Mouse Anti-OGA Recombinant Antibody (A1080) (CBMAB-AP11813LY)

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Basic Information

Host Animal
Mouse
Clone
A1080
Application
ELISA, IF, IHC, WB
Immunogen
Fusion protein of MGEA5
Specificity
Human
Antibody Isotype
IgG1
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
Purity
Affinity purity
Storage
Store at +4°C short term (1-2 weeks). Aliquot and store at -20°C long term. Avoid repeated freezethaw cycles.
More Infomation

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
UniProt ID
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
E-AB-27245
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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