Anti-GALNT12 / Polypeptide N-acetylgalactosaminyltransferase 12

Adding 0.2 ml of distilled water will yield a concentration of 500 ug/ml. GALNT12 antibody detects Polypeptide N-acetylgalactosaminyltransferase 12, an enzyme involved in initiating mucin-type O-linked glycosylation of proteins. Encoded by the GALNT12 gene on chromosome 9q22.33, this Golgi-resident glycosyltransferase catalyzes the transfer of N-acetylgalactosamine (GalNAc) from UDP-GalNAc to serine or threonine residues on target proteins, forming the Tn antigen and enabling further elongation of O-glycan structures. GALNT12 plays a crucial role in regulating protein stability, secretion, and cell-cell communication through glycosylation control.Structurally, GALNT12 contains a catalytic domain typical of the GalNAc-transferase family and a ricin-like lectin domain that mediates substrate recognition. It preferentially glycosylates substrates involved in epithelial integrity and mucin production. GALNT12 is expressed in gastrointestinal tissues and epithelial linings, where it influences mucin biosynthesis, cell adhesion, and signaling. Its activity affects the glycoprotein composition of the extracellular matrix and epithelial surfaces.The GALNT12 antibody is widely used in glycobiology, cancer, and epithelial research to study O-glycosylation and mucin biosynthesis. Western blot analysis identifies a 60 kilodalton band corresponding to GALNT12, while immunofluorescence reveals perinuclear staining consistent with Golgi localization. This antibody is instrumental in evaluating changes in glycosylation during differentiation, inflammation, and tumorigenesis.Mutations in GALNT12 are associated with colorectal cancer susceptibility, where altered O-glycosylation patterns affect cell adhesion and immune recognition. Dysregulated GALNT12 expression may lead to incomplete mucin glycosylation, contributing to tumor progression and epithelial dysfunction. The GALNT12 antibody supports research into glycosylation-dependent signaling, epithelial homeostasis, and cancer pathogenesis. NSJ Bioreagents offers this antibody validated for its applications, ensuring reliable performance in studies of glycoprotein biology and epithelial regulation.