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anti-Human ST3GAL1 Anticorps:
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Human Polyclonal ST3GAL1 Primary Antibody pour WB - ABIN520192
Petrosyan, Cheng: Golgi fragmentation induced by heat shock or inhibition of heat shock proteins is mediated by non-muscle myosin IIA via its interaction with glycosyltransferases. dans Cell stress & chaperones 2014
Show all 3 Pubmed References
Study demonstrates that ST3GalI regulates ovarian cancer cell migration and peritoneal dissemination via EGFR signaling.
ST3Gal I and ST6Gal I have different sialic acid donor specificity.
Describe differential expression profiles of alpha-2, 3-sialyltransferases (ST) and miR-4701-5p in three pairs of chronic myeloid leukemia (CML) cell lines and 48 clinical samples of bone marrow mononuclear cells from CML patients. miR-4701-5p directly targeted ST3GAL1 to reduce CML cells resistance to multiple chemotherapeutics in vitro.
rs113350588 and rs1048479 may alter the function of ST3GAL1. The GC haplotype was associated with an increased risk of death in subjects with influenza. The AT haplotype was associated with an increased risk of severe disease and death.
ST3GAL1-associated transcriptomic program portends poor prognosis in glioma patients with higher tumor grades.ST3Gal1-regulated self-renewal traits are crucial to the sustenance of glioblastoma multiforme growth.
Results show that ST3Gal1 uses GM130-GRASP65 and giantin, whereas C2GnT-L uses only giantin for Golgi targeting and defective giantin dimerization in PC-3 and DU145 prostate cancer cells causes fragmentation of the Golgi and prevents its targeting.
NMIIA is the master regulator of Golgi fragmentation induced by heat shock or inhibition/depletion of HSP70/90 through interaction with gylosyltransferases.
the high expression of ST3Gal I and ST6Gal I, in skin tumors, is associated with tumors with greater potential for invasion and metastasis, as in the case of squamous cell carcinoma, and this may be related to their behavior.
Induction of COX-2 in breast cancer cell line results in the increased expression of ST3Gal-I.
Down-regulation of ST3GalI is correlated with breast cancer
Over-expression of ST3Gal-I promotes mammary tumorigenesis.
ST3Gal.I plays the major role in the sialylation of the T antigen in bladder cancer.
Although the human ST3Gal I has four N-glycan attachment sites in its catalytic domain that are potentially glycosylated, none necessary for enzyme activity, but N-glycosylation contributes to the folding and trafficking of the enzyme.
sialyltransferases expression and activity are increased in Grave's disease
ST3Gal-I inactivation or enzymatic removal of its product renders CD8+ T cells, but not CD4+ T cells, susceptible to apoptosis by differential cross-linking of O-glycoproteins in the absence of interleukin-2 and T-cell receptor (TCR) signaling.
regulation of O-glycosylation controls sLe(x) expression, and also suggest that O-glycans may have a function in dendritic cells migration
evidence of the association of bipolar disorder with SIAT4A was seen
these results identified the core promoter region in the pST3Gal I promoter and demonstrated that Smad-3 binding to the Samd-3 binding site at -1020 is essential for transcriptional activation of pST3Gal I in TGF-beta1-induced PK-15 cells.
ST3GAL-1 is an independent adverse prognostic factor for recurrence and survival of patients with clear cell renal cell carcinoma
tryptophan and cysteine residues conserved in ST3Gal I are critical for its activity
tissue-specific alterations in sialylation and sialic acid 9-O-acetylation in knockout mice
ST3Gal-I mRNA is extensively expressed during Th2, but not Th1 differentiation; suggests that lack of ST3Gal-I expression in Th1 cells allows the formation of surface core2 O-glycans and supports their interactions with endothelial selectins
was not found to play a role in regulating synthesis of selectin ligands nor in vitro rolling of marrow-derived neutrophils on E- or P-selectins presented by Chinese hamster ovary cells
STsGal-I deficiency shows no discernible effect on the pattern of CD8 noncognate binding during thymocyte development and does not impact susceptibility of thymocytes to CD8-induced apoptosis.
St3gal-1 functions to protect CD8 T cells from apoptosis
The protein encoded by this gene is a type II membrane protein that catalyzes the transfer of sialic acid from CMP-sialic acid to galactose-containing substrates. The encoded protein is normally found in the Golgi but can be proteolytically processed to a soluble form. Correct glycosylation of the encoded protein may be critical to its sialyltransferase activity. This protein, which is a member of glycosyltransferase family 29, can use the same acceptor substrates as does sialyltransferase 4B. Two transcript variants encoding the same protein have been found for this gene. Other transcript variants may exist, but have not been fully characterized yet.
, CMP-N-acetylneuraminate-beta-galactosamide-alpha-2,3-sialyltransferase 1
, ST3Gal I
, alpha 2,3-ST 1
, beta-galactoside alpha-2,3-sialyltransferase 1
, sialyltransferase 4A
, sialyltransferase 4A (beta-galactosidase alpha-2,3-sialytransferase)
, sialyltransferase 4A (beta-galactoside alpha-2,3-sialyltransferase)
, sialyltransferase 4A (beta-galactoside alpha-2,3-sialytransferase)
, gal beta-1,3 GalNAc alpha-2,3 sialyltransferase
, CMP-N-acetylneuraminate: [beta-galactosidase alpha-2,3] sialytransferase
, Gal beta1,3 GalNAc alpha2,3 sialyltransferase
, ST3GAL-I sialyltransferase
, sialyltransferase ST3Gal-I