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The protein encoded by MGAT5 belongs to the glycosyltransferase family. Additionally we are shipping MGAT5 Kits (13) and MGAT5 Proteins (6) and many more products for this protein.
Showing 10 out of 47 products:
Human Polyclonal MGAT5 Primary Antibody for ELISA, WB - ABIN561815
Hamanoue, Ikeda, Ogata, Takamatsu: Predominant expression of N-acetylglucosaminyltransferase V (GnT-V) in neural stem/progenitor cells. in Stem cell research 2015
Overexpression of GnT-V exacerbated murine experimental colitis by inducing macrophage dysfunction, thereby enhancing colorectal tumorigenesis
Expression of GnT-V was also elevated in bleomycin (BLM)-injected sclerotic skin, and MGAT5(-/-) mice were resistant to BLM-induced skin sclerosis with reduced collagen type 1 alpha1 content.
GnT-V regulates the canonical Wnt (show WNT2 Antibodies)/beta-catenin (show CTNNB1 Antibodies) signaling pathway by modulating N-glycosylation of Wnt (show WNT2 Antibodies) receptors, which changes cancer stem cells in colorectal tumors, causing altered colon tumorigenesis and adenoma progression in Apc (show APC Antibodies)(min/+) mice
this study suggests that the GnT-V expression is inversely correlated with radiation sensitivity in prostate cancer(PCa (show ENPP1 Antibodies))cells
The GnT-V prevented steatohepatitis progression through modulating lymphocyte and HSC (show FUT1 Antibodies) functions.
GnT-V overexpression promotes EMT (show ITK Antibodies) and keratinocyte migration in part through enhanced EGF receptor (show EGFR Antibodies) signaling.
Mgat5-dependent glycosylation of proteins can modulate acquired immune responses, but it is not essential for the development of OVA-induced eosinophilic airway inflammation.
GnT-V expression and its branched glycan products effectively modulate her-2 (show ERBB2 Antibodies)-mediated signaling pathways that, in turn, regulate the relative proportion of tumor initiating cells and the latency of her-2 (show ERBB2 Antibodies)-driven tumor onset
A secreted type of beta 1,6-N-acetylglucosaminyltransferase V (show MGAT5B Antibodies) (GnT-V) induces tumor angiogenesis without mediation of glycosylation: a novel function of GnT-V distinct from the original glycosyltransferase (show GTDC2 Antibodies) activity.
expression of Mgat5 sensitized cells to multiple cytokines;Galectin-3 (show LGALS3 Antibodies) cross-linked Mgat5-modified N-glycans on epidermal growth factor (show EGF Antibodies) and transforming growth factor-beta receptors at the cell surface and delayed their removal by constitutive endocytosis
the knockdown of GnTV significantly suppressed the proliferation, migration and invasion (P<0.05) of the SMMC7721/R cells.
role in the inhibition of trophoblast cell invasion and migration during early pregnancy by direct or indirect regulation of MMP2 (show MMP2 Antibodies)/9 activity
the level of TGFBR1 and early osteogenic differentiation were abolished in the DPSCs transfected with siRNA for GnT-V knockdown...GnT-V plays a critical role in the hexosamine-induced activation of TGF-b signaling and osteogenic differentiation
binding of recombinant Gal-3 (show LGALS3 Antibodies) to the RPE (show RPE Antibodies) cell surface and inhibitory effects on RPE (show RPE Antibodies) attachment and spreading largely dependent on interaction with Mgat5 modified N-glycans
Mgat5 plays an important role in early spontaneous miscarriage in humans.
Gnt-V caused tumour growth more quickly
High expression of GnT-V was observed in infiltrating cells in skin section samples from systemic and localized patients with scleroderma.
MGAT5 protein and gene expression in in uveal and cutaneous melanoma cells
UDP-galactose (show B4GALT1 Antibodies) (SLC35A2 (show SLC35A2 Antibodies)) and UDP-N-acetylglucosamine (show MGAT4B Antibodies) (SLC35A3 (show SLC35A3 Antibodies)) Transporters Form Glycosylation-related Complexes with Mannoside Acetylglucosaminyltransferases (Mgats).
Human Mgat5 increases amino acid uptake, intracellular levels of glycolytic and TCA intermediates, as well as HEK293 cell growth.
The protein encoded by this gene belongs to the glycosyltransferase family. It catalyzes the addition of beta-1,6-N-acetylglucosamine to the alpha-linked mannose of biantennary N-linked oligosaccharides present on the newly synthesized glycoproteins. It is one of the most important enzymes involved in the regulation of the biosynthesis of glycoprotein oligosaccharides. Alterations of the oligosaccharides on cell surface glycoproteins cause significant changes in the adhesive or migratory behavior of a cell. Increase in the activity of this enzyme has been correlated with the progression of invasive malignancies.
Alpha-1,6-mannosylglycoprotein 6-beta-N-acetylglucosaminyltransferase A
, Alpha-mannoside beta-1,6-N-acetylglucosaminyltransferase
, GlcNAc-T V
, Mannoside acetylglucosaminyltransferase 5
, N-acetylglucosaminyl-transferase V
, alpha-1,6-mannosylglycoprotein 6-beta-N-acetylglucosaminyltransferase A
, alpha-mannoside beta-1,6-N-acetylglucosaminyltransferase
, beta1,6N-acetylglucosaminyltransferase V
, glcNAc-T V
, mannoside acetylglucosaminyltransferase 5
, N-acetylglucosaminyltransferase V
, alpha-1,6-mannosyl-glycoprotein 6-beta-N-acetylglucosaminyltransferase