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The protein encoded by MGAT5 belongs to the glycosyltransferase family. Zusätzlich bieten wir Ihnen MGAT5 Kits (15) und MGAT5 Proteine (6) und viele weitere Produktgruppen zu diesem Protein an.
Showing 10 out of 49 products:
Human Polyclonal MGAT5 Primary Antibody für 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
Study indicates that Mgat5 genotype affects both behaviour and physical outcomes in response to early life stress, suggesting some shared pathways for both in a mouse model. These results provide a starting point for studying the mechanisms by which protein N-glycosylation mediates the effects of early life adversity.
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 (zeige WNT2 Antikörper)/beta-catenin (zeige CTNNB1 Antikörper) signaling pathway by modulating N-glycosylation of Wnt (zeige WNT2 Antikörper) receptors, which changes cancer stem cells in colorectal tumors, causing altered colon tumorigenesis and adenoma progression in Apc (zeige APC Antikörper)(min/+) mice
this study suggests that the GnT-V expression is inversely correlated with radiation sensitivity in prostate cancer(PCa (zeige ENPP1 Antikörper))cells
The GnT-V prevented steatohepatitis progression through modulating lymphocyte and HSC (zeige FUT1 Antikörper) functions.
GnT-V overexpression promotes EMT (zeige ITK Antikörper) and keratinocyte migration in part through enhanced EGF receptor (zeige EGFR Antikörper) 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 (zeige ERBB2 Antikörper)-mediated signaling pathways that, in turn, regulate the relative proportion of tumor initiating cells and the latency of her-2 (zeige ERBB2 Antikörper)-driven tumor onset
A secreted type of beta 1,6-N-acetylglucosaminyltransferase V (zeige MGAT5B Antikörper) (GnT-V) induces tumor angiogenesis without mediation of glycosylation: a novel function of GnT-V distinct from the original glycosyltransferase (zeige GTDC2 Antikörper) activity.
The best homology model is consistent with available experimental data. The three-dimensional model, the structure of the enzyme catalytic site and binding information obtained for the donor and acceptor can be useful in studies of the catalytic mechanism and design of inhibitors of GnT-V.
Our data suggest that oxidative stress induces the overexpression of MGAT5 via the regulation of the focal adhesion kinase-extracellular signal-regulated kinase signaling pathway, which, in turn, affects the function of endothelial cells, which then participates in the pathogenesis of preeclampsia.
PTPalpha (zeige PTPRA Antikörper) is identified as a novel substrate of N-Acetylglucosaminyltransferase V (GnT-V) and could be a factor regulating promotion of migration in breast cancer cells
Tunicamycin, an inhibitor of N-glycan biosynthesis, was also able to enhance the radiosensitivity of U251 cells. Thus, our results suggest that development of therapeutic approaches targeting N-linked beta1,6-GlcNAc branches which are encoded by N-acetylglucosaminyltransferase V may be a promising strategy in glioblastoma treatment
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 (zeige MMP2 Antikörper)/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 (zeige LGALS3 Antikörper) to the RPE (zeige RPE Antikörper) cell surface and inhibitory effects on RPE (zeige RPE Antikörper) 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
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