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GALNT7 Antibody
Rabbit Polyclonal Antibody
- SPECIFICATION
- CITATIONS
- PROTOCOLS
- BACKGROUND
Application 
| WB, IHC-P |
|---|---|
| Primary Accession | Q86SF2 |
| Reactivity | Human |
| Host | Rabbit |
| Clonality | Polyclonal |
| Calculated MW | 75kDa |
| Dilution | IHC-P (5 µg/ml) |
| Gene ID | 51809 |
|---|---|
| Other Names | N-acetylgalactosaminyltransferase 7, 2.4.1.-, Polypeptide GalNAc transferase 7, GalNAc-T7, pp-GaNTase 7, Protein-UDP acetylgalactosaminyltransferase 7, UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase 7, GALNT7 |
| Reconstitution & Storage | Short term 4°C, long term aliquot and store at -20°C, avoid freeze thaw cycles. |
| Precautions | GALNT7 Antibody is for research use only and not for use in diagnostic or therapeutic procedures. |
| Name | GALNT7 |
|---|---|
| Function | Glycopeptide transferase involved in O-linked oligosaccharide biosynthesis, which catalyzes the transfer of an N-acetyl-D- galactosamine residue to an already glycosylated peptide. In contrast to other proteins of the family, it does not act as a peptide transferase that transfers GalNAc onto serine or threonine residue on the protein receptor, but instead requires the prior addition of a GalNAc on a peptide before adding additional GalNAc moieties. Some peptide transferase activity is however not excluded, considering that its appropriate peptide substrate may remain unidentified. |
| Cellular Location | Golgi apparatus membrane; Single- pass type II membrane protein |
| Tissue Location | Widely expressed. Expressed in uterus, retina, kidney, small intestine, omentum, stomach and CNS |
Thousands of laboratories across the world have published research that depended on the performance of antibodies from Abcepta to advance their research. Check out links to articles that cite our products in major peer-reviewed journals, organized by research category.
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Provided below are standard protocols that you may find useful for product applications.
Background
Glycopeptide transferase involved in O-linked oligosaccharide biosynthesis, which catalyzes the transfer of an N-acetyl-D-galactosamine residue to an already glycosylated peptide. In contrast to other proteins of the family, it does not act as a peptide transferase that transfers GalNAc onto serine or threonine residue on the protein receptor, but instead requires the prior addition of a GalNAc on a peptide before adding additional GalNAc moieties. Some peptide transferase activity is however not excluded, considering that its appropriate peptide substrate may remain unidentified.
References
Bennett E.P.,et al.FEBS Lett. 460:226-230(1999).
Otsuki T.,et al.DNA Res. 12:117-126(2005).
Mural R.J.,et al.Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
Burkard T.R.,et al.BMC Syst. Biol. 5:17-17(2011).
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