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Mouse Monoclonal anti-HIF-1 alpha (H1alpha67) | Novus Biologicals antibody product information
CatalogCode:NB100-123SS
ProductName:HIF-1 alpha Antibody
Product Description:Mouse Monoclonal anti-HIF-1 alpha (H1alpha67)
Clone:H1alpha67
Clonality:Monoclonal
Immunogen:Fusion protein containing amino acids 432-528 of human HIF-1alpha
Specificity:This antibody is specific for HIF-1alpha.
CrossReactivity:Recognizes human, sheep, mouse, rat, pig, bovine and ferret HIF-1 alpha.
Packaging:0.025 ml protein G purified Mouse ascites.
Uses:By Western blot, recognizes bands at 120kDa representing HIF-1 alpha in induced tissues and cells. Multiple bands may be seen at 120kDa representing post-translational modification. Can also be used for immunohistochemistry detection of human HIF-1alpha. The investigator should determine the optimal working dilution for a specific application.
Localization:HIF-1 is a nuclear protein that activates gene transcription in response to reduced cellular O2 concentration. Activates transcription of EPO, VEGF, iNOS, heme oxygenase 1 and other critical intracellular responses to hypoxia.
Background:Hypoxia contributes significantly to the pathophysiology of major categories of human disease, including myocardial and cerebral ischemia, cancer, pulmonary hypertension, congenital heart disease and chronic obstructive pulmonary disease. HIF-1 is a nuclear protein involved in mammalian oxygen homeostasis. This occurs as a posttranslational modification by prolyl hydroxylation. HIF-1 is a heterodimer composed of HIF-1 alpha and HIF-1 beta subunits. Both subunits are constantly translated. However, under normoxic conditions, human HIF-1 alpha is hydroxylated at Pro402 or Pro564 by a set of HIF prolyl hydroxylases, is polyubiquinated, and eventually degraded in proteosomes. Under hypoxic conditions, the lack of hydroxylation prevents HIF degradation and increases transcriptional activity. Therefore, the concentration of HIF-1 alpha increases in the cell. In contrast, HIF-1 beta remains stable under either condition. HIF hydroxylases provide insight into hypoxic cell responses, which may be used to help isolate therapeutic targets.
Storage:Store at 4C. Avoid freeze thaw cycles.
Purity:protein G purified
Isotype:IgG2b
Host_Name:Mouse
Buffer:PBS
ListPrice:100
NovusRef:1. An, H.-J., et al. (2006) Activation of Ras Up-regulates Pro-apoptotic BNIP3 in Nitric Oxide-induced Cell Death, 281, 33939-33948. 2. Burke, B., et al. Hypoxia-induced gene expression in human macrophages: Implications for ischemic tissues and hypoxia-regulated gene therapy. Amer. J. of Pathology. 163(4):1233-1242, 2003. (Immunohistochemistry, human) 3. de Candia, P., et al. Angiogenesis impariment in Id-deficient mice cooperates with an Hsp90 inhibitor to completely supress HER2/neu-dependent breast tumors. PNAS. 100(21):12337-12342, 2003. (Immunohistochemistry-paraffin, mouse) 4. Duyndam, M.C.A., et al. Induction of vascular endothelial growth factor expression and hypoxia-inducible factor 1a protien by the oxidative stressor arsenite. J. Biol. Chem. 276(51):48066-48076, 2001. (Western blot, human) 5. Franco, M., et al. Targeted Anti-Vascular Endothelial Growth Factor Receptor-2 Therapy Leads to Short-term and Long-term Impairment of Vascular Function and Increase in Tumor Hypoxia. Cancer Res 2006; 66: (7), 2006. 6. Fujii, T., et al. Effect of hypoxia on human seminoma cells. Int. J. Oncology. 20:955-962, 2002. (Immunocytochemistry, human) 7. Khan, Z., et al. (2006) Peroxisomal Localization of Hypoxia-Inducible Factors and Hypoxia-Inducible Factor Regulatory Hydroxylases in Primary Rat Hepatocytes Exposed to Hypoxia-Reoxygenation. 169: 1251-1269. 8. Laderoute, K. R., et al. (2006) 5Prime-AMP-Activated Protein Kinase (AMPK) Is Induced by Low-Oxygen and Glucose Deprivation Conditions Found in Solid-Tumor Microenvironments, 26, 5336-5347. 