EGLN1 Antibody / Egl nine homolog 1 / PHD2, 100ug

EGLN1 antibody targets Egl nine homolog 1, encoded by the EGLN1 gene. Egl nine homolog 1, also known as prolyl hydroxylase domain protein 2, is a cytoplasmic and nuclear enzyme that functions as a central oxygen sensor in mammalian cells. EGLN1 belongs to the family of 2-oxoglutarate-dependent dioxygenases and catalyzes proline hydroxylation reactions that are tightly regulated by cellular oxygen availability.<br><br>Functionally, Egl nine homolog 1 plays a critical role in regulation of hypoxia-inducible factor signaling. Under normoxic conditions, EGLN1 hydroxylates specific proline residues on hypoxia-inducible factor alpha subunits, marking them for recognition by the von Hippel-Lindau protein and subsequent proteasomal degradation. Through this mechanism, EGLN1 maintains low hypoxia-inducible factor activity when oxygen levels are sufficient. An EGLN1 antibody supports studies focused on oxygen sensing and hypoxia-regulated transcription.<br><br>EGLN1 is broadly expressed across tissues, reflecting the universal need for oxygen-sensing mechanisms in mammalian physiology. Its activity is particularly relevant in tissues with fluctuating oxygen supply, such as kidney, lung, and vascular-associated cells. EGLN1 localization and activity can be influenced by cellular redox state, metabolic intermediates, and cofactor availability, allowing fine control of hypoxia-responsive pathways.<br><br>From a disease-relevance perspective, Egl nine homolog 1 has been extensively studied in cancer, cardiovascular disease, and ischemic disorders. Dysregulation of EGLN1 activity can lead to aberrant hypoxia-inducible factor stabilization, promoting angiogenesis, metabolic reprogramming, and altered cell survival. Genetic variation in EGLN1 has also been linked to high-altitude adaptation and erythropoiesis, highlighting its importance in systemic oxygen homeostasis.<br><br>At the molecular level, Egl nine homolog 1 contains conserved catalytic domains required for iron and 2-oxoglutarate binding, which are essential for hydroxylase activity. Post-translational modifications and cellular context can influence its enzymatic activity and apparent behavior in biochemical assays without altering the primary amino acid sequence. EGLN1 antibody reagents support research applications focused on hypoxia signaling, oxygen-dependent gene regulation, and disease-associated cellular adaptation, with NSJ Bioreagents providing reagents intended for research use.

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