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Human Monoclonal B3GNT2 Primary Antibody for IF, IHC - ABIN2716501
Mkhikian, Mortales, Zhou, Khachikyan, Wu, Haslam, Kavarian, Dell, Demetriou: Golgi self-correction generates bioequivalent glycans to preserve cellular homeostasis. in eLife 2016
Human Polyclonal B3GNT2 Primary Antibody for ELISA, WB - ABIN548158
Hayashi, Nakamori, Okami, Nagano, Dono, Umeshita, Sakon, Narimatsu, Monden: Association between expression levels of CA 19-9 and N-acetylglucosamine-beta;1,3-galactosyltransferase 5 gene in human pancreatic cancer tissue. in Pathobiology : journal of immunopathology, molecular and cellular biology 2003
we confirmed the involvement of BGNT-1.1 in ciliated sensory neuron function and morphogenesis. BGNT-1.1 functions at the trans-Golgi network of sheath cells (glia) to influence dye-filling and cilium length, in a cell non-autonomous manner. Notably, BGNT-1.1 is the orthologue of human B3GNT1/B4GAT1, a glycosyltransferase associated with Walker-Warburg syndrome (WWS).
Study provides evidence that mutations in B3GNT2, B4GALT2, and ST6GALNAC2 underlie aberrant glycosylation, and contribute to the pathogenesis of molecular subsets of colon and other gastrointestinal malignancies.
High B3GNT2 expression is associated with hepatocellular carcinoma.
data reveals beta3GnT2 and polyLacNAc may be involved in the progression of the pre-malignant lesions of human the uterine cervix.
beta3Gal-T5, controlled by the intestinal homeoproteins, may play an important role in the specific function of intestinal cells by modifying the carbohydrate structure of glycoproteins
beta3Gal-T5 is presumed to be responsible for the synthesis of CA 19-9 in pancreatic cancer tissue.
beta 3Gal-T5 plays a relevant role in gastrointestinal and pancreatic tissues counteracting the glycosylation pattern associated with malignancy
beta1, 3-N-acetylglucosaminyltransferase is similar to a new protein, beta3-GnTL1
up-regulation of beta3Gn-T8 in differentiated cells increases poly-N-acetyllactosamine chains by activating intrinsic beta3Gn-T2.
These data clearly suggest that GCNT2 functions in vivo together with beta3GnT2 to determine poly-N-acetyllactosamine (PLN) levels in olfactory neurons by regulating beta1,6-branches that promote PLN extension.
These results identify a novel function for beta3GnT2 glycosylation in maintaining expression of layer-specific vomeronasal receptors
Beta3GnT2(-/-) mice exhibit a relatively small deficit in their ability to discriminate divergent odors.
The results suggested taht beta3GnT2 maintains adenylyl cyclase-3 signaling and axon guidance molecule expression in the olfactory epithelium.
In beta1,3-N-acetylglucosaminyltransferase (B3gnt2) B3gnt2-deficient (B3gnt2-/-) mice, the number of polylactosamine structures was markedly lower than in wild-type mice
This gene encodes a member of the beta-1,3-N-acetylglucosaminyltransferase family. This enzyme is a type II transmembrane protein. It prefers the substrate of lacto-N-neotetraose, and is involved in the biosynthesis of poly-N-acetyllactosamine chains.
UDP-GlcNAc:betaGal beta-1,3-N-acetylglucosaminyltransferase 1
, beta-1,3-N-acetylglucosaminyltransferase bGnT-1
, beta-1,3-N-acetylglucosaminyltransferase bGnT-2
, UDP-Gal:betaGlcNAc beta 1,3-galactosyltransferase, polypeptide 6
, beta-1,3-N-acetylglucosaminyltransferase 1
, beta-1,3-N-acetylglucosaminyltransferase 2
, UDP-GlcNAc:betaGal beta-1,3-N-acetylglucosaminyltransferase 2
, N-acetyllactosaminide beta-1,3-N-acetylglucosaminyltransferase 2