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Human MGEA5 Protein expressed in HEK-293 Cells - ABIN2725936
Ding, Ping, Shi, Feng, Zheng, Song, Zhu: Thiamet-G-mediated inhibition of O-GlcNAcase sensitizes human leukemia cells to microtubule-stabilizing agent paclitaxel. in Biochemical and biophysical research communications 2014
Beta-N-acetylhexosaminidase substrate recognition and specificity
Tax interacts with the host OGT/OGA complex and inhibits the activity of OGT-bound OGA.
TGFBR3 and/or MGEA5 rearrangements are much more common in hybrid hemosiderotic fibrolipomatous tumor-myxoinflammatory fibroblastic sarcomas than in classical myxoinflammatory fibroblastic sarcomas.
Data suggest that the substrate specificity of O-GlcNAcase/OGA does not extend to proteins/peptides modified with S-GlcNAc (an analog of O-GlcNAc); proteins modified with S-GlcNAc appear to be stable against O-GlcNAcase/OGA hydrolysis.
hOGA forms an unusual arm-in-arm homodimer in which the catalytic domain of one monomer is covered by the stalk domain of the sister monomer to create a substrate-binding cleft.
OGA is physically associated with the known RNA polymerase II (pol II) pausing/elongation factors SPT5 and TRIM28-KAP1-TIF1beta, and a purified OGA-SPT5-TIF1beta complex has elongation properties.
the O-linked N-acetylglucosamine (O-GlcNAc) processing enzymes, O-GlcNAc-transferase (OGT) and O-GlcNAcase (OGA), interact with the (A)gamma-globin promoter at the -566 GATA repressor site
E2F1 negatively regulates both Ogt and Mgea5 expression in an Rb1 protein-dependent manner.
OGA overexpression in endothelial cells improves endothelial function and may have a beneficial effect on coronary vascular complications in diabetes.
Amino acid composition of splice variants, post-translational modifications, and stable associations with regulatory proteins influence subcellular distribution/substrate specificity of OGA and OGT (O-linked N-acetylglucosamine transferase). [REVIEW]
This work identifies the first target of miR-539 in the heart and the first miRNA that regulates OGA.
Report the presence of TGFBR3 and/or MGEA5 rearrangements in pleomorphic hyalinizing angiectatic tumors and the spectrum of related neoplasms.
Estrogen replacement therapy and plyometric training influence muscle OGT and OGA gene expression, which may be one of the mechanisms by which HRT and PT prevent aging-related loss of muscle mass.
O-linked beta-N-acetylglucosaminylation (O-GlcNAcylation) in primary and metastatic colorectal cancer clones and effect of N-acetyl-beta-D-glucosaminidase silencing on cell phenotype and transcriptome.
Data show that the interplay between O-GlcNAc and phosphorylation on proteins and indicate that these effects can be mediated by changes in hOGT and hOGA kinetic activity.
Analysis of urinary content of MGEA5 and OGT may be useful for bladder cancer diagnostics.
Decrease in MGEA5 and increase in O-GlcNAc transferease expression in higher grade tumors suggests that increased O-GlcNAc modification may be implicated in breast tumor progression and metastasis.
Chromosomal translocation t(1;10) is consistent with rearrangements of TGFBR3 and MGEA5 in both myxoinflammatory fibroblastic sarcoma and hemosiderotic fibrolipomatous tumor.
Reducing ChREBP(OG) levels via OGA overexpression decreased lipogenic protein content (ACC, FAS), prevented hepatic steatosis, and improved the lipidic profile of OGA-treated db/db mice.
Direct evidence links muscle atrophy and the disruption of O-GlcNAcase activity in male bitransgenic mice.
Furthermore, both Ogt and Oga were required for the reversion from primed ESD-EpiSCs to naive rESCs. These findings indicate that O-GlcNAcylation plays an important role in the survival of primed ESD-EpiSCs and in their reversion to naive rESCs.
Oga(+/-) mice resist high-fat diet-induced obesity with ameliorated hepatic steatosis and improved glucose metabolism
plays a critical role in placental vasculogenesis by modulating HIF-1alpha stabilization
Conditional disruption of the O-GlcNAcase in mice leads to metabolic deregulation and semi-penetrant perinatal lethality.
The O-GlcNAcase active site resembles those of glycosidases which carry out the hydrolysis of GlcNAc linkages in a substrate-assisted acid-base manner.
Data suggest that enzymes in hexosamine biosynthesis pathway and downstream protein O-GlcNAcylation are important for preimplantation development; these include Oga, Gfpt (glutamine-fructose-6-P aminotransferase), and Ogt (O-GlcNAc transferase).
The dynamic modification of cytoplasmic and nuclear proteins by O-linked N-acetylglucosamine (O-GlcNAc) addition and removal on serine and threonine residues is catalyzed by OGT (MIM 300255), which adds O-GlcNAc, and MGEA5, a glycosidase that removes O-GlcNAc modifications (Gao et al., 2001
, bifunctional protein NCOAT
, hyaluronidase in meningioma
, meningioma-expressed antigen 5
, nuclear cytoplasmic O-GlcNAcase and acetyltransferase