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Mouse Anti-OGA Recombinant Antibody (CF286) (CBMAB-FT212LY)

The product is antibody recognizes MGEA5 . The antibody CF286 immunoassay techniques such as: ELISA, WB, IF, IHC.
See all OGA antibodies

Summary

Host Animal
Mouse
Specificity
Human
Clone
CF286
Antibody Isotype
IgG2a
Application
ELISA, WB, IF, IHC

Basic Information

Immunogen
meningioma expressed antigen 5 (hyaluronidase)
Specificity
Human
Antibody Isotype
IgG2a
Clonality
Monoclonal
Application Notes
The COA includes recommended starting dilutions, optimal dilutions should be determined by the end user.

Formulations & Storage [For reference only, actual COA shall prevail!]

Format
Liquid
Buffer
50% glycerol
Preservative
0.02% sodium azide
Storage
Store at +4°C short term (1-2 weeks). Aliquot and store at -20°C long term. Avoid repeated freezethaw cycles.

Target

Full Name
O-GlcNAcase
Introduction
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 [PubMed 11148210]).[supplied by OMIM, Mar 2008]
Entrez Gene ID
10724
UniProt ID
O60502
Alternative Names
HEXC, KIAA0679, MEA5
Function
Isoform 1
Cleaves GlcNAc but not GalNAc from O-glycosylated proteins. Can use p-nitrophenyl-beta-GlcNAc and 4-methylumbelliferone-GlcNAc as substrates but not p-nitrophenyl-beta-GalNAc or p-nitrophenyl-alpha-GlcNAc (in vitro) (PubMed:11148210).
Does not bind acetyl-CoA and does not have histone acetyltransferase activity (PubMed:24088714).
Isoform 3
Cleaves GlcNAc but not GalNAc from O-glycosylated proteins. Can use p-nitrophenyl-beta-GlcNAc as substrate but not p-nitrophenyl-beta-GalNAc or p-nitrophenyl-alpha-GlcNAc (in vitro), but has about six times lower specific activity than isoform 1.
Biological Process
Isoform 3
Nucleus
Isoform 1
Cytoplasm
PTM
Proteolytically cleaved by caspase-3 during apoptosis. The fragments interact with each other; cleavage does not decrease enzyme activity.

Pagesy, P., Bouaboud, A., Feng, Z., Hulin, P., & Issad, T. (2022). Short O-GlcNAcase is targeted to the mitochondria and regulates mitochondrial reactive oxygen species level. Cells, 11(11), 1827.

Muha, V., Authier, F., Szoke-Kovacs, Z., Johnson, S., Gallagher, J., McNeilly, A., ... & van Aalten, D. M. (2021). Loss of O-GlcNAcase catalytic activity leads to defects in mouse embryogenesis. Journal of Biological Chemistry, 296.

Bartolomé-Nebreda, J. M., Trabanco, A. A., Velter, A. I., & Buijnsters, P. (2021). O-GlcNAcase inhibitors as potential therapeutics for the treatment of Alzheimer’s disease and related tauopathies: analysis of the patent literature. Expert opinion on therapeutic patents, 31(12), 1117-1154.

Stephen, H. M., Adams, T. M., & Wells, L. (2021). Regulating the regulators: mechanisms of substrate selection of the O-GlcNAc cycling enzymes OGT and OGA. Glycobiology, 31(7), 724-733.

Kositzke, A., Fan, D., Wang, A., Li, H., Worth, M., & Jiang, J. (2021). Elucidating the protein substrate recognition of O-GlcNAc transferase (OGT) toward O-GlcNAcase (OGA) using a GlcNAc electrophilic probe. International journal of biological macromolecules, 169, 51-59.

Elbatrawy, A. A., Kim, E. J., & Nam, G. (2020). O‐GlcNAcase: emerging mechanism, substrate recognition and small‐molecule inhibitors. ChemMedChem, 15(14), 1244-1257.

Martínez-Viturro, C. M., Trabanco, A. A., Royes, J., Fernández, E., Tresadern, G., Vega, J. A., ... & Bartolomé-Nebreda, J. M. (2020). Diazaspirononane nonsaccharide inhibitors of O-GlcNAcase (OGA) for the treatment of neurodegenerative disorders. Journal of medicinal chemistry, 63(22), 14017-14044.

Muha, V., Fenckova, M., Ferenbach, A. T., Catinozzi, M., Eidhof, I., Storkebaum, E., ... & van Aalten, D. M. (2020). O-GlcNAcase contributes to cognitive function in Drosophila. Journal of Biological Chemistry, 295(26), 8636-8646.

Singh, J. P., Qian, K., Lee, J. S., Zhou, J., Han, X., Zhang, B., ... & Yang, X. (2020). O-GlcNAcase targets pyruvate kinase M2 to regulate tumor growth. Oncogene, 39(3), 560-573.

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For research use only. Not intended for any clinical use.

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