GalNAc-T2, soluble fragment, Human Recombinant | P1215

Polypeptide N-acetylgalactosaminyltransferase 2 (GalNAc-T2) catalyzes the transfer of N-acetylgalactosamine (GalNAc) from UDP-GalNAc to the hydroxyl group of serine and threonine residues. Twenty GalNAc-T genes have been identified in humans and most have been shown to represent active GalNAc-Ts. All isoforms are type II transmembrane proteins, with different but partly overlapping substrate preferences. The GalNAc-Ts control the initiation of mucin-type O-linked glycosylation and determine the location and density of O-glycans in a protein. Addition of GalNAc to an unglycosylated Ser/Thr residue creates the Tn antigen GalNAca1-S/T, and subsequent addition of sialic acid by ST6GalNAc-I forms the cancer associated STn antigen. GalNAc-T2 is primarily located in Golgi, and is widely distributed in human tissues.

P1215 | GalNAc-T2 soluble fragment Human Recombinant DataSheet

Biomolecule/Target: GALNT2

Synonyms: Polypeptide N-acetylgalactosaminyltransferase 2, Polypeptide GalNAc transferase 2, GaNTase 2

Alternates names: Polypeptide N-acetylgalactosaminyltransferase 2, Polypeptide GalNAc transferase 2, GaNTase 2

Taglines: Catalyzes the initial reaction in O-linked oligosaccharide biosynthesis

NCBI Gene ID #: 2254

NCBI Gene Symbol: FGF9

Gene Source: Human

Accession #: P54130

Recombinant: Yes

Source: Insect cells

Purity by SDS-PAGEs: 98%

Assay: SDS-PAGE

Purity: N/A

Assay #2: N/A

Endotoxin Level: N/A

Activity (Specifications/test method): Measured by transfer of GalNAc from UDP-GalNAc to the peptide MEELGMAPALQPTQGAMPAF.

Biological activity: Specific activity is greater than 300 pmol/min/µg. Measured by transfer of GalNAc from UDP-GalNAc to the peptide MEELGMAPALQPTQGAMPAF, enzyme reactions containing: 25 mM Calcium carbonate pH 7.4, 10 mM manganese chloride, 0.25% Triton X 100, 2 mM UDP-GalNAc and 10 µg (400 µg/mL final) peptide. Incubated at 37 ºC.

Results: >300 pmol/min/ug

Binding Capacity: N/A

Unit Definition: N/A

Molecular Weight: N/A

Concentration: 360 ug/ml

Appearance: Liquid

Physical form description: Sterile filtered solution in 20 mM Hepes pH 7 and 100 mM NaCl

Reconstitution Instructions: N/A

Amino acid sequence: N/A