Anti-MGEA5/OGA Antibody Picoband® Fluoro647 Conjugated

Protein O-GlcNAcase (EC 3.2.1.169, OGA, glycoside hydrolase O-GlcNAcase, O-GlcNAcase, BtGH84, O-GlcNAc hydrolase) is an enzyme with systematic name (protein) -3-O- (N-acetyl-D-glucosaminyl) -L-serine/threonine N-acetylglucosaminyl hydrolase. 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.

Could induce apoptosis in a BH3 domain-dependent manner. The interaction network of Bcl-2 family members may play a key role in modulation RTL10/BOP intrinsic apoptotic signaling activity.

1. Comtesse, N., Maldener, E., Meese, E. Identification of a nuclear variant of MGEA5, a cytoplasmic hyaluronidase and a beta-N-acetylglucosaminidase. Biochem. Biophys. Res. Commun. 283: 634-640, 2001. 2. Forsythe, M. E., Love, D. C., Lazarus, B. D., Kim, E. J., Prinz, W. A., Ashwell, G., Krause, M. W., Hanover, J. A. Caenorhabditis elegans ortholog of a diabetes susceptibility locus: oga-1 (O-GlcNAcase) knockout impacts O-GlcNAc cycling, metabolism, and dauer. Proc. Nat. Acad. Sci. 103: 11952-11957, 2006. 3. Gao, Y., Wells, L., Comer, F. I., Parker, G. J., Hart, G. W. Dynamic O-glycosylation of nuclear and cytosolic proteins: cloning and characterization of a neutral, cytosolic, beta-N-acetylglucosaminidase from human brain. J. Biol. Chem. 276: 9838-9845, 2001.