epitope corresponding to amino acids 121-195 of Mox1 of human origin
Modification Notes
Mox1 and the glycoprotein gp91 phox are largely related proteins that are essential components of the NADPH oxidase (1). The superoxide-generating NADPH oxidase is present in phagocytes, neuroepithelial bodies, vascular smooth muscle cells, and endothelial cells (2). It includes a membrane-bound flavocytochrome containing two subunits, gp91 phox and p22 phox, and the cytosolic proteins p47 phox and p67 phox (3). During activation of the NADPH oxidase, p47 phox and p67 phox migrate to the plasma membrane where they associate with the flavocytochrome, cytochrome b558, to form the active enzyme complex (4). The p22 and gp91 phox subunits also function as surface O2 sensors that initiate cellular signaling in response to hypoxic conditions (5). Mox1 and gp91 contain identical C-terminal sequence identity, yet they have distinct expression patterns. gp91 phox is expressed in eosinophils, neutrophils, monocytes, and B-lymphocytes, whereas Mox1 is predominantly detected in the colon, and low expression is also detected in the uterus and prostate (1,6). Mox1 is also upregulated in vascular smooth-muscle cells in response to PDGF stimulation, which collectively indicates that Mox1 may function analogously to gp91 phox, yet regulate the NADPH superoxide production in non-phagocytic cells (7).
Key Feature
Clonality
Polyclonal
Isotype
IgG
Host Species
Rabbit
Tested Applications
WBIPIFIHCELISA
recommended for detection of Mox1 of mouse, rat and human origin by WB, IP, IF, IHC(P) and ELISA:
Species Reactivity
HumanMouseRat
Concentration
1mg/ml
Purification
Affinity purified
Target Information
Alternative Names
epitope corresponding to amino acids 121-195 of Mox1 of human origin
Tissue Specificity
epitope corresponding to amino acids 121-195 of Mox1 of human origin