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Recombinant Human NOX2 Protein

Nori Human IL-9 ELISA Kit
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DataSheet   

The recombinant human NOX2 protein is derived from in vivo expression of human NOX2 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 NOX2: NADPH oxidase 2 (Nox2), cytochrome b(558) subunit beta, Cytochrome b-245 heavy chain

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 NOX2 Protein Summary

Alternative names for NOX2: NADPH oxidase 2 (Nox2), cytochrome b(558) subunit beta, Cytochrome b-245 heavy chain

 

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 NOX2.
Accession # P04839
N-Terminal Sequence Analysis Ser
Amino Acid Sequence Ser475-Phe570
Predicted Molecular Mass 26 kDa
SDS-PAGE 26 kDa, reducing conditions

 

Background: 

NADPH oxidase 2 (Nox2), also known as cytochrome b(558) subunit beta or Cytochrome b-245 heavy chain, is a protein that in humans is encoded by the NOX2 gene (also called CYBB gene).[1] The protein is a super-oxide generating enzyme which forms reactive oxygen species (ROS). Nox2 is composed of cytochrome b alpha (CYBA) and beta (CYBB) chain and contains an N-terminal transmembrane domain that binds two heme groups, and a C-terminal domain that is able to bind to FAD and NADPH.[2] Nox2 is the catalytic, membrane-bound subunit of NADPH oxidase. It is inactive until it binds to the membrane-anchored p22phox, forming the heterodimer known as flavocytochrome b558.[3] After activation, the regulatory subunits p67phox, p47phox, p40phox and a GTPase, typically Rac, are recruited to the complex to form NADPH oxidase on the plasma membrane or phagosomal membrane.[4]  Nox2 may play an important role in atherosclerotic lesion development in the aortic arch, thoracic, and abdominal aorta.[5][6] Nox2 may play a role in determining the size of a myocardial infarction due to its connection to ROS, which play a role in myocardial reperfusion injury. This was a result of the relation between Nox2 and signaling necessary for neutrophil recruitment.[7] Furthermore, it increases global post-reperfusion oxidative stress, likely due to decreased STAT3 and Erk phosphorylation.[7] In addition, it appears that hippocampal oxidative stress is increased in septic animals due to the actions of Nox2.[8] Nox2 may also plays an important role in angiotensin II-mediated inward remodelling in cerebral arterioles due to the emittance of superoxides from Nox2-containing NADPH oxidases.[9] CYBB transcript levels are upregulated in the lung parenchyma of smokers. [10]

References

1.     Royer-Pokora,B., et al. (1986) Nature 322 (6074), 32-38.

2.     Aguirre, Jesús; Lambeth, J (2010). Free Radical Biology and Medicine. 49 (9): 1342–1353.

  1. Hervé C, et al. (2006). Current Genetics. 49(3): 190–204.
  2. Kawahara T, Lambeth JD (2007). BMC Evolutionary Biology. 7: 178.
  3. Sorescu, D; et al. (2002). Circulation. 105 (12): 1429–35.
  4. Chaubey, S; et al. (2013). PLOS ONE. 8 (2): e54869. doi:1371/journal.pone.0054869.
  5. Braunersreuther V, et al. (2013). Journal of Molecular and Cellular Cardiology. 64: 99–107.
  6. Hernandes MS, et al. (2014). J Neuroinflammation. 11 (1): 36. doi:1186/1742-2094-11-36.
  7. Chan SL, Baumbach GL (2013). Frontiers in Physiology. 4: 133.
  8. Pintarelli G, et al. (2019). Scientific Reports. 9 (1): 13039. doi:1038/s41598-019-49648-2.

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