9. Lu, H., et al. Reversible inactivation of HIF-1 prolyl hydroxylases allows cell metabolism to control basal HIF-1. J. Biol. Chem. 280:41928-41939, 2005. 10. Mandiota, S.J., et al. HIF activation identifies early lesions in VHL kidneys: Evidence for site-specific tumor supressor function in the nephron. Cancer Cell. 1:459-468, 2002. (Immunohistochemistry, human) 11. Ramanathan, Madhuri, et al. Synergistic Up-Regulation of Vascular Endothelial Growth Factor (VEGF) Expression in Macrophages by Adenosine A2A Receptor Agnosts and Endotoxin Involves Transcriptional Regulation via the Hypoxia Response Element (HRE) in the VEGF Promoter. Mol. Biol. Cell. 10.1091/mbc.E06-07-0596, 2006. 12. Tang, T., et al. Phosphorylation by mitogen-activated protein kinase mediates the hypoxia-induced turnover of the TAL1-SCL transcription factor in endothelial cells. J. Biol. Chem. 277(21):18365-18372, 2002. (Western blot, human) 13. Zhong, H., et al. Can. Res. 59:5830-5835, 1999. (Immunohistochemistry-paraffin, mouse/human) 14. Khan, Aahida., et al. Gastrointestinal, gepatobiliary and pancreatic pathology: Peroxisomal Localization of Hypoxia-Inducible Factors and Hypoxia Inducible Factor Regulatory Hydroxylases in Primary Rat Hepatocytes Exposed to Hypoxia-Reoxygenation. 169: 1251-1269, 2006. 15. Ramanathan, Madhuri., et al. Synergistic Up-Regulation of Vascular Endothelial Growth Factor (VEGF) Expression in Macrophages by Adenosine A2A Receptor Agonists and Endotoxin Involves Transcriptional Regulation via the Hypoxia Response Element (HRE) in the VEGF Promoter. 10.1091/mbc.E06-07-0596, 2006. 16.An, Hyun-Jung., et al. Mechanisms of Signal Transduction: Activation of ras up-regulates pro-apoptotic BNIP2 in nitric oxideinduced cell death. 281: 33939-33948, 2006. 17. Yamamoto, Y., et al. Hypoxia-inducible factor 1alpha is closely linked to an aggressive phenotype in breast cancer. Breast Cancer Res Treat. DOI 10.1007/s10549-007-9742-1. 18. Tracy, K., B. C. Dibling, et al. (2007). BNIP3 Is an RB/E2F Target Gene Required for Hypoxia-Induced Autophagy. 27: 6229-6242. 19. Tacchini, L., et al. Hepatocyte growth factor signalling stimulates hyposia inducible factor-1 (HIF-1) activity in HepG2 hepatoma cells. Carcinogenesis, 22: 1363-1371 2001 20. Klatte, T., et al. Imaging, Diagnosis, Prognosis: Hypoxia-Inducible Factor 1alpha in Clear Cell Renal Cell Carcinoma. Clin. Cancer Res., 13: 7388-7393, 2007 21. Rosenberger C, Rosen S, Shina A, et al. Activation of hypoxia inducible factors (HIF) ameliorates hypoxic distal tubular injury in the isolated perfused rat kidney. Nephrol Dial Transplant. May 29, 2008:gfn276. 22. Radek KA, Kovacs EJ, Gallo RL, DiPietro LA. Acute Ethanol Exposure Disrupts VEGF Receptor Cell Signaling in Endothelial Cells. Am J Physiol Heart Circ Physiol. May 9, 2008:00699.2007.
AppSummary:IHC, WB
SpeciesSummary:Bv, Hu, Mu, Rt, Ft, Sh, Po
ALTnames:anti-Hypoxia-inducible factor 1 alpha antibody; anti-HIF1 alpha antibody; anti-ARNT interacting proteinantibody; anti-Hif1a antibody; anti-ARNT interacting protein antibody; anti-HIF-1alpha antibody; anti-Hypoxia inducible factor 1 alpha antibody; anti-Hypoxia inducible factor 1 alpha subunit basic helix antibody
ProteinTarget:HIF-1 alpha
PackageSize:0.025 ml
NotesMain:This antibody has demonstrated varying results in Western blot applications. Product NB100-105 is recommended for most Western blot experiments. You may use COS-7 treated and untreated nuclear extracts for your positive and negative controls for hypoxic upregulation, NB800-PC26. A good positive control for IHC is glioblastoma multiforme. * The mobility of HIF-1 alpha induced by desferrioxamine or cobalt chloride treatment differs from the mobility of the hypoxia-induced protein. The reason is not known.
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Also see:
all rat Hif1a antibodies
all human HIF1A antibodies
all mouse Hif1a antibodies
anti mouse secondary antibodies


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