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  • Mouse Anti-OGA Recombinant Antibody (CBFYM-0633)

Mouse Anti-OGA Recombinant Antibody (CBFYM-0633) (CBMAB-M0768-FY)

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Datasheet
SDS
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Datasheet Target References Q & As Review & reward Protocols Associated Products

Basic Information

Host Animal
Mouse
Clone
CBFYM-0633
Application
ELISA, WB
Specificity
Human
Antibody Isotype
IgG2a, k
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
Storage
Store at +4°C short term (1-2 weeks). Aliquot and store at -20°C long term. Avoid repeated freeze/thaw cycles.
More Infomation

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
10724
UniProt ID
O60502
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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Please try the standard protocols which include: protocols, troubleshooting and guide.

Enzyme-linked Immunosorbent Assay (ELISA)
Flow Cytometry
Immunofluorescence (IF)
Immunohistochemistry (IHC)
Immunoprecipitation (IP)
Western Blot (WB)
Enzyme-Linked Immunospot (ELISpot)
Proteogenomics
Other Protocols

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Isotype control

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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