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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
Tax (show CNTN2 Proteins) interacts with the host OGT (show OGT Proteins)/OGA complex and inhibits the activity of OGT (show OGT Proteins)-bound OGA.
TGFBR3 (show TGFBR3 Proteins) 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 (show OGT Proteins)); proteins modified with S-GlcNAc appear to be stable against O-GlcNAcase/OGA hydrolysis.
hOGA (show OAT Proteins) 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 (show SUPT5H Proteins) and TRIM28-KAP1-TIF1beta (show TRIM28 Proteins), and a purified OGA-SPT5 (show SUPT5H Proteins)-TIF1beta (show TRIM28 Proteins) complex has elongation properties.
the O-linked N-acetylglucosamine (O-GlcNAc (show OGT Proteins)) processing enzymes, O-GlcNAc (show OGT Proteins)-transferase (OGT (show OGT Proteins)) and O-GlcNAcase (OGA), interact with the (A)gamma-globin (show HBG1 Proteins) promoter at the -566 GATA repressor (show ZBTB32 Proteins) site
E2F1 (show E2F1 Proteins) negatively regulates both Ogt (show OGT Proteins) and Mgea5 expression in an Rb1 (show RB1 Proteins) 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 (show OGT Proteins)). [REVIEW]
This work identifies the first target of miR (show MLXIP Proteins)-539 in the heart and the first miRNA that regulates OGA.
Furthermore, both Ogt (show OGT Proteins) and Oga were required for the reversion from primed ESD (show ESD Proteins)-EpiSCs to naive rESCs. These findings indicate that O-GlcNAcylation plays an important role in the survival of primed ESD (show ESD Proteins)-EpiSCs and in their reversion to naive rESCs.
the O-linked N-acetylglucosamine (O-GlcNAc) processing enzymes, O-GlcNAc-transferase (OGT (show OGT Proteins)) and O-GlcNAcase (OGA), interact with the (A)gamma-globin (show HBG1 Proteins) promoter at the -566 GATA repressor (show ZBTB32 Proteins) site
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 (show HIF1A Proteins) 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