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Description
The neutrophil respiratory burst oxidase (NADPH-oxidase) generates superoxide and secondary oxygen-derived toxic products in response to bacteria or a variety of soluble stimuli. The active site of this enzyme is located in an integral membrane cytochrome, b558, that consists of the two subunits gp91 [phox] and p21 [phox]. Superoxide production depends on the formation of a complex that includes p67 [phox], p47 [phox], and the GTP-binding protein Rac. Upon activation, these proteins translocate from the cytosol to the membrane where they assemble with b558 and induce oxidase activity. p67 [phox] contains two SH3 domains and binds, via its C-terminal SH3 domain, to the proline rich
region of p47 [phox]. This binding allows p67 [phox] to indirectly associate with the oxidase. It is thought that the phosphorylated forms of p67 [phox] and p47 [phox] interact and that the phosphorylation of p67 [phox] is regulated by both PKC-dependent and independent pathways. Although the role of p67 [phox] in electron flow control is poorly understood, it is thought that it regulates the transfer of electrons from NADPH to reduce flavin.
Immunofluorescence, Western Blotting
Specifications
Specifications
| Antigen | p67 (phox) |
| Applications | Western Blot |
| Classification | Monoclonal |
| Clone | 29 |
| Concentration | 250μg/mL |
| Conjugate | Unconjugated |
| Formulation | Aqueous buffered solution containing BSA, glycerol, and ≤0.09% sodium azide. |
| Host Species | Mouse |
| Immunogen | Human p67 [phox] aa. 317-469 |
| Purification Method | Affinity Purified |
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Safety and Handling
For Research Use Only.
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