoxidase -antineutrophil cytoplasmic autoantibodies necrotizing and crescentic glomerulonephritis severity was investigated using 13 inbred mouse strains. PMID: 23384999
  23. MPO, via its catalytic activity, inhibits the generation of adaptive immunity by suppressing dendritic cell activation, antigen uptake/processing, and migration to lymph nodes to limit pathological tissue inflammation. PMID: 23509155
  24. ceruloplasmin should provide a protective shield against inadvertent oxidant production by myeloperoxidase during inflammation PMID: 23306200
  25. The immunodominant myeloperoxidase T-cell epitope induces local cell-mediated injury in antimyeloperoxidase glomerulonephritis. PMID: 22955884
  26. MPO exacerbated secondary injury and impaired the functional recovery by generating strong oxidant HOCl, and enhancing neutrophil infiltration after spinal cord injury. PMID: 22322369
  27. Results provide evidence for the participation of myeloperoxidase (MPO) - one of the key-orchestrators of inflammatory response. PMID: 22479306
  28. The present study suggests that myeloperoxidase-mediated OCl(-) generation affects claudin molecules and leads to protein leakage and viral spread as a damage factor in influenza-induced acute respiratory distress syndrome. PMID: 22211924
  29. Green tea extract attenuates NADPH oxidase activity and the expression of myeloperoxidase and inducible nitric oxide synthase in ob/ob mice, thereby suppressing oxidative and nitrative modifications that otherwise lead to liver injury. PMID: 21543212
  30. MPO has dual functionality under rotenone-exposed conditions, playing a critical regulatory role in modulating pathological and protective events in the brain PMID: 21704008
  31. MPO is susceptible to the free radicals it generates, and this Achilles' heel of the enzyme can be exploited to block oxidative stress during inflammation. PMID: 21880720
  32. Rosiglitazone inhibits MPO secretion in RAW264.7 cells. PMID: 19778788
  33. Given MPO's affinity to both the endothelial and the leukocyte's surface, MPO evolves as a mediator of PMN recruitment because of its positive surface charge. PMID: 20980678
  34. Data indicate that myeloperoxidase contributes to the reduced reverse cholesterol transport observed during acute phase responses. PMID: 20061576
  35. myeloperoxidase is responsible for protein nitration and cardiomyocyte apoptosis in nonlethal traumatic mice. PMID: 20153732
  36. Contribution of myeloperoxidase to coronary artery vasculitis associated with MPO-ANCA production. PMID: 11831441
  37. MPO and NADPH-oxidase are equally important for early host defense against a large inoculum of Candida. PMID: 12085336
  38. MPO was observed to modulate the vascular signaling and vasodilatory functions of nitric oxide (NO) during acute inflammation PMID: 12089442
  39. Data show that myeloperoxidase and plasminogen activator inhibitor 1 play a critical role in the left ventricular response immediately after myocardial infarction. PMID: 12615902
  40. the MPO/H2O2 system has a role in up-regulating the catalytic activity of iNOS that occurs at sites of inflammation PMID: 14657339
  41. In knockout mice, suppressed MPO-derived oxidative/nitrative stress is associated with enhanced lung inflammation and persistent alveolar epithelial injury. PMID: 15020295
  42. Role of MPO in cellular immunity to fungi and bacteria in MPO knockout and chronic granulomatous disease mice. PMID: 15507755
  43. Compelling evidence is provided that susceptibility to infection with Gram-negative Klebsiella pneumoniae is enhanced in myeloperoxidase-deficient mice. PMID: 15661916
  44. mechanical loading activates neutrophil-mediated lysis of muscle cells through an MPO-dependent pathway PMID: 15790660
  45. aberrant MPO-antineutrophil cytoplasmic autoantibody production was exclusively controlled by Man-1 PMID: 16517735
  46. data suggest a major role of myeloperoxidase in the immunological defence to Cryptococcus neoformans infection PMID: 16914663
  47. myeloperoxidase is regulated by LXR and PPARalpha ligands PMID: 16956579
  48. Along with the activation of AMPD3, ischemia-reperfusion-induced lung inflammation is associated with increased MPO activity and TNF-alpha level. PMID: 17384464
  49. These results are consistent with the notion that nitric oxide and MPO contribute in liver tissue lipid peroxidation in peritonitis. PMID: 17901846
  50. blood myeloperoxidase is increased and myeloperoxidase-positive neutrophils develop in atherosclerotic lesions in LDLR-/- mice PMID: 17991873

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Subcellular Location
Lysosome.
Protein Families
Peroxidase family, XPO subfamily
Database Links
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