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The protein encoded by MGAT5 belongs to the glycosyltransferase family. 再加上，我们可以发MGAT5 抗体 (49) 和 MGAT5 蛋白 (6)和数多这个蛋白质的别的产品。
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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 (显示 WNT2 ELISA试剂盒)/beta-catenin (显示 CTNNB1 ELISA试剂盒) signaling pathway by modulating N-glycosylation of Wnt (显示 WNT2 ELISA试剂盒) receptors, which changes cancer stem cells in colorectal tumors, causing altered colon tumorigenesis and adenoma progression in Apc (显示 APC ELISA试剂盒)(min/+) mice
this study suggests that the GnT-V expression is inversely correlated with radiation sensitivity in prostate cancer(PCa (显示 ENPP1 ELISA试剂盒))cells
The GnT-V prevented steatohepatitis progression through modulating lymphocyte and HSC (显示 FUT1 ELISA试剂盒) functions.
GnT-V overexpression promotes EMT (显示 ITK ELISA试剂盒) and keratinocyte migration in part through enhanced EGF receptor (显示 EGFR ELISA试剂盒) 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 (显示 ERBB2 ELISA试剂盒)-mediated signaling pathways that, in turn, regulate the relative proportion of tumor initiating cells and the latency of her-2 (显示 ERBB2 ELISA试剂盒)-driven tumor onset
A secreted type of beta 1,6-N-acetylglucosaminyltransferase V (显示 MGAT5B ELISA试剂盒) (GnT-V) induces tumor angiogenesis without mediation of glycosylation: a novel function of GnT-V distinct from the original glycosyltransferase 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 (显示 PTPRA ELISA试剂盒) 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 (显示 MMP2 ELISA试剂盒)/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 (显示 LGALS3 ELISA试剂盒) to the RPE cell surface and inhibitory effects on RPE 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