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FUT8 encodes an enzyme belonging to the family of fucosyltransferases. Additionally we are shipping FUT8 Antibodies (57) and FUT8 Kits (18) and many more products for this protein.
Showing 7 out of 11 products:
our study provides the first direct evidence for the involvement of Fut8 in liver regeneration.
Loss of core fucosylation on AMPARs enhanced their heteromerization, which increase sensitivity for postsynaptic depolarization and persistently activate N-methyl-d-aspartate receptors as well as Ca(2 (show CA2 Proteins)+) influx and CaMKII (show CAMK2G Proteins) and then impair LTP (show SCP2 Proteins).
findings define FUT8 as a novel factor for hemoglobin production and demonstrate that core fucosylation plays an important role in erythroid differentiation
FUT8 is up-regulated during epithelial-mesenchymal transition (EMT (show ITK Proteins)), a critical process for malignant transformation of tumor, via the transactivation of beta-catenin (show CTNNB1 Proteins)/lymphoid enhancer-binding factor-1 (LEF-1 (show LEF1 Proteins)).
These data suggest that reduced Fut8 activity is associated with the progression of COPD (show ARCN1 Proteins) and serum Fut8 activity is a non-invasive predictive biomarker candidate for progression and exacerbation of COPD (show ARCN1 Proteins).
Increased expression and activity of alpha-1,6-fucosyltransferase (FUT8) in the liver are strongly linked to the age-related changes in protein glycosylation.
epidermal growth factor (show EGF Proteins) induced phosphorylation levels of the EGF receptor (EGFR (show EGFR Proteins)) were substantially blocked in Fut8-/- cells. Consistent with this, EGFR (show EGFR Proteins)-mediated JNK (show MAPK8 Proteins) or ERK (show EPHB2 Proteins) activation was significantly suppressed in Fut8-/- cells.
EGFR (show EGFR Proteins)-trypsin-PAR-2 (show F2RL1 Proteins) pathway is suppressed in Fut8-/- mice.
Reduced alpha4 1 integrin/vascular cell adhesion molecule 1 (show VCAM1 Proteins) interactions lead to impaired pre-B cell repopulation in alpha 1,6-fucosyltransferase deficient mice
Vascular endothelial growth factor receptor-2 (VEGFR-2 (show KDR Proteins)) expression was significantly suppressed in Fut8(-/-) mice, suggesting that Fut8 was required for VEGFR-2 (show KDR Proteins) expression.
We observed a strong correlation between EVI1 (show MECOM Proteins) and alpha1, 6-fucosyltransferase (FUT8) in the chronic phase of the disease and both of them were found to be up-regulated with the progression of the disease.
results suggest that an appropriate polypeptide context or other adequate structural elements in the acceptor substrate could facilitate the core fucosylation by FUT8
FUT8 is a driver of melanoma metastasis which, when silenced, suppresses invasion and tumor dissemination.
The production of the homogeneous core-fucosylated Man5GlcNAc2 glycoform of EPO (show EPO Proteins) in the FUT8-overexpressed HEK293S GnT I (show MGAT1 Proteins)(-/-) cell line represents the first example of production of fully core-fucosylated high-mannose glycoforms.
Expression of FUT8 can stratify breast cancer tissue and may be considered a prognostic marker for breast cancer patients
MiR (show MLXIP Proteins)-198 was shown to target the 3'UTR of FUT8 directly to downregulate FUT8 expression.
High expression of FUT8 is associated with an unfavorable clinical outcome in patients with potentially curatively resected NSCLCs, suggesting that FUT8 can be a prognostic factor.
Our results suggest that FUT8 may be associated with aggressive PCa (show FLVCR1 Proteins) and thus is potentially useful for its prognosis.
miR-122 and miR-34a are able to target FUT8 3'UTR
Results suggest that FUT4 (show FUT4 Proteins)-, FUT6 (show FUT6 Proteins)- or FUT8-mediated MDR in human HCC (show FAM126A Proteins) is associated with the activation of the PI3K (show PIK3CA Proteins)/Akt (show AKT1 Proteins) pathway and the expression of MRP1 (show MDM4 Proteins).
This gene encodes an enzyme belonging to the family of fucosyltransferases. The product of this gene catalyzes the transfer of fucose from GDP-fucose to N-linked type complex glycopeptides. This enzyme is distinct from other fucosyltransferases which catalyze alpha1-2, alpha1-3, and alpha1-4 fucose addition. The expression of this gene may contribute to the malignancy of cancer cells and to their invasive and metastatic capabilities. Alternative splicing results in multiple transcript variants.
, GDP-fucose--glycoprotein fucosyltransferase
, alpha (1,6) fucosyltransferase
, glycoprotein 6-alpha-L-fucosyltransferase
, Glycoprotein 6-alpha-L-fucosyltransferase
, alpha 1,6 fucosyltransferase