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The GALNT13 protein is a member of the UDP-N-acetyl-alpha-D-galactosamine:polypeptide N-acetylgalactosaminyltransferase (GalNAcT\; EC 188.8.131.52) family, which initiate O-linked glycosylation of mucins (see MUC3A, MIM 158371) by the initial transfer of N-acetylgalactosamine (GalNAc) with an alpha-linkage to a serine or threonine residue.[supplied by OMIM, Apr 2004].. De plus, nous expédions GALNT13 Anticorps (49) et GALNT13 Protéines (7) et beaucoup plus de produits pour cette protéine.
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This study suggests that ppGalNAc-T13 contributes to neuronal differentiation through glycosylating and stabilizing PDPN (Montrer PDPN Kits ELISA), which provides insights into the regulatory roles of O-glycosylation in mammalian neural development.
high expression of the ppGalNAc-T13 gene generates tTn (Montrer TTN Kits ELISA) antigen on Syndecan 1 (Montrer SDC1 Kits ELISA), leading to enhanced invasion and metastasis via the formation of a complex consisting of integrin alpha5beta1, Syndecan 1 (Montrer SDC1 Kits ELISA), and MMP-9 (Montrer MMP9 Kits ELISA) in the glycolipid-enriched microdomain/rafts.
These data suggested that high expression of pp-GalNAc-T13 gene generated trimeric Tn antigen on Syndecan-1 (Montrer SDC1 Kits ELISA), leading to the enhanced metastasis.
cloning and characterization of pp-GalNAc-T13; expressed in all neuroblastoma cells examined and primary cultured neurons but not in glioblastoma cells and primary cultured astrocytes
the GalNAc-T13 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.
Study showed that GALNT13 mRNA is highly expressed in lung cancer patients and associated with poor prognosis.
Data suggest microRNA-424 regulates expression of MGAT4A (Montrer MGAT4A Kits ELISA) (mannoside beta-1,4-N-acetylglucosaminyltransferase A), OGT (O-linked N-acetylglucosamine transferase (Montrer OGT Kits ELISA)), and GALNT13 (polypeptide N-acetylgalactosaminyltransferase 13) in mammary epithelium.
we integrated different computational tools to perform the in silico analysis of clinically significant mutations (nsSNPs/single amino acid change) at both functional and structural levels, found in human GALNT3 (Montrer GALNT3 Kits ELISA), GALNT8, GALNT12 (Montrer GALNT12 Kits ELISA), and GALNT13 genes.
GALNT13 encodes a glycosyltransferase enzyme responsible for the synthesis of O-glycan.
The GALNT13 protein is a member of the UDP-N-acetyl-alpha-D-galactosamine:polypeptide N-acetylgalactosaminyltransferase (GalNAcT\; EC 184.108.40.206) family, which initiate O-linked glycosylation of mucins (see MUC3A, MIM 158371) by the initial transfer of N-acetylgalactosamine (GalNAc) with an alpha-linkage to a serine or threonine residue.
UDP-N-acetyl-alpha-D-galactosamine:polypeptide N-acetylgalactosaminyltransferase 13 (GalNAc-T13)
, polypeptide N-acetylgalactosaminyltransferase 13
, polypeptide N-acetylgalactosaminyltransferase 13-like
, UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase 13
, polypeptide GalNAc transferase 13
, pp-GaNTase 13
, protein-UDP acetylgalactosaminyltransferase 13
, GalNAc transferase 13