Rabbit Polyclonal GALNT7 antibody. Suitable for WB and reacts with Human samples. Cited in 3 publications. Immunogen corresponding to Recombinant Fragment Protein within Human GALNT7 aa 1-500.
pH: 7
Preservative: 0.01% Thimerosal (merthiolate)
Constituents: 10% Glycerol (glycerin, glycerine), 1.21% Tris, 0.75% Glycine
WB | |
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Human | Tested |
Mouse | Predicted |
Rat | Predicted |
Species | Dilution info | Notes |
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Species Human | Dilution info 1/500.00000 - 1/3000.00000 | Notes - |
Species | Dilution info | Notes |
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Species Mouse, Rat | Dilution info - | Notes - |
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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.
N-acetylgalactosaminyltransferase 7, Polypeptide GalNAc transferase 7, Protein-UDP acetylgalactosaminyltransferase 7, UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase 7, GalNAc-T7, pp-GaNTase 7, GALNT7
Rabbit Polyclonal GALNT7 antibody. Suitable for WB and reacts with Human samples. Cited in 3 publications. Immunogen corresponding to Recombinant Fragment Protein within Human GALNT7 aa 1-500.
pH: 7
Preservative: 0.01% Thimerosal (merthiolate)
Constituents: 10% Glycerol (glycerin, glycerine), 1.21% Tris, 0.75% Glycine
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GALNT7 also known as polypeptide N-acetylgalactosaminyltransferase 7 is an enzyme involved in the initial step of O-glycosylation. This process involves the transfer of N-acetylgalactosamine (GalNAc) to serine or threonine residues on proteins. GALNT7 weighs approximately 72 kilodaltons and belongs to the family of GalNAc-transferases. The expression of GALNT7 is widespread predominantly found in the liver and pancreas but is also present in other tissues.
GALNT7 catalyzes the addition of GalNAc to proteins in the Golgi apparatus. This modification is important for mucin-type O-glycan biosynthesis which influences protein folding stability and cellular signaling. GALNT7 does not function as part of a large protein complex but individually modifies substrate proteins. Its enzymatic activity impacts multiple cellular processes including cell adhesion and immune response.
GALNT7 participates significantly in the mucin-type O-glycan biosynthesis pathway. This pathway is essential for generating glycoproteins commonly seen on cell surfaces and in secretions. GALNT7 does not act alone; it works alongside other GalNAc-transferases like GALNT2 which can influence substrate specificity and tissue-specific glycosylation. Another related pathway is the protein O-linked glycosylation pathway where GALNT7 interacts with proteins like MUC1 playing a role in glycoprotein configuration.
GALNT7 has associations with cancers particularly colorectal cancer. Abnormal glycosylation patterns resulting from altered GALNT7 activity can contribute to tumor growth and metastasis. Researchers study GALNT7 expression in cancer tissues to understand its role in oncogenesis. Additionally changes in GALNT7 activity may relate to inflammatory disorders such as Crohn's disease where mucin glycosylation influences intestinal barrier function and inflammation. The interaction between GALNT7 and MUC1 in these contexts is of significant interest especially in examining how it influences disease progression.
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7.5% SDS-PAGE
All lanes: Western blot - Anti-GALNT7 antibody (ab97645) at 1/10000 dilution
All lanes: A431 whole cell lysate at 30 µg
Predicted band size: 75 kDa
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