OGFOD3 Antibody / 2-Oxoglutarate and iron-dependent oxygenase domain-containing protein 3, 100 ug

OGFOD3 antibody detects 2-oxoglutarate and iron-dependent oxygenase domain-containing protein 3, a member of the 2OG/Fe(II)-dependent dioxygenase superfamily involved in protein hydroxylation and cellular stress regulation. Encoded by the OGFOD3 gene on chromosome 1p22.2, this small nuclear protein contains a conserved dioxygenase domain that utilizes 2-oxoglutarate and Fe2+ as cofactors for oxidative catalysis. Although its exact substrates remain under investigation, OGFOD3 is thought to participate in hydroxylation of ribosomal and transcriptional proteins, influencing translation fidelity and stress responses. This family of enzymes links oxygen and nutrient availability to cellular metabolism and gene expression through oxygen-dependent modification reactions.

OGFOD3 is expressed in most tissues, with notable enrichment in the brain, testis, and liver. Localization studies show nuclear distribution with occasional cytoplasmic presence, suggesting roles in both nuclear signaling and translational control. Comparative genomics indicates that OGFOD3 shares structural similarity with OGFOD1, an enzyme known to hydroxylate ribosomal protein RPS23, implying potential overlap in function. The OGFOD3 antibody is used to investigate dioxygenase-mediated post-translational modifications and the cellular response to oxidative or metabolic stress.

Although less characterized than its paralogs, OGFOD3 has been linked to cellular stress pathways and protein biosynthesis. Studies show that depletion of OGFOD3 alters ribosomal activity and activates integrated stress response signaling. In cancer research, OGFOD3 expression is dysregulated in several tumor types, including lung and colon carcinomas, where it may influence adaptation to hypoxia or nutrient deprivation. The OGFOD3 antibody allows researchers to detect expression changes under stress conditions and to localize the protein within cells using immunocytochemical or immunofluorescent assays. Western blot analysis identifies a 38 kilodalton band corresponding to the full-length protein.

In the context of oxygen sensing and translational control, OGFOD3 may coordinate with other 2OG oxygenases to maintain homeostasis during metabolic shifts. It potentially affects protein synthesis by modifying translation factors or ribosomal subunits, modulating global translational output in response to stress. NSJ Bioreagents provides the OGFOD3 antibody validated for western blotting, immunohistochemistry, and immunofluorescence, enabling accurate detection and characterization of this emerging regulatory enzyme in studies of oxygen-dependent signaling and metabolism.