Neutrophil Cytosolic Factor 2 (NCF2) (AA 317-469) antibody

Antigen: Neutrophil Cytosolic Factor 2 (NCF2)

Synonyms: NCF-2, NOXA2, P67PHOX, FLJ93058, P67-PHOX, Ncf-2, p67phox, NCF2, MGC179493, MGC81877, zgc:158405, noxa2, p67-phox, MGC108334, DKFZp469H1220

Binding Site: AA 317-469

Clonality: Monoclonal (29)

Host: Mouse

Reactivity: Human

Conjugate: Un-conjugated

Application: Western Blotting (WB), Immunofluorescence (IF)

Catalog no.: ABIN968245

Additional Information

Alternative name: p67 phox

Immunogen: Human p67 [phox]

Cross-Reactivity: Mouse (Murine)

Format: Liquid

Isotype: IgG2b

Clone: 29

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.

Characteristics: 1. Since applications vary, each investigator should titrate the reagent to obtain optimal results.
2. Please refer to us for technical protocols.
3. Caution: Sodium azide yields highly toxic hydrazoic acid under acidic conditions. Dilute azide compounds in running water before discarding to avoid accumulation of potentially explosive deposits in plumbing.
4. Source of all serum proteins is from USDA inspected abattoirs located in the United States.

Molecular Weight: 67 kDa

Comments:

Related Products: ABIN968584, ABIN967389

Application Details

Concentration: 250 µg/ml

Purity: Purified

Purification: Purified from tissue culture supernatant or ascites by affinity chromatography.

Buffer: Aqueous buffered solution containing BSA, glycerol.

Preservative: 0.09% Sodium azide.

Storage: Store undiluted at -20° C.

Restrictions: For Research Use only

Images

Western blot analysis of p67 [phox] on a EB1 cell lysate (Human B lymphoblast, Burkitt's lymphoma, ATCC HTB-60). Lane 1: 1:500, lane 2: 1:1000, lane 3: 1:2000 dilution of the mouse anti-p67 [phox] antibody.

Immunofluorescence staining of C3H/10T1/2 cells (Mouse embryonic fibroblasts, ATCC CCL-226).

Publications

Product: Leto, Lomax, Volpp et al.: "Cloning of a 67-kD neutrophil oxidase factor with similarity to a noncatalytic region of p60c-src." in: Science (New York, N.Y.), Vol. 248, Issue 4956, pp. 727-30, 1990 (PubMed).

Leto, Adams, de Mendez: "Assembly of the phagocyte NADPH oxidase: binding of Src homology 3 domains to proline-rich targets." in: Proceedings of the National Academy of Sciences of the United States of America, Vol. 91, Issue 22, pp. 10650-4, 1994 (PubMed).

Freeman, Lambeth: "NADPH oxidase activity is independent of p47phox in vitro." in: The Journal of biological chemistry, Vol. 271, Issue 37, pp. 22578-82, 1996 (PubMed).

Benna, Dang, Gaudry et al.: "Phosphorylation of the respiratory burst oxidase subunit p67(phox) during human neutrophil activation. Regulation by protein kinase C-dependent and independent pathways." in: The Journal of biological chemistry, Vol. 272, Issue 27, pp. 17204-8, 1997 (PubMed).

Ago, Nunoi, Ito et al.: "Mechanism for phosphorylation-induced activation of the phagocyte NADPH oxidase protein p47(phox). Triple replacement of serines 303, 304, and 328 with aspartates disrupts the SH3 domain-mediated intramolecular interaction in p47(phox), thereby activating" in: The Journal of biological chemistry, Vol. 274, Issue 47, pp. 33644-53, 1999 (PubMed).