The GALNT11 Polyclonal Antibody (PAC046946) is a powerful tool for researchers studying GALNT11, a glycosyltransferase enzyme involved in protein glycosylation. This antibody, produced in rabbits, exhibits high specificity and sensitivity towards human samples, making it an excellent choice for Western blot applications. By binding to the GALNT11 protein, researchers can investigate its role in various biological processes, particularly in the context of cancer and other diseases.GALNT11 is known for its involvement in protein glycosylation, a post-translational modification crucial for protein function and localization. Dysregulation of GALNT11 has been implicated in cancer progression and metastasis, making it a promising target for therapeutic development.
Research on GALNT11 can provide valuable insights into the mechanisms underlying tumorigenesis and potentially lead to the discovery of new cancer treatments.In summary, the GALNT11 Polyclonal Antibody is a reliable tool for studying the function of GALNT11 in biological processes, with a particular emphasis on cancer research. Its specificity and sensitivity make it a valuable asset for any laboratory conducting investigations into protein glycosylation and its implications for human health.
Immunohistochemistry of paraffin-embedded human gastric cancer using PACO46946 at dilution of 1:100.
Immunofluorescent analysis of Hela cells using PACO46946 at dilution of 1:100 and Alexa Fluor 488-congugated AffiniPure Goat Anti-Rabbit IgG(H+L).
Immunohistochemistry of paraffin-embedded human cervical cancer using PACO46946 at dilution of 1:100.
Background:
Polypeptide N-acetylgalactosaminyltransferase that catalyzes the initiation of protein O-linked glycosylation and is involved in left/right asymmetry by mediating O-glycosylation of NOTCH1. O-glycosylation of NOTCH1 promotes activation of NOTCH1, modulating the balance between motile and immotile (sensory) cilia at the left-right organiser (LRO). Polypeptide N-acetylgalactosaminyltransferases catalyze the transfer of an N-acetyl-D-galactosamine residue to a serine or threonine residue on the protein receptor. Displays the same enzyme activity toward MUC1, MUC4, and EA2 than GALNT1. Not involved in glycosylation of erythropoietin (EPO).
GALNT11: Catalyzes the initial reaction in O-linked oligosaccharide biosynthesis, the transfer of an N-acetyl-D- galactosamine residue to a serine or threonine residue on the protein receptor. Displays the same enzyme activity toward Muc1, Muc4.1, and EA2 than GALNT1. Does not appear to be involved in glycosylation of erythropoietin. Belongs to the glycosyltransferase 2 family. GalNAc-T subfamily. 2 isoforms of the human protein are produced by alternative splicing.Protein type: EC 2.4.1.41; Transferase; Membrane protein, integral; Glycan Metabolism - O-glycan biosynthesisChromosomal Location of Human Ortholog: 7q36.1|7q36.1Cellular Component: Golgi membraneMolecular Function: Notch binding; polypeptide N-acetylgalactosaminyltransferase activityBiological Process: determination of left/right symmetry; Notch receptor processing; O-glycan processing; protein amino acid O-linked glycosylation via threonine; regulation of Notch signaling pathway
