|Other Names||Neutrophil cytosol factor 4, NCF-4, Neutrophil NADPH oxidase factor 4, SH3 and PX domain-containing protein 4, p40-phox, p40phox, NCF4, SH3PXD4|
|Target/Specificity||The synthetic peptide sequence used to generate the antibody AP7615b was selected from the C-term region of human NCF4. A 10 to 100 fold molar excess to antibody is recommended. Precise conditions should be optimized for a particular assay.|
|Storage||Maintain refrigerated at 2-8°C for up to 6 months. For long term storage store at -20°C.|
|Precautions||This product is for research use only. Not for use in diagnostic or therapeutic procedures.|
|Function||Component of the NADPH-oxidase, a multicomponent enzyme system responsible for the oxidative burst in which electrons are transported from NADPH to molecular oxygen, generating reactive oxidant intermediates. It may be important for the assembly and/or activation of the NADPH-oxidase complex.|
|Cellular Location||Cytoplasm, cytosol. Endosome membrane; Peripheral membrane protein; Cytoplasmic side. Membrane; Peripheral membrane protein|
|Tissue Location||Expression is restricted to hematopoietic cells|
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Provided below are standard protocols that you may find useful for product applications.
NCF4 is a cytosolic regulatory component of the superoxide-producing phagocyte NADPH-oxidase, a multicomponent enzyme system important for host defense. This protein is preferentially expressed in cells of myeloid lineage. It interacts primarily with neutrophil cytosolic factor 2(NCF2/p67-phox) to form a complex with neutrophil cytosolic factor 1 (NCF1/p47-phox), which further interacts with the small G protein RAC1 and translocates to the membrane upon cell stimulation. This complex then activates flavocytochrome b, the membrane-integrated catalytic core of the enzyme system. The PX domain of this protein can bind phospholipid products of the PI(3) kinase, which suggests its role in PI(3) kinase-mediated signaling events. The phosphorylation of this protein was found to negatively regulate the enzyme activity.
Glas,J., Seiderer,J. Am. J. Gastroenterol. 104 (3), 665-672 (2009)Honbou,K. Seikagaku 80 (8), 743-747 (2008)Dusi,S., Donini,M. Biochem. J. 314 (PT 2), 409-412 (1996)Leto,T.L. Proc. Natl. Acad. Sci. U.S.A. 91 (22), 10650-10654 (1994)
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