The ST6GALNAC1 Polyclonal Antibody (PAC052758) is a valuable tool for researchers studying ST6GALNAC1, an enzyme involved in glycosylation processes. This antibody, produced in rabbits, exhibits high reactivity with human samples and is validated for use in various applications, including Western blotting.ST6GALNAC1 is a key player in the glycosylation pathway, contributing to the addition of glycans to proteins and lipids. Dysregulation of this enzyme has been implicated in various diseases, including cancer and neurodegenerative disorders.
By targeting ST6GALNAC1, researchers can gain insights into glycosylation patterns and their roles in disease progression.With its specificity and sensitivity, the ST6GALNAC1 Polyclonal Antibody is an essential tool for investigating glycosylation processes and their implications in health and disease. It enables precise detection and analysis of ST6GALNAC1 expression in different cell types, making it a valuable asset for studies in glycobiology and biomedical research.
Western Blot. Positive WB detected in: HepG2 whole cell lysate. All lanes: ST6GALNAC1 antibody at 2.7µg/ml. Secondary. Goat polyclonal to rabbit IgG at 1/50000 dilution. Predicted band size: 69 kDa. Observed band size: 69 kDa.
Immunohistochemistry of paraffin-embedded human skin tissue using PACO52758 at dilution of 1:100.
Immunohistochemistry of paraffin-embedded human melanoma using PACO52758 at dilution of 1:100.
Background:
Golgi membrane, alpha-N-acetylgalactosaminide alpha-2,6-sialyltransferase activity, sialyltransferase activity, ganglioside biosynthetic process, oligosaccharide metabolic process, protein glycosylation, protein N-linked glycosylation via asparagine
ST6GALNAC1: Belongs to the glycosyltransferase 29 familyProtein type: Transferase; Membrane protein, integral; EC 2.4.99.3; Glycan Metabolism - O-glycan biosynthesisChromosomal Location of Human Ortholog: 17q25.1Cellular Component: Golgi membraneMolecular Function: alpha-N-acetylgalactosaminide alpha-2,6-sialyltransferase activityBiological Process: ganglioside biosynthetic process; oligosaccharide metabolic process; protein amino acid N-linked glycosylation via asparagine
UniProt Protein Details:
NCBI Summary:
Glycosylation of proteins affects cell-cell interaction, interactions with the matrix, and the functions of intracellular molecules. ST6GALNAC1 transfers a sialic acid, N-acetylneuraminic acid (NeuAc), in an alpha-2,6 linkage to O-linked GalNAc residues. The cancer-associated sialyl-Tn (sTn) antigen is formed by ST6GALNAC1-catalyzed sialylation of GalNAc residues on mucins (Ikehara et al., 1999 [PubMed 10536037]; Sewell et al., 2006 [PubMed 16319059]).[supplied by OMIM, Mar 2008]