The UDP-N-acetyl-alpha-D-galactosamine:polypeptide N-acetylgalactosaminyltransferase (GalNAc-T) family of enzymes are substrate-specific proteins that catalyze the transfer of GalNAc (N-acetylgalactosamine) to serine and threonine residues onto various proteins, thereby initiating mucin-type O-linked glycosylation in the Golgi apparatus. GalNAc-T5 (Polypeptide N-acetylgalactosaminyltransferase 5), also known as UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase 5, is a 940 amino acid protein that displays enzymatic activity toward EA2 peptide substrate with weaker activity toward Muc2 or Muc 1b substrates. Its N-terminal domain is involved in substrate binding and manganese coordination, while the C-terminal domain is involved in UDP-Gal binding and catalytic reaction. EXT2 directly interacts with GalNAc-T5, suggesting that these proteins may corroborate in glycosaminoglycan synthesis.

GALNAC T5;
N acetylgalactosaminyltransferase;
Polypeptide GalNAc transferase 5;
polypeptide N -acetylgalactosaminyltransferase 5;
pp GaNTase 5;
Protein UDP acetylgalactosaminyltransferase 5;
UDP GalNAc:polypeptide N acetylgalactosaminyltransferase 5;
UDP N acetyl alpha D galactosamine:polypeptide N acetylgalactosaminyltransferase 5.

Human,Mouse

IHC,IF,ICC,ELISA

IHC 1:50-1:200
IF 1:100-500
ICC 1:100-1:400
ELISA 1:5000-10000

106kD

11227

Q7Z7M9

https://www.uniprot.org/uniprotkb/Q7Z7M9

Cell Membrane and Golgi Apparatus

KLH conjugated synthetic peptide derived from human GALNT5

Rabbit

Polyclonal

IgG

affinity purified by Protein A

Liquid

0.01M TBS (pH7.4) with 1% BSA, 0.02% Proclin300 and 50% Glycerol.

Shipped at 4℃. Store at -20℃ for one year. Avoid repeated freeze/thaw cycles.