Anti-PHYHD1 / Phytanoyl-CoA dioxygenase domain-containing protein 1

Adding 0.2 ml of distilled water will yield a concentration of 500 ug/ml. PHYHD1 antibody detects Phytanoyl-CoA dioxygenase domain-containing protein 1, a putative oxidative enzyme that may play roles in lipid metabolism and cellular stress responses. The UniProt recommended name is Phytanoyl-CoA dioxygenase domain-containing protein 1 (PHYHD1). This non-heme iron-dependent enzyme is thought to participate in hydroxylation or oxidative reactions linked to fatty acid metabolism and peroxisomal function.Functionally, PHYHD1 antibody identifies a 290-amino-acid protein localized mainly in the cytoplasm and potentially associated with peroxisomes. PHYHD1 contains a conserved 2-oxoglutarate (2OG) and Fe(II)-dependent oxygenase domain that catalyzes oxidation reactions using molecular oxygen and 2-oxoglutarate as cofactors. Although its precise substrates remain under investigation, PHYHD1 may regulate lipid processing, hypoxia response, and reactive oxygen species signaling.The PHYHD1 gene is located on chromosome 9q34.11 and is expressed in brain, liver, and kidney. Transcription of PHYHD1 is induced by cellular stress and metabolic cues, suggesting it plays a role in adaptive metabolic regulation. Comparative genomics studies indicate conservation across vertebrates, implying fundamental metabolic importance.Pathologically, alterations in PHYHD1 expression have been associated with gliomas and metabolic disorders involving peroxisomal dysfunction. Reduced PHYHD1 levels may impair fatty acid oxidation and redox homeostasis, while overexpression correlates with enhanced metabolic flexibility in cancer cells. Research using PHYHD1 antibody supports studies in lipid oxidation, metabolic adaptation, and enzymatic regulation under hypoxia.PHYHD1 antibody is validated for western blotting, immunofluorescence, and ELISA to detect 2OG-dependent oxygenases. NSJ Bioreagents provides PHYHD1 antibody reagents optimized for research in oxidative metabolism, enzymology, and metabolic disease mechanisms.Structurally, Phytanoyl-CoA dioxygenase domain-containing protein 1 features a double-stranded beta-helix fold typical of 2OG oxygenases, with a conserved His-Asp-His metal-binding triad that coordinates Fe(II). This structure enables catalytic hydroxylation reactions essential for lipid and oxygen metabolism. This antibody facilitates analysis of PHYHD1's role in oxidative biochemistry, peroxisomal function, and metabolic stress response.