1/50 - 1/100. Perform heat mediated antigen retrieval with citrate buffer pH 6 before commencing with IHC staining protocol.
Catalyzes the initial reaction in O-linked oligosaccharide biosynthesis, the transfer of an N-acetyl-D-galactosamine residue to a serine or threonine residue on the protein receptor. Has a broad spectrum of substrates for peptides such as EA2, Muc5AC, Muc1a, Muc1b. Probably involved in O-linked glycosylation of the immunoglobulin A1 (IgA1) hinge region.
Protein modification; protein glycosylation.
Belongs to the glycosyltransferase 2 family. GalNAc-T subfamily. Contains 1 ricin B-type lectin domain.
There are two conserved domains in the glycosyltransferase region: the N-terminal domain (domain A, also called GT1 motif), which is probably involved in manganese coordination and substrate binding and the C-terminal domain (domain B, also called Gal/GalNAc-T motif), which is probably involved in catalytic reaction and UDP-Gal binding. The ricin B-type lectin domain binds to GalNAc and contributes to the glycopeptide specificity.
Golgi apparatus > Golgi stack membrane. Secreted. Resides preferentially in the trans and medial parts of the Golgi stack. A secreted form also exists.
Immunocytochemistry/ Immunofluorescence - Anti-GALNT2 antibody (ab102650)This image is courtesy of an anonymous Abreview
ab102650 staining GALNT2 in HeLa cells by ICC/IF (Immunocytochemistry/immunofluorescence). Cells were fixed with paraformaldehyde, permeabilized with 0.2% Triton X-100 and blocked with 1% BSA for 30 minutes at 25°C. Samples were incubated with primary antibody (1/50) for 1 hour at 25°C. A TRITC-conjugated goat anti-rabbit IgG monoclonal (1/250) was used as the secondary antibody.