Anti-Nitric Oxide Synthase [3F7-B11-B5] Antibody
This mouse IgM antibody was generated against purified, bovine cerebellum NOS and recognizes the ~130 kDa iNOS protein, the ~155 kDa bNOS protein, and the ~140 kDa eNOS protein.
Nitric oxide (NO) has a broad range of biological activities and is implicated in signaling pathways in phylogenetically diverse species. Nitric oxide synthases (NOS), the enzymes responsible for synthesis of NO, are homodimers whose monomers are themselves two fused enzymes: a cytochrome reductase and a cytochrome that requires three cosubstrates (L-arginine, NADPH and O2) and five cofactors or prosthetic groups (FAD, FMN, calmodulin, tetrahydrobiopterin and heme).
From the laboratory of Roger A. Johns, MD, University of Virginia.
This mouse IgM antibody was generated against purified, bovine cerebellum NOS and recognizes the ~130 kDa iNOS protein, the ~155 kDa bNOS protein, and the ~140 kDa eNOS protein.
Nitric oxide (NO) has a broad range of biological activities and is implicated in signaling pathways in phylogenetically diverse species. Nitric oxide synthases (NOS), the enzymes responsible for synthesis of NO, are homodimers whose monomers are themselves two fused enzymes: a cytochrome reductase and a cytochrome that requires three cosubstrates (L-arginine, NADPH and O2) and five cofactors or prosthetic groups (FAD, FMN, calmodulin, tetrahydrobiopterin and heme).
From the laboratory of Roger A. Johns, MD, University of Virginia.
| Product Type: | Antibody |
| Accession ID: | P29475 |
| Isotype: | IgM |
| Clonality: | Monoclonal |
| Clone Name: | 3F7-B11-B5 |
| Specificity: | Recognizes the ~130 kDa iNOS protein, the ~155 kDa bNOS protein, and the ~140 kDa eNOS protein |
| Immunogen: | Generated against purified, bovine cerebellum NOS |
| Species Immunized: | Mouse |
| Tested Applications: | WB, IHC |
| Storage: | -20C |
| Shipped: | Cold packs |
Western blot analysis of nitric oxide synthase (NOS) with anti-NOS antibody. Partially purified constitutive NOSs from bovine cerebellum (lanes 1 and 2, each 1 ug) and cultured aortic endothelial cells (lane 3, 1 ug) and inducible NOS from interferon-y- and linonolvsaccharides- (LPS) stimulated cultured RAW 264.7 macrophages” (lane 4, 1 ug) were fractionated by SDS-polyacrylamide gel electrophoresis. Proteins were then electrophoretically transferred to a nitrocellulose membrane and immunodetected with culture supernatant (anti-NOS antibody) from hybridoma cells. In lane 2, anti-NOS antibody was preblocked with excess NO synthase. Position of various molecular mass markers is shown on left. Arrows indicate cerebellum (150 kDa) and endothelial and macrophage (130 kDa) NO synthases.
Adapted from: Rengasamy A, Xue C, and Johns RA. Immunohistochemical demonstration of a paracrine role of nitric oxide in bronchial function. 267(6 Pt 1):L704-L711, (1994).
- Rengasamy A, Xue C, and Johns RA. Immunohistochemical demonstration of a paracrine role of nitric oxide in bronchial function. 267(6 Pt 1):L704-L711, (1994).
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