抗HIF-1 alpha [Hydroxy Pro564]抗体 | Anti-HIF-1 alpha [Hydroxy Pro564] Antibody

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Western Blot: HIF-1 alpha [Hydroxy Pro564] Antibody [NB110-74679] - Detection (left panel) of hydroxylated HIF-1alpha in nuclear extracts of A549 cells treated with MG132 (a proteasome inhibitor). Hydroxyproline is not recognized on HIF-1alpha when cells are first treated with DFO, a prolyl hydroxylase inhibitor that prevents HIF hydroxylation. Control staining is shown (right panel) using conventional anti-HIF-1alpha. The asterisk marks a band approximately 110 kDa in size corresponding to HIF1-The primary antibody was used at a 1:1,000 dilution in 2% BLOTTO.

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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. The stabilization of HIF-1 alpha by hypoxia is critically dependent upon the hydroxylation of certain Proline residues that exist in the oxygen-dependent degradation domain of HIF-1 alpha. 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.

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