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Galnt1 encodes a member of the UDP-N-acetyl-alpha-D-galactosamine:polypeptide N-acetylgalactosaminyltransferase (GalNAc-T) family of enzymes. Additionally we are shipping Galnt1 Antibodies (22) and many more products for this protein.
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Study show that in Galnt1 null mouse, there is compromised cardiac function that mimics human congenital heart disease suggesting that Galnt1 expression is required for normal heart valve development.
The GALNT1 is the glycosyltransferase (show GTDC2 Proteins) enzyme family covering a single known glycosidic linkage.
Polypeptide GalNAcT (show B4GALNT1 Proteins)-1 plays a predominant role in leukocyte recruitment in vivo by attaching functionally relevant O-linked glycans to L-selectin (show SELL Proteins) ligands.
Growth factor stimulation regulates O-glycosylation initiation in a Src (show SRC Proteins)-dependent fashion by GalNac-T (show B4GALNT1 Proteins) redistribution from golgi to the endoplasmic reticulum.
ppGalNAcT-1 to be indispensable for O-glycosylation at specific sites of the bone glycoproteins OPN (show SPP1 Proteins) and BSP (show KLK6 Proteins).
We have elucidated a novel miR-30-GALNT1/2 axis whose dysregulation increases the proportion of inactive proBNP secreted by the heart and impairs the compensatory actions of BNP during the progression of heart failure.
the GalNAc-T13 (show GALNT13 Proteins) isoform is predicted to function similarly to GalNAc-T1 against peptide substrates in vivo, in contrast to a prior report, but is unique by being selectively expressed in the brain.
Expression of GALNT3 (show GALNT3 Proteins) was reduced in CAD patients, and down regulation of GALNT3 (show GALNT3 Proteins) contributed to endothelial injury by promoting apoptosis and up-regulating the expression of MMP-2 (show MMP2 Proteins) and MMP-14 (show MMP14 Proteins) genes via p38 MAPK (show MAPK14 Proteins) activation.
appears to be responsive to the inhibition of GALNT1 and SHH (show SHH Proteins) signaling
Study demonstrates that down-regulation of GALNT1 is sufficient to suppress malignant phenotype of HCC (show FAM126A Proteins) cells by decreasing EGFR (show EGFR Proteins) signaling.
Utilizing unnatural glycopeptide substrates for GalNAc-T3 we demonstrated that the GalNAc-specific sugar recognition of the lectin domain regulates further glycosylation.
the present analysis fails to replicate an earlier reported association of a GALNT1 variant with risk of ovarian cancer
First simultaneous kinetic description of O-glycosylation events by recombinant UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase (show B4GALNT2 Proteins) I at all putative O-glycosylation sites within human mucin (show SLC13A2 Proteins) MUC1 (show MUC1 Proteins) containing 5 tandem repeats.
This gene encodes a member of the UDP-N-acetyl-alpha-D-galactosamine:polypeptide N-acetylgalactosaminyltransferase (GalNAc-T) family of enzymes. GalNAc-Ts initiate mucin-type O-linked glycosylation in the Golgi apparatus by catalyzing the transfer of GalNAc to serine and threonine residues on target proteins. They are characterized by an N-terminal transmembrane domain, a stem region, a lumenal catalytic domain containing a GT1 motif and Gal/GalNAc transferase motif, and a C-terminal ricin/lectin-like domain. GalNAc-Ts have different, but overlapping, substrate specificities and patterns of expression. Transcript variants derived from this gene that utilize alternative polyA signals have been described in the literature.
polypeptide N-acetylgalactosaminyltransferase 1
, UDP-N-acetyl-alpha-D-galactosamine:polypeptide N-acetylgalactosaminyltransferase 1 (GalNAc-T1)
, polypeptide N-acetylgalactosaminyltransferase 1-like
, UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase 1
, polypeptide GalNAc transferase 1
, pp-GaNTase 1
, protein-UDP acetylgalactosaminyltransferase 1
, GalNAc transferase 1
, polypeptide GalNAc transferase T1