Human Polypeptide GalNac Transferase 2/
GALNT2 Alexa Fluor™ Plus 488-conjugated Antibody

GALNT2 (N-Acetyl-Galactoseaminyl Transferase 2; also UDP-Acetylgalactosaminyltransferase 2 and ppGalNAc-T2) is a 68-74 kDa member of the GalNAC transferase subfamily, glycosyltransferase 2 family of enzymes. It is widely expressed, being found on basal keratinocytes, hepatocytes, B cells, renal tubular epithelium, and virtually all cell lines examined to date. GALNT2 is found in the Golgi apparatus, and catalyzes the transfer of UDP-GalNAC onto either a Ser or Thr residue on a previously glycosylated peptide/polypeptide backbone. The generation of O-linked carbohydrates is believed to play a role in cytokine proteolytic processing, as the presence of O-linked sugar adjacent to a PC processing site is known to inhibit proteolysis and molecule inactivation. Human GALNT2 is a 571 amino acid (aa) type II transmembrane protein. It contains a six aa N-terminal cytoplasmic region and a 547 aa extracellular domain (aa 25-571). The ECD possesses two key parts, a catalytic region with two catalytic subdomains (aa 135-240 and 300-362), and a ricin-type lectin domain that binds carbohydrates (aa 456‑566). The latter domain is suggested to facilitate GALNT2 action by imparting specificity and stability to the overall enzyme activity. A 52 kDa soluble form of GALNT2 has been reported that begins at Lys52. There are two potential splice form variants. Both contain a four aa substitution for aa 1-42, and one contains an additional four aa substitution for aa 543-571. Over aa 52-571, human GALNT2 shares 97% aa sequence identity with mouse GALNT2.