GalNAc-T3 Active Protein | GALNT3 active protein

GalNAc-T3, soluble fragment, Human Recombinant

Cat. Num. AAA849843

• Gene Names: GALNT3; HHS; HFTC; GalNAc-T3
• Purity: >95% by SDS-PAGE
• Synonyms: GalNAc-T3; soluble fragment; Human Recombinant; Polypeptide N-acetylgalactosaminyltransferase 3; Polypeptide GalNAc transferase 3; GaNTase 3; GALNT3 active protein

• Host: Insect cells
• Purity/Purification: >95% by SDS-PAGE
• Form/Format: Liquid. Sterile filtered solution in 25mM Tris pH7.5 and 150mM NaCl
• Concentration: 466ug/ml (varies by lot)

• Gene Source: Human
• Biological Activity: Specific activity >500 pmol/min/ug; Measured by transfer of N-acetylgalatosamine (GalNac) from UDP-Gal to the peptide EA2, as measured with a phosphatase-coupled assay.
• Preparation and Storage: Store at -20 degree C; Centrifuge the vial prior to opening.; Shelf life: ~12 months

Testing Data

Related Product Information for GALNT3 active protein

Polypeptide N-acetylgalactosaminyltransferase 3 (GalNAc-T3) 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 GalNAcalpha1-S/T, and subsequent addition of sialic acid by ST6GalNAc-I forms the cancer associated STn antigen. GalNAc-T3 is highly expressed in pancreas and testis, and weakly expressed in a few other organs such as placenta. The expression levels of GalNAc-T3 were found to be upregulated in highly differentiated types of adenocarcinoma cell lines as opposed to less differentiated types. Overexpression of GalNAc-T3 has also been found to promote pancreatic cancer cell growth. Mutations in GalNAc-T3 were found to be involved in familial tumoral calcinosis, which may be mediated through glycosylation of fibroblast growth factor 23, protecting it from proteolytic cleavage. GalNAc-T3 has a preference for mono- or diglycosylated substrates.

Product Categories/Family for GALNT3 active protein

Proteins; Enzymes; Proteins & Enzymes (A-Z); Glycosyltransferase Enzymes

NCBI and Uniprot Product Information

• NCBI GI #: 153266878
• NCBI GeneID: 2591
• NCBI Accession #: NP_004473.2
• NCBI GenBank Nucleotide #: NM_004482.3
• UniProt Accession #: Q14435; Q53TG9; Q7Z476
• Molecular Weight: 22,212 Da
• NCBI Official Full Name: polypeptide N-acetylgalactosaminyltransferase 3
• NCBI Official Synonym Full Names: polypeptide N-acetylgalactosaminyltransferase 3
• NCBI Official Symbol: GALNT3
• NCBI Official Synonym Symbols: HHS; HFTC; GalNAc-T3
• NCBI Protein Information: polypeptide N-acetylgalactosaminyltransferase 3
• UniProt Protein Name: Polypeptide N-acetylgalactosaminyltransferase 3
• UniProt Gene Name: GALNT3
• UniProt Synonym Gene Names: GalNAc-T3; pp-GaNTase 3

NCBI Description

This gene encodes UDP-GalNAc transferase 3, a member of the GalNAc-transferases family. This family transfers an N-acetyl galactosamine to the hydroxyl group of a serine or threonine residue in the first step of O-linked oligosaccharide biosynthesis. Individual GalNAc-transferases have distinct activities and initiation of O-glycosylation is regulated by a repertoire of GalNAc-transferases. The protein encoded by this gene is highly homologous to other family members, however the enzymes have different substrate specificities. [provided by RefSeq, Jul 2008]

Uniprot Description

GALNT3: an enzyme that 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. A single-pass type II membrane protein that localizes to the Golgi apparatus membrane. Has activity toward HIV envelope glycoprotein gp120, EA2, Muc2 and Muc5. Probably glycosylates fibronectin in vivo. Plays a central role in phosphate homeostasis. Mutations cause cause familial tumoral calcinosis, a severe autosomal recessive metabolic disorder that manifests with hyperphosphatemia and massive calcium deposits in the skin and subcutaneous tissues. Overexpressed in many differentiated carcinomas, suggesting that it may serve as a marker of tumor differentiation. Two alternatively spliced human isoforms have been described.

Protein type: EC 2.4.1.41; Glycan Metabolism - O-glycan biosynthesis; Membrane protein, integral; Transferase

Chromosomal Location of Human Ortholog: 2q24.3

Cellular Component: extracellular exosome; Golgi apparatus; Golgi membrane; integral component of membrane; membrane; perinuclear region of cytoplasm

Molecular Function: calcium ion binding; carbohydrate binding; manganese ion binding; polypeptide N-acetylgalactosaminyltransferase activity

Biological Process: carbohydrate metabolic process; fibroblast growth factor receptor signaling pathway; O-glycan processing; protein O-linked glycosylation via serine; protein O-linked glycosylation via threonine

Disease: Tumoral Calcinosis, Hyperphosphatemic, Familial