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The protein encoded by FUT7 is a Golgi stack membrane protein that is involved in the creation of sialyl-Lewis X antigens. Additionally we are shipping Fucosyltransferase 7 (Alpha (1,3) Fucosyltransferase) Antibodies (48) and Fucosyltransferase 7 (Alpha (1,3) Fucosyltransferase) Kits (4) and many more products for this protein.
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The bfut7 gene encodes an enzyme that mainly ensures the synthesis of the sialyl-lewis X (show FUT4 Proteins) motif.
FUT7 silencing causes inhibition of adhesion and migration of HepG2 hepatocellular carcinoma cells in vitro.
FUT7 overexpression significantly promoted monocyte-endothelial adhesion, while FUT7 knockdown obviously inhibited IL-1beta (show IL1B Proteins)-induced monocyte-endothelial adhesion
The DNA demethylation within the fut7 gene controls selectin ligand expression in humans, including the inducible topographic commitment of T cells for skin and inflamed sites.
This study presents the first example of a distinct regulatory mechanism involving transcriptional down-regulation of Fut7 by MAPCs that could modulate the trafficking behavior of T cells in vivo.
After transfection of JAR (show MYO6 Proteins) cells with fucosyltransferase VII, the expression of FUT7 and sLeX synthesis were increased, and the percent adhesion of trophoblast cells to RL95-2 cell monolayer was significantly increased.
Overexpression of alpha1,3 FucT-VII promoted the expression of CD24 (show CD24 Proteins) and SLe X and is associated with colorectal carcinoma metastases.
The Fuc-T VII (show TH Proteins) promoter is transactivated by Tax (show CNTN2 Proteins) in concert with CBP (show CREBBP Proteins) through a CRE-like sequence in a manner similar to that of viral CRE in HTLV-1 LTR.
H-Ras (show HRAS Proteins) mediates FucT-VII induction in Jurkat T cells via the activation of the Raf (show RAF1 Proteins), PI3K (show PIK3CA Proteins), and a distinct, H-Ras (show HRAS Proteins)-specific effector signaling pathway.
These results suggest that the FucT-VII may be a major regulator of the biosynthesis of the sLe(x)-epitopes on T lymphoblasts.
human FucT-IV (show FUT4 Proteins) and -VII (show TH Proteins) both contribute and cooperate in regulating L-selectin (show SELL Proteins)-, P-selectin (show SELP Proteins)-, and E-selectin (show SELE Proteins)-dependent rolling on PSGL-1 (show SELPLG Proteins), with FucT-VII playing a predominant role in conferring selectin binding activity to PSGL-1 (show SELPLG Proteins)
The DNA demethylation within the fut7 gene controls selectin ligand expression in mice, including the inducible topographic commitment of T cells for skin and inflamed sites.
Cloning of an intragenic region spanning a 1kb region upstream of exon 4 into an enhancer-containing vector indeed elicited fut7 promoter activity in cd4 (show CD4 Proteins) positive T cells.
These results demonstrate that all genetic information essential for appropriate and selective expression of Fut7 in diverse cell types and in response to distinct developmental signals is contained within this comparatively small genetic region.
alpha(1,3)-Fucosyltransferases FUT4 (show FUT4 Proteins) and FUT7 control murine susceptibility to thrombosis.
Functional PSGL-1 generated by basophil FT-IV/VII and its subsequent binding to L-selectin could be one of the essential steps required for initial basophil recruitment and the development of IgE-chronic allergic inflammation in mice.
striking differences between the requirement of FucT-VII and C2GlcNAcT-I for Ligands for E-selectin (show SELE Proteins) and P-selectin (show SELP Proteins) expression in CD4 (show CD4 Proteins)+ T cells.
Loss of the barrier protective molecule TFF3 (show TFF3 Proteins) leads to a profound increase in susceptibility to DSS (show PMP22 Proteins)-induced colitis, and this can be abrogated by reducing Fuc-TVII-dependent leukocyte recruitment.
FucT-VII is an important pathophysiologic mediator of renal ischemia reperfusion injury, structural damage, and neutrophil infiltration postischemia.
Efficient recruitment of activated lymphocytes to the brain in a model mimicking early inflammation during experimental allergic encephalomyelitis is controlled by FucT-VII.
FT-IV and FT-VII (show TH Proteins) are both important contributors to selectin-dependent eosinophil recruitment to the skin and may represent therapeutic targets for treating diseases in which eosinophil recruitment contributes to pathophysiology.
The protein encoded by this gene is a Golgi stack membrane protein that is involved in the creation of sialyl-Lewis X antigens. The encoded protein can direct the synthesis of the E-selectin-binding sialyl-Lewis X moiety.
, alpha-1,3-fucosyltransferase 7
, fucosyltransferase 7
, alpha 1,3 fucosyltransferase
, alpha (1,3) fucosyltransferase
, fucosyltransferase VII
, galactoside 3-L-fucosyltransferase
, selectin ligand synthase
, selectin-ligand synthase
, fucosyltransferase 7 (alpha (1,3) fucosyltransferase)