Anti-P3H2 / Prolyl 3-hydroxylase 2

Adding 0.2 ml of distilled water will yield a concentration of 500 ug/ml. P3H2 antibody detects Prolyl 3-hydroxylase 2, an endoplasmic reticulum enzyme responsible for hydroxylating proline residues in collagen and collagen-like proteins. Encoded by the P3H2 gene on chromosome 3q28, this enzyme belongs to the 2-oxoglutarate-dependent dioxygenase family and functions in post-translational modification of extracellular matrix proteins. P3H2 catalyzes the formation of 3-hydroxyproline at specific sites in fibrillar collagens, contributing to the stability, folding, and assembly of collagen triple helices.P3H2 localizes to the lumen of the endoplasmic reticulum, where it operates as part of a multi-enzyme complex with cartilage-associated protein (CRTAP) and cyclophilin B (PPIB). This complex ensures proper hydroxylation and folding of procollagen molecules prior to secretion. The enzymatic reaction requires Fe2+, 2-oxoglutarate, and ascorbate as cofactors. Loss of P3H2 activity leads to underhydroxylated collagen and defects in connective tissue organization.The P3H2 antibody is used in extracellular matrix, connective tissue, and skeletal biology research to study collagen modification and protein maturation. Western blot analysis detects a 90 kilodalton band corresponding to P3H2, while immunofluorescence reveals reticular ER localization consistent with its role in collagen biosynthesis. This antibody allows characterization of collagen-modifying enzymes and post-translational hydroxylation mechanisms.Altered expression or mutation of P3H2 has been implicated in connective tissue disorders, osteogenesis imperfecta, and fibrosis, where abnormal collagen hydroxylation compromises structural integrity. The P3H2 antibody is an essential reagent for exploring collagen maturation, matrix assembly, and disease-associated remodeling. NSJ Bioreagents offers this antibody validated for western blotting, immunofluorescence, and immunohistochemistry, ensuring accuracy in studies of extracellular matrix biology and protein modification.