|Detection of Human Polypeptide GalNac Transferase 2/GALNT2 by Western Blot. Western blot shows lysates of MOLT‑4 human acute lymphoblastic leukemia cell line, HeLa human cervical epithelial carcinoma cell line, and HepG2 human hepatocellular carcinoma cell line. PVDF membrane was probed with 1 µg/mL of Sheep Anti-Human Polypeptide GalNac Transferase 2/GALNT2 Antigen Affinity-purified Polyclonal Antibody (Catalog # AF7507) followed by HRP-conjugated Anti-Sheep IgG Secondary Antibody (Catalog # HAF016). A specific band was detected for Polypeptide GalNac Transferase 2/GALNT2 at approximately 65-70 kDa (as indicated). This experiment was conducted under reducing conditions and using Immunoblot Buffer Group 1.|
|Polypeptide GalNac Transferase 2/GALNT2 in HeLa Human Cell Line. Polypeptide GalNac Transferase 2/GALNT2 was detected in immersion fixed HeLa human cervical epithelial carcinoma cell line using Sheep Anti-Human Polypeptide GalNac Transferase 2/GALNT2 Antigen Affinity-purified Polyclonal Antibody (Catalog # AF7507) at 1.7 µg/mL for 3 hours at room temperature. Cells were stained using the NorthernLights™ 557-conjugated Anti-Sheep IgG Secondary Antibody (red; Catalog # NL010) and counterstained with DAPI (blue). Specific staining was localized to the trans-Golgi secretory reticulum. View our protocol for Fluorescent ICC Staining of Cells on Coverslips.|
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.