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). 
Increased levels of PHD2 have been reported in both hypoxic human articular cartilage cells as detected by immunoblotting using anti- PHD2 antibodies, in fact PHD 2 was the most abundant as compared to PHD1 and PHD3 counterparts suggesting that PHD2 plays an important role in tissue repair under hypoxic conditions in vivo (2). The discovery of oxygen sensors including prolyl hydroxylase domain-containing proteins 1-3 (PHD1-3) has yielded exciting novel insights into how cells sense oxygen and keep oxygen supply and consumption in balance. Advances in understanding of the role of these oxygen sensors in hypoxia tolerance, ischemic preconditioning and inflammation can create new opportunities for pharmacological interventions for ischemic and inflammatory diseases. Novus Biologicals offers an extensive collection of research tools in the form of siRNA, cell lysates and anti-HIF Prolyl Hydroxylase 2 antibodies for your research needs.
Novus Biologicals offers HIF Prolyl Hydroxylase 2 reagents for your research needs including:
