GALNT7 Antibody
Rabbit Polyclonal Antibody
- SPECIFICATION
- CITATIONS
- PROTOCOLS
- BACKGROUND
Application
| WB, IHC-P |
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Primary Accession | Q86SF2 |
Reactivity | Human |
Host | Rabbit |
Clonality | Polyclonal |
Calculated MW | 75kDa |
Dilution | IHC-P (5 µg/ml) |
Gene ID | 51809 |
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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 |
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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 |
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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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