HIF-1 alpha

Hypoxia-inducible factor 1 (HIF-1) allows cells to respond to changing levels of oxygen in the environment. HIF-1 is a heterodimeric transcription factor consisting of alpha and beta subunits. Under normal conditions HIF-1 alpha is continuously synthesized and degraded. HIF-1 alpha degradation is mediated through an oxygen-dependent degradation domain that is hydroxylated and leads to ubiquitylation and proteolysis. HIF-1 beta on the other hand is constitutively expressed and localizes to the nucleus.

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FIH-1/HIF-1AN (factor inhibiting hypoxia-inducible factor-1/ HIF1AN) is a 40.3kDa protein which is expressed as asparaginyl hydroxylase enzyme in various multicellular organisms from worms/flies to mouse/rat and human beings.

Autophagy, a protein degradation process through autophagosome-lysosomal pathway, is important for cellular homeostasis and plays a role in many diseases. To help researchers learn more about this process and the products available for its study, Novus Biologicals has released a new Autophagy catalog.

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. Hypoxia-inducible factor 1 (HIF-1) is a nuclear protein involved in mammalian oxygen homeostasis.

Encoded by the HIF1A gene, HIF-1 alpha has a critical role in cellular response to hypoxia. In hypoxic conditions, HIF-1 alpha activates the transcription of several genes to facilitate metabolic reaction for lack of oxygen. In normoxic conditions, HIF-1 alpha is degraded by the proteasome system.

Learn more about HIF-1 Alpha in our infographic below.

Hypoxia-inducible factor-1 is a major transcription factor composed of two subunits: HIF-1alpha and HIF-1 beta. Under normoxic conditions, HIF-1 alpha is targeted to proteosomal degradation via ubiquitination.

Hypoxia inducible factor-1 (HIF-1) is a major transcription factor that is composed of two subunits: HIF-1 alpha and HIF-1 beta, the latter being a constitutively-expressed aryl hydrocarbon receptor nuclear transporter (ARNT).

Prolyl hydroxylase domain (PHD) proteins, including PHD1, PHD2, and PHD3, mediate oxygen-dependent degradation of hypoxia-inducible factor (HIF) alpha subunits. Suppression of PHD enzymes leads to stabilization of HIFs and offers a potential treatment option for many ischemic disorders, such as peripheral artery occlusive disease, myocardial infarction, and stroke (1).

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