Hypoxia Inducible Factor (HIF) regulates responses to hypoxia and is comprised of two subunits alpha and beta. Upon cellular exposure to hypoxic conditions, the HIF complex (alpha and beta subunits) is stabilized and binds to DNA transcriptionally activating genes linked to the cellular processes of angiogenesis and glucose metabolism1. Under normal conditions, the HIF-alpha subunit is hydroxylated by the enzyme HIF-alpha prolyl hydroxylase (HIF-PH) leading to ubiquitylation of HIF-alpha and subsequent destruction2. DMOG (dimethyloxalylglycine) is a cell permeable competitive inhibitor of HIF-alpha prolyl hydroxylase (HIF-PH) leading to the stabilization of HIF and subsequent angiogenesis and glucose metabolism at concentrations between 0.1 and 1 mM3,4
References
1) Ivan, M., K. Kondo, et al. (2001). “HIFalpha targeted for VHL-mediated destruction by proline hydroxylation: implications for O2 sensing.” Science 292(5516): 464-8.2) Jaakkola, P., D. R. Mole, et al. (2001). “Targeting of HIF-alpha to the von Hippel-Lindau ubiquitylation complex by O2-regulated prolyl hydroxylation.” Science 292(5516): 468-72.3) Cummins, E. P., F. Seeballuck, et al. (2008). “The hydroxylase inhibitor dimethyloxalylglycine is protective in a murine model of colitis.” Gastroenterology 134(1): 156-65.4) Glassford, A. J., P. Yue, et al. (2007). “HIF-1 regulates hypoxia- and insulin-induced expression of apelin in adipocytes.” Am J Physiol Endocrinol Metab 293(6): E1590-6.
| Categories | Biochemical Reagents |
|---|
| Filter | HEME Pathway |
|---|
| CAS Number | 89464-63-1 |
|---|
| Molecular Formula | C6H9NO5 |
|---|
| Molecular Weight (g/mol) | 175.14 |
|---|
| Purity | >95% |
|---|
| Storage | -20 °C or below |
|---|
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