Fusion protein to human HIF-1 beta. Containing a.a. 496-789.
Buffer
0.02% sodium azide
Clone Name
Isotype
Species Reactivity
human, bovine, sheep, mouse, rat, ferret
Concentration
Purification
Whole antisera
Guaranteed Application *
WB, IHC
Suggested Dilutions
WB (1:2000), IHC, IP
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-1 beta is a series of aryl hydrocarbon receptor nuclear translocator (ARNT) gene products. (1,5,6)
Related Pathway
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HEK293T cells were transfected with the pCMV6-ENTRY control or pCMV6-ENTRY ARNT (RC216724) cDNA for 48 hrs and lysed. Equivalent amounts of cell lysates (5 ug per lane) were separated by SDS-PAGE and immunoblotted with anti-ARNT.
