Alexa Fluor® 488 Anti-PHD1/prolyl hydroxylase antibody [EPR2746]

Supplementary info

This supplementary information is collated from multiple sources and compiled automatically.

Activity summary

Prolyl hydroxylase 1 (PHD1) also known as EGLN2 is an enzyme that hydroxylates specific proline residues within target proteins. This process of prolyl hydroxylation is critical for regulating protein stability. PHD1 shares structural similarities with other members of the 2-oxoglutarate-dependent dioxygenase family and includes a conserved iron-binding motif essential for its enzymatic activity. PHD1 has a molecular mass of approximately 46 kDa and is expressed in a variety of tissues with notable presence in skeletal muscle heart and the liver.

Biological function summary

PHD1 modulates the stability of the hypoxia-inducible factor (HIF) proteins which are key regulators of oxygen homeostasis in the cell. Under normoxic conditions PHD1 hydroxylates specific proline residues on HIF-alpha marking it for degradation via the ubiquitin-proteasome pathway. This enzyme does not function as part of a larger protein complex but it plays a pivotal role in determining the cellular response to oxygen levels. Additionally PHD1 expression affects the metabolic adaptation processes and energy expenditure in cells.

Pathways

PHD1 plays a role in the cellular response to hypoxia and is integral to the HIF signaling pathway. It interacts directly with HIF-alpha subunits mediating their degradation under normal oxygen conditions to ensure HIF activity remains inhibited. Additionally PHD1 is indirectly involved in modulating the angiogenesis pathway as it influences the availability of HIF-related transcription factors which promote transcription of vascular endothelial growth factor (VEGF) under low oxygen conditions. The interplay between PHD1 PHD2 and PHD3 ensures a fine-tuned regulation of the HIF pathway based on oxygen availability.

Associated diseases and disorders

PHD1 has links to cancer progression and ischemic conditions. The enzyme’s activity is often altered in response to the aberrant hypoxic signaling found within tumors impacting cellular proliferation and survival. In ischemic conditions reduced PHD1 activity leads to stabilization of HIF proteins and adaptation responses aimed at tissue survival. Mutations or dysregulation in PHD1 expression have been observed in metabolic syndromes suggesting potential therapeutic targets. Through its control over hypoxia-related proteins PHD1 also interacts with von Hippel-Lindau (VHL) protein which is part of the E3 ubiquitin ligase complex important for HIF-alpha degradation.