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GALNT6 Antibody (C-term) Blocking Peptide
Synthetic peptide
- SPECIFICATION
- CITATIONS
- PROTOCOLS
- BACKGROUND
| Primary Accession | Q8NCL4 |
|---|---|
| Clone Names | 110617146 |
| Gene ID | 11226 |
|---|---|
| Other Names | Polypeptide N-acetylgalactosaminyltransferase 6, Polypeptide GalNAc transferase 6, GalNAc-T6, pp-GaNTase 6, Protein-UDP acetylgalactosaminyltransferase 6, UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase 6, GALNT6 |
| Format | Peptides are lyophilized in a solid powder format. Peptides can be reconstituted in solution using the appropriate buffer as needed. |
| Storage | Maintain refrigerated at 2-8°C for up to 6 months. For long term storage store at -20°C. |
| Precautions | This product is for research use only. Not for use in diagnostic or therapeutic procedures. |
| Name | GALNT6 |
|---|---|
| Function | 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 (PubMed:10464263, PubMed:31932717). May participate in synthesis of oncofetal fibronectin (PubMed:10464263). Has activity toward MUC1A, MUC2, EA2 and fibronectin peptides (PubMed:10464263). Glycosylates FGF23 (PubMed:31932717). |
| Cellular Location | Golgi apparatus membrane {ECO:0000250|UniProtKB:Q14435}; Single-pass type II membrane protein {ECO:0000250|UniProtKB:Q14435} |
| Tissue Location | Expressed in placenta and trachea. Weakly expressed in brain and pancreas. Expressed in fibroblast. Weakly or not expressed in lung, liver, muscle, kidney, spleen, thymus, prostate, testis, ovary, intestine, colon, leukocyte, stomach, thyroid, spinal cord, lymph node, trachea, adrenal gland and bone marrow |
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Provided below are standard protocols that you may find useful for product applications.
Background
This gene encodes a member of theUDP-N-acetyl-alpha-D-galactosamine:polypeptideN-acetylgalactosaminyltransferase (GalNAc-T) family of enzymes.GalNAc-Ts initiate mucin-type O-linked glycosylation in the Golgiapparatus by catalyzing the transfer of GalNAc to serine andthreonine residues on target proteins. They are characterized by anN-terminal transmembrane domain, a stem region, a lumenal catalyticdomain containing a GT1 motif and Gal/GalNAc transferase motif, anda C-terminal ricin/lectin-like domain. GalNAc-Ts have different,but overlapping, substrate specificities and patterns ofexpression. The encoded protein is capable of glycosylatingfibronectin peptide in vitro and is expressed in a fibroblast cellline, indicating that it may be involved in the synthesis ofoncofetal fibronectin.
References
Rose, J.E., et al. Mol. Med. 16 (7-8), 247-253 (2010) :Gomes, J., et al. J. Histochem. Cytochem. 57(1):79-86(2009)Patani, N., et al. Cancer Genomics Proteomics 5(6):333-340(2008)Argueso, P., et al. Invest. Ophthalmol. Vis. Sci. 44(1):86-92(2003)Bennett, E.P., et al. J. Biol. Chem. 274(36):25362-25370(1999)
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