Anti-GALNT7 / Polypeptide N-acetylgalactosaminyltransferase 7

Adding 0.2 ml of distilled water will yield a concentration of 500 ug/ml. GALNT7 antibody detects Polypeptide N-acetylgalactosaminyltransferase 7, encoded by the GALNT7 gene on chromosome 4q31.1. GALNT7 antibody recognizes this glycosyltransferase, which belongs to the family of enzymes that initiate mucin-type O-linked glycosylation. GALNT7 transfers N-acetylgalactosamine (GalNAc) from UDP-GalNAc to serine or threonine residues in polypeptides, producing the Tn antigen and triggering formation of more complex O-glycan structures. This initial step in O-glycosylation regulates stability, solubility, localization, and function of diverse secreted and membrane proteins.Structurally, GALNT7 contains a conserved catalytic glycosyltransferase domain with motifs required for UDP-sugar binding and catalysis. Its C-terminal ricin B-type lectin domain recognizes GalNAc-containing glycans, enhancing substrate specificity by targeting partially glycosylated peptides. This dual-domain organization ensures GALNT7 selectively modifies glycoproteins in the Golgi apparatus. Differential expression across tissues enables cell type-specific glycosylation signatures that influence developmental and immune processes.Functionally, GALNT7 participates in modifying mucins, adhesion molecules, and receptors that mediate signaling and cellular interactions. Aberrant GALNT7 activity alters glycosylation, impacting tumor progression and immune recognition. In cervical, breast, and prostate cancers, GALNT7 is overexpressed, producing truncated glycans and exposing Tn antigens that promote metastasis and immune evasion. Conversely, loss of GALNT7 disrupts epithelial integrity and reduces protective mucin barriers. Regulation of GALNT7 by microRNAs and transcriptional programs further links it to cancer biology and development.Beyond cancer, GALNT7 is implicated in immune modulation. It modifies receptors involved in lymphocyte activation and adhesion molecules guiding leukocyte trafficking. Dysregulated O-glycosylation by GALNT7 can impair immune tolerance, alter antigen presentation, and contribute to inflammatory conditions. Developmentally, GALNT7 expression is enriched in epithelial tissues and during organogenesis, suggesting roles in morphogenesis and cell differentiation. Researchers rely on GALNT7 antibody to evaluate enzyme expression in contexts ranging from tumor progression to immune regulation.In experimental research, GALNT7 antibody is used in western blotting to quantify protein levels, immunofluorescence to assess Golgi localization, and immunohistochemistry to map expression in tumors. Co-immunoprecipitation studies combined with glycoproteomics reveal GALNT7 substrates including MUC1, integrins, and growth factor receptors. By enabling detection of this enzyme, GALNT7 antibody supports functional analyses of O-glycosylation pathways. NSJ Bioreagents provides GALNT7 antibody for reliable use in glycobiology, oncology, and immunology research.