GALNT2 Antibody HeLa Cell IF. Immunofluorescence analysis of HeLa cells using GALNT2 Antibody (green) and alpha tubulin antibody (red). Cells were treated with enzyme antigen retrieval reagent for 15 minutes prior to blocking with goat serum and overnight incubation with GALNT2 Antibody (5 ug/mL) and alpha tubulin antibody at 4°C. Fluoro488- and Cy3-conjugated secondary antibodies were used for detection, and DAPI (blue) was used as a nuclear counterstain. GALNT2 displays concentrated perinuclear staining consistent with Golgi localization, while alpha tubulin highlights the cytoskeletal network. These results support the use of GALNT2 Antibody / O-Glycosylation Enzyme Antibody for studying GALNT2 expression, Golgi organization and protein O-glycosylation.

GALNT2 Antibody HeLa Cell IP. Immunoprecipitation of GALNT2 from HeLa whole cell lysate using GALNT2 Antibody, followed by Western blot analysis with the same antibody. Lane 1: HeLa input lysate (30 ug); Lane 2: rabbit control IgG immunoprecipitation; Lane 3: GALNT2 immunoprecipitation using 2 ug of GALNT2 Antibody from 500 ug of HeLa lysate. A specific band is enriched at approximately 65-70 kDa in the GALNT2 immunoprecipitation sample, while no corresponding GALNT2 band is detected in the control IgG lane, confirming specific enrichment of endogenous GALNT2. These results support the use of GALNT2 Antibody / O-Glycosylation Enzyme Antibody for immunoprecipitation, protein interaction studies and investigations of Golgi-associated O-glycosylation pathways.

GALNT2 Antibody Human, Mouse and Rat WB. Western blot analysis using GALNT2 Antibody. Lane 1: human A549 cells; Lane 2: human HeLa cells; Lane 3: human MOLT-4 cells; Lane 4: rat liver tissue lysate. A specific band is detected at approximately 65 kDa in all samples, consistent with the expected molecular weight of GALNT2. The broad expression observed across human cell lines and rat liver tissue is consistent with the widespread distribution of this Golgi-resident glycosyltransferase, which initiates mucin-type O-linked glycosylation of numerous membrane and secreted proteins. These results support the use of GALNT2 Antibody / O-Glycosylation Enzyme Antibody for studying GALNT2 expression, protein O-glycosylation and Golgi-associated protein processing.