Anti-p22phox [44.1] Antibody
![Anti-p22phox [44.1] Antibody](https://www.kerafast.com/MediaStorage/Product/Images/Large/842_200120200126248410.jpg "Anti-p22phox [44.1] Antibody")
This IgG2 mouse mononoclonal antibody was generated against the partially purified human neutrophil flavocytochrome b (cytochrome b559 or cytochrome b558) and is reactive against human p22phox amino acids 29-33 & 183-188.
The integral membrane protein flavocytochrome b (Cyt b), a heterodimer formed by a 91-kD glycoprotein (heavy chain) and a 22-kD polypeptide (light chain), is the catalytic core of the phagocyte NADPH oxidase and generates superoxide which plays a critical role in host defense. The p22phox gene encodes the light alpha subunit which has been proposed as a primary component of the microbicidal oxidase system of phagocytes. Mutations in this gene are associated with autosomal recessive chronic granulomatous disease (CGD) that is characterized by the failure of activated phagocytes to generate superoxide, which is important for the microbicidal activity of these cells.
From the laboratory of Algirdas J. Jesaitis, PhD, Montana State University.
Part of The Investigator's Annexe program.
This IgG2 mouse mononoclonal antibody was generated against the partially purified human neutrophil flavocytochrome b (cytochrome b559 or cytochrome b558) and is reactive against human p22phox amino acids 29-33 & 183-188.
The integral membrane protein flavocytochrome b (Cyt b), a heterodimer formed by a 91-kD glycoprotein (heavy chain) and a 22-kD polypeptide (light chain), is the catalytic core of the phagocyte NADPH oxidase and generates superoxide which plays a critical role in host defense. The p22phox gene encodes the light alpha subunit which has been proposed as a primary component of the microbicidal oxidase system of phagocytes. Mutations in this gene are associated with autosomal recessive chronic granulomatous disease (CGD) that is characterized by the failure of activated phagocytes to generate superoxide, which is important for the microbicidal activity of these cells.
From the laboratory of Algirdas J. Jesaitis, PhD, Montana State University.
Part of The Investigator's Annexe program.
| Product Type: | Antibody |
| Name: | Anti-p22phox [44.1] Antibody |
| Alternative Name(s): | CYBA antibody, Cytochrome b 245 alpha polypeptide antibody, Cytochrome b 245 light chain antibody, Cytochrome b alpha polypeptide antibody, Cytochrome b(558) alpha chain antibody, Cytochrome b(558) alpha subunit antibody, Cytochrome b558 subunit alpha antibody, Flavocytochrome b 558 alpha polypeptide antibody, Neutrophil cytochrome b 22 kDa polypeptide antibody, p22 phagocyte B-cytochrome antibody, p22-phox antibody, p22phox antibody, Superoxide-generating NADPH oxidase light chain subunit antibody |
| Accession ID: | P13498 |
| Molecular Weight: | 21 kDa |
| Isotype: | IgG2 |
| Clonality: | Monoclonal |
| Clone Name: | 44.1 |
| Reactivity: | Human |
| Specificity: | Human p22phox |
| Immunogen: | Partially purified human neutrophil flavocytochrome b (heparin Ultrogel/lectin affinity purification - in Triton X-100) |
| Species Immunized: | Mouse |
| Myeloma Used: | Sp2/0 |
| Epitope: | 29-TAGRF-33 & 183-PQVNPI-188 |
| Purification Method: | Protein G |
| Buffer: | 0.1M Sodium Phosphate, pH 7.4, 0.15M NaCl, 0.05% (w/v) Sodium Azide |
| Tested Applications: | WB (1:1000) |
| Storage: | -20C |
| Shipped: | Cold packs |
Specificity of mAb for cytochrome b and phage pIII proteins. Intact phage expressing known amino acid sequences (lanes B, C, E, and F) and partially purified cytochrome b (lanes A and D) were separated on SDS-PAGE polyacrylamide gels and transferred to nitrocellulose. Samples were Western blotted with mAb 54.1 (lanes A-C) or mAb 44.1 (lanes D-F). Lanes B and F contain proteins of phage sequence 3 (PQVRPI), and lanes C and E contain proteins of phage sequence 27 (FKRGVD.
Adapted from: Burritt, J.B. et al. J.Biol.Chem. 270:16974-16980, 1995.
- Burritt, J.B., Quinn, M.T., Jutila, M.A., Bond, C.W. and Jesaitis, A.J. Topological mapping of neutrophil cytochrome b epitopes with phage display libraries. J.Biol.Chem. 270:16974-16980, 1995.
- Burritt, J.B., Busse, S.C., Gizachew, D., Siemsen, D.W., Quinn, M.T., Bond, C.W., Dratz, E.A. and Jesaitis, A.J. Antibody imprint of a membrane protein surface: Phagocyte Flavocytochrome b. J Biol. Chem., 273:24847-52, 1998.
- Taylor, R.M. Jesaitis, A.J Immunoaffinity purification of human phagocyte flavocytochrome b and analysis of conformational dynamics. Methods Mol Biol. 2007;412:429-37, 2007.
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