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The enzymatic hydroxylation of HIF1 defines the classical O2- sensing HIF1-pathway. Proline modifications are due to one of the three prolyl-hydroxylase (PHD) enzymes, which mediates recognition of the VHL–Elongins complex and ubiquitination (Ub) of HIF1-alpha and hence targeting for proteasomal degradation. Oncogenic activation, associated with activation of the Ras–RAF–MAPK (mitogen-activated protein kinase), phosphoinositide 3-kinase (PI3K), PTEN or Akt pathways cause HIF1-alpha accumulation through unknown mediators. Tri-carboxylic acid cycle intermediates such as succinate and fumarate, or perhaps mitochondrial reactive oxygen species (ROS), can inhibit the activity of PHDs, also stabilizing HIF1- alpha. Stabilized HIF1-alpha associates with HIF1-beta, which binds to cognate hypoxia-responsive elements (HREs) in target genes.

Confocal immunofluorescent analysis of ARNT2 (Center) Antibody #AP16544c on Hela cell. 0.02 mg/ml primary antibody was followed by FITC-conjugated goat anti-rabbit lgG. FITC emits green fluorescence. DAPI was used to stain the cell nucleus (blue). F-actin filaments have been labeled with phalloidin (red). Immunoreactivity for ARNT2 (HIF1 ) in the nucleus (constitutive).

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Immunity Source (Host)
Available staus
HIF1β ()