HIF-1α (C-Term) Polyclonal Antibody

Hypoxia-inducible factor-1α (HIF-1α) is a transcription factor that accumulates under low-oxygen conditions.^1,2 Following hypoxic stimulus and cytoplasmic accumulation, HIF-1α migrates to the nucleus where with other transcription factors, it drives the production of stress-adaptive proteins. This response is essential for maintenance of normal oxidative physiology, however overexpression in cancer cells promotes tumor survival.^2,3,4,5,6 HIF-1α is an endothelial PAS domain protein 1 (EPAS-1) family member with phosphorylation dependent activities.^7,8 Cayman Chemical’s HIF-1α polyclonal antibody can be used for WB analysis for HIF-1α on samples from human, mouse, and simian. It is not suitable for ICC or IP. Other applications for use of this antibody have not yet been tested.

WARNING This product is not for human or veterinary use.

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7. Richard, D.E., Berra, E., Gothié, E., et al. p42/p44 Mitogen-activated protein kinases phosphorylate hypoxia-inducible factor 1α (HIF-1α) and enhance the transcriptional activity of HIF-1. The Journal of Biological Chemisty 274(46), 32631-32637 (1999).

8. Liu, X.H., Kirschenbaum, A., Lu, M., et al. Prostaglandin E₂ induces hypoxia-inducible factor-1α stabilization and nuclear localization in a human prostate cancer cell line. The Journal of Biological Chemisty 277(51), 50081-50086 (2002).

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Backer, V., Cheung, F.-Y., Siveke, J.T., et al. Knockdown of myeloid cell hypoxia-inducible factor-1α ameliorates the acute pathology in DSS-induced colitis. PLoS One 12(12), e0190074 (2017).

Serrano-Pozo, A., Sanchez-Garcia, M.A., Heras-Garvin, A., et al. Acute and chronic sustained hypoxia do not substantially regulate amyloid-b peptide generation in vivo. PLoS One 12(1), e0170345 (2017).

Nakazawa, H., Ikeda, K., Shinozaki, S., et al. Burn-induced muscle metabolic derangements and mitochondrial dysfunction are associated with activation of HIF-1a and mTORC1: Role of protein farnesylation. Sci. Rep. 7(6618), (2017).

Kim, Y., Nam, H.J., Lee, J., et al. Methylation-dependent regulation of HIF-1a stability restricts retinal and tumour angiogenesis. Nat. Commun. 7, 10347 (2016).

Lajko, M., Cardona, H.J., Taylor, J.M., et al. Hyperoxia-induced proliferative retinopathy: Early interruption of retinal vascular development with severe and irreversible neurovscular disruption. PLoS One 2016, e0166886 (2016).

Chou, T.-F., Chuang, Y.-T., Hsieh, W.-C., et al. Tumour suppressor death-associated protein kinase targets cytoplasmic HIF-1a for Th17 suppression. Nat. Commun. 7, 11904 (2016).

Yoon, C., Lee, H.-J., Park, D.J., et al. Hypoxia-activated chemotherapeutic TH-302 enhances the effects of VEGF-A inhibition and radiation on sarcomas. Br. J. Cancer 113, 46-56 (2015).

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Yuan, Q., Bleiziffer, O., Boos, A.M., et al. PHDs inhibitor DMOG promotes the vascularization process in the AV loop by HIF-1a up-regulation and the preliminary discussion on its kinetics in rat. BMC Biotechnol. 14, 112 (2014).

Genetos, D.C., Cheung, W.K., Decaris, M.L., et al. Oxygen tension modulates neurite outgrowth in PC12 cells through a mechanism involving HIF and VEGF. J. Mol. Neurosci. 40(3), 360-366 (2010).

Decaris, M.L., Lee, C.I., Yoder, M.C., et al. Influence of the oxygen microenvironment on the proangiogenic potential of human endothelial colony forming cells. Angiogenesis 12(4), 303-311 (2009).