Human Polypeptide GalNac Transferase 2/
GALNT2 Antibody
Human Polypeptide GalNac Transferase 2/
GALNT2 Antibody Summary
Lys52-Gln571
Accession # Q10471
Applications
Please Note: Optimal dilutions should be determined by each laboratory for each application. General Protocols are available in the Technical Information section on our website.
Scientific Data
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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.
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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.
Reconstitution Calculator
Preparation and Storage
- 12 months from date of receipt, -20 to -70 °C as supplied.
- 1 month, 2 to 8 °C under sterile conditions after reconstitution.
- 6 months, -20 to -70 °C under sterile conditions after reconstitution.
Background: Polypeptide GalNAc Transferase 2/GALNT2
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.
Product Datasheets
Citation for Human Polypeptide GalNac Transferase 2/
GALNT2 Antibody
R&D Systems personnel manually curate a database that contains references using R&D Systems products. The data collected includes not only links to publications in PubMed, but also provides information about sample types, species, and experimental conditions.
1 Citation: Showing 1 - 1
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A CRISPR screen in intestinal epithelial cells identifies novel factors for polarity and apical transport
Authors: KMC Klee, MW Hess, M Lohmüller, S Herzog, K Pfaller, T Müller, GF Vogel, LA Huber
Elife, 2023-01-20;12(0):.
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GALNT2 Antibody
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