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Merck

SAB4200311

Anti-O-GlcNAcase (OGA) (C-terminal region) antibody produced in rabbit

~1.5 mg/mL, affinity isolated antibody

Synonym(s):

Anti-Beta-N-acetylhexosaminidase, Anti-Hexosaminidase C, Anti-MEA5, Anti-Meningioma expressed antigen 5 (hyaluronidase), Anti-N-acetyl-beta-D-glucosaminidase, Anti-N-acetyl-beta-glucosaminidase, Anti-NCOAT, Anti-O-GlcNAcase, Anti-OGA

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About This Item

NACRES:
NA.41
UNSPSC Code:
12352203

Key Documents

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Product Name

Anti-O-GlcNAcase (OGA) (C-terminal region) antibody produced in rabbit, ~1.5 mg/mL, affinity isolated antibody

biological source

rabbit

conjugate

unconjugated

antibody form

affinity isolated antibody

antibody product type

primary antibodies

clone

polyclonal

form

buffered aqueous solution

mol wt

antigen ~130 kDa

species reactivity

canine, human

concentration

~1.5 mg/mL

technique(s)

immunoprecipitation (IP): 3-6 μg using MDCK cells.
western blot: 2-4 μg/mL using MCF7 cell extracts.

UniProt accession no.

O60502

shipped in

dry ice

storage temp.

−20°C

target post-translational modification

unmodified

Quality Level

200

Gene Information

human ... MGEA5(10724)

Application

Anti-O-GlcNAcase (OGA) (C-terminal region) antibody produced in rabbit has been used in:
  • Western blotting
  • Immunoprecipitation
  • Microarray analysis

Applications in which this antibody has been used successfully, and the associated peer-reviewed papers, are given below.
Western Blotting (1 paper)

Biochem/physiol Actions

β-N-acetylglucosaminidase (OGA) along with O-GlcNAc transferase (OGT) are key enzymes which regulate cycling O-linked N-acetylglucosamine. OGA is responsible for cleaving the modification from target proteins. OGA is also glycosylated by OGT and a regulatory feedback loop exists between these two enzymes. OGA and OGT have been found to strongly associate together in transcriptional co-repression complexes with histone deacetylases (HDACs).

Disclaimer

Unless otherwise stated in our catalog or other company documentation accompanying the product(s), our products are intended for research use only and are not to be used for any other purpose, which includes but is not limited to, unauthorized commercial uses, in vitro diagnostic uses, ex vivo or in vivo therapeutic uses or any type of consumption or application to humans or animals.

General description

The β-N-acetylglucosaminidase (OGA) gene encodes two alternatively spliced isoforms that are widely expressed in mammalian tissues. OGA (also known as O-GlcNAcase, MGEA5, NCOAT) belongs to the family of 84 glycoside hydrolases. The longer OGA form is a bifunctional nuclear/cytoplasmic enzyme that contains two distinct domains, an O-GlcNAcase domain at the N-terminus and a C-terminal putative histone acetyltransferase (HAT) domain. The shorter OGA form contains only the N-terminal O-GlcNAcase domain.

Immunogen

synthetic peptide corresponding to a sequence near the C-terminus of human O-GlcNAcase (OGA), conjugated to KLH. The corresponding sequence is identical in human OGA isoform B, and highly conserved (single amino acid substitution) in rat and mouse OGA.

Physical form

Solution in 0.01 M phos­phate buffered saline, pH 7.4, containing 15 mM sodium azide.

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Storage Class

12 - Non Combustible Liquids

wgk

WGK 1

flash_point_f

Not applicable

flash_point_c

Not applicable

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Certificates of Analysis (COA)

Lot/Batch Number
059M4853V
028M4783V
028M4783
086M4785V
086M4785

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Seokwon Jo et al.
Frontiers in endocrinology, 13, 1040014-1040014 (2022-11-18)
Protein O-GlcNAcylation is a nutrient and stress-sensitive protein post-translational modification (PTM). The addition of an O-GlcNAc molecule to proteins is catalyzed by O-GlcNAc transferase (OGT), whereas O-GlcNAcase (OGA) enzyme is responsible for removal of this PTM. Previous work showed that
Nutrient-driven O-GlcNAc cycling-think globally but act locally
Harwood KR and Hanover JA
Journal of Cell Science, 127(9), 1857-1867 (2014)
O-GlcNAc cycling: implications for neurodegenerative disorders
Lazarus BD, et al.
The International Journal of Biochemistry & Cell Biology, 41(11), 2134-2146 (2009)
Cell Metabolism Control Through O-GlcNAcylation of STAT5: A Full or Empty Fuel Tank Makes a Big Difference for Cancer Cell Growth and Survival
Rauth M, et al.
International Journal of Molecular Sciences, 20(5), 1028-1028 (2019)
Changes in O-linked N-acetylglucosamine (O-GlcNAc) homeostasis activate the p53 pathway in ovarian cancer cells
de Queiroz RM, et al.
The Journal of Biological Chemistry, 291(36), 18897-18914 (2016)
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