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FUT8 encodes an enzyme belonging to the family of fucosyltransferases. 再加上，我们可以发FUT8 抗体 (67) 和 FUT8 试剂盒 (19)和数多这个蛋白质的别的产品。
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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 (显示 CA2 蛋白)+) influx and CaMKII (显示 CAMK2G 蛋白) and then impair LTP (显示 SCP2 蛋白).
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 (显示 ITK 蛋白)), a critical process for malignant transformation of tumor, via the transactivation of beta-catenin (显示 CTNNB1 蛋白)/lymphoid enhancer-binding factor-1 (LEF-1 (显示 LEF1 蛋白)).
These data suggest that reduced Fut8 activity is associated with the progression of COPD (显示 ARCN1 蛋白) and serum Fut8 activity is a non-invasive predictive biomarker candidate for progression and exacerbation of COPD (显示 ARCN1 蛋白).
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 (显示 EGF 蛋白) induced phosphorylation levels of the EGF receptor (EGFR (显示 EGFR 蛋白)) were substantially blocked in Fut8-/- cells. Consistent with this, EGFR (显示 EGFR 蛋白)-mediated JNK (显示 MAPK8 蛋白) or ERK (显示 EPHB2 蛋白) activation was significantly suppressed in Fut8-/- cells.
EGFR (显示 EGFR 蛋白)-trypsin-PAR-2 (显示 F2RL1 蛋白) pathway is suppressed in Fut8-/- mice.
Reduced alpha4 1 integrin/vascular cell adhesion molecule 1 (显示 VCAM1 蛋白) interactions lead to impaired pre-B cell repopulation in alpha 1,6-fucosyltransferase deficient mice
Vascular endothelial growth factor receptor-2 (VEGFR-2 (显示 KDR 蛋白)) expression was significantly suppressed in Fut8(-/-) mice, suggesting that Fut8 was required for VEGFR-2 (显示 KDR 蛋白) expression.
This study thus provides insights into the interplay among FUT8, N-acetylglucosaminyltransferase (显示 GCNT2 蛋白) , and GnT-V (显示 MGAT5 蛋白) in N-linked glycosylation during the assembly of glycoproteins.
Our results reveal a positive feedback mechanism of FUT8-mediated receptor core fucosylation that promotes TGF-b signaling and EMT (显示 ITK 蛋白), thus stimulating breast cancer cell invasion and metastasis.
FUT8 is regulated by microRNAs and has a role in hepatocellular carcinoma progression
the possibility that the higher fucose levels on cell surface glycans of aggressive anaplastic thyroid cancer samples (ATCs (显示 CHST14 蛋白)), compared to those of less aggressive papillary thyroid cancer samples(PTC (显示 F9 蛋白)), may be at least in part responsible for the more aggressive and metastatic phenotype of ATCs (显示 CHST14 蛋白) compared to PTCs, as the expression levels of FUCA1 (显示 FUCA1 蛋白) and FUT8 were inversely related in these two types of cancers.
We observed a strong correlation between EVI1 (显示 MECOM 蛋白) 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 (显示 EPO 蛋白) in the FUT8-overexpressed HEK293S GnT I (显示 MGAT1 蛋白)(-/-) 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 (显示 MLXIP 蛋白)-198 was shown to target the 3'UTR of FUT8 directly to downregulate FUT8 expression.
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