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Rabbit Anti-OGA Recombinant Antibody (CBFYM-2176) (CBMAB-M2358-FY)

This product is rabbit antibody that recognizes MGEA5. The antibody CBFYM-2176 can be used for immunoassay techniques such as: WB, IP, IHC-P.
See all OGA antibodies

Summary

Host Animal
Rabbit
Specificity
Mouse, Human
Clone
CBFYM-2176
Antibody Isotype
IgG
Application
WB, IP, IHC-P

Basic Information

Immunogen
A synthetic peptide corresponding to residues in human MGEA5
Specificity
Mouse, Human
Antibody Isotype
IgG
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
PBS, pH 7.2, 50% glycerol, 0.05% BSA
Preservative
0.01% Sodium azide
Storage
Store at +4°C short term (1-2 weeks). Aliquot and store at -20°C long term. Avoid repeated freeze/thaw cycles.

Target

Full Name
O-GlcNAcase
Introduction
The dynamic modification of cytoplasmic and nuclear proteins by O-linked N-acetylglucosamine addition and removal on serine and threonine residues is catalyzed by OGT, which adds O-GlcNAc, and MGEA5, a glycosidase that removes O-GlcNAc modifications.
Entrez Gene ID
Human10724
Mouse76055
UniProt ID
HumanO60502
MouseQ9EQQ9
Alternative Names
Meningioma Expressed Antigen 5 (Hyaluronidase); Nuclear Cytoplasmic O-GlcNAcase And Acetyltransferase; N-Acetyl-Beta-D-Glucosaminidase; Meningioma-Expressed Antigen 5; N-Acetyl-Beta-Glucosaminidase; Beta-N-Acetylglucosaminidase; Beta-N-Acetylhexosaminidase; Beta-Hexosaminidase; NCOAT; 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.

Custom Antibody Labeling

We also offer labeled antibodies developed using our catalog antibody products and nonfluorescent conjugates (HRP, AP, Biotin, etc.) or fluorescent conjugates (Alexa Fluor, FITC, TRITC, Rhodamine, Texas Red, R-PE, APC, Qdot Probes, Pacific Dyes, etc.).

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