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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 Galnt1 Proteins (10) and many more products for this protein.
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 enzyme family covering a single known glycosidic linkage.
Polypeptide GalNAcT (show B4GALNT1 ELISA Kits)-1 plays a predominant role in leukocyte recruitment in vivo by attaching functionally relevant O-linked glycans to L-selectin (show SELL ELISA Kits) ligands.
Growth factor stimulation regulates O-glycosylation initiation in a Src (show SRC ELISA Kits)-dependent fashion by GalNac-T (show B4GALNT1 ELISA Kits) 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 ELISA Kits) and BSP (show KLK6 ELISA Kits).
Expression of GALNT3 (show GALNT3 ELISA Kits) was reduced in CAD (show CAD ELISA Kits) patients, and down regulation of GALNT3 (show GALNT3 ELISA Kits) contributed to endothelial injury by promoting apoptosis and up-regulating the expression of MMP-2 (show MMP2 ELISA Kits) and MMP-14 (show MMP14 ELISA Kits) genes via p38 MAPK (show MAPK14 ELISA Kits) activation.
appears to be responsive to the inhibition of GALNT1 and SHH (show SHH ELISA Kits) signaling
Study demonstrates that down-regulation of GALNT1 is sufficient to suppress malignant phenotype of HCC (show FAM126A ELISA Kits) cells by decreasing EGFR (show EGFR ELISA Kits) 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 ELISA Kits) I at all putative O-glycosylation sites within human mucin (show SLC13A2 ELISA Kits) MUC1 (show MUC1 ELISA Kits) containing 5 tandem repeats.
The results indicated that IL-4 (show IL4 ELISA Kits)-treated LS174T cells are able to produce mucins with a higher degree of O-glycosylation than untreated counterparts.
GalNAc T10 (show GALNT10 ELISA Kits) has a large and pronounced glycopeptide preference for Ser (show SIGLEC1 ELISA Kits)/Thr (show TRH ELISA Kits)-O-GalNAc only at the +1 position from the acceptor site, whereas T1 and T2 have significantly reduced and variable preferences for Ser (show SIGLEC1 ELISA Kits)/Thr (show TRH ELISA Kits)-O-GalNAc.
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