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Merck
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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

UNSPSC Code:
12352203
NACRES:
NA.41

Key Documents

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biological source

rabbit

Quality Level

200

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

Gene Information

human ... MGEA5(10724)

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.

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).

Physical form

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

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.

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Storage Class Code

12 - Non Combustible Liquids

WGK

WGK 1

Flash Point(F)

Not applicable

Flash Point(C)

Not applicable

Regulatory Information

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Certificates of Analysis (COA)

Lot/Batch Number
0000314963
0000314963
0000245267
0000245267
0000134863

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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)
Hijacking of the O-GlcNAcZYME complex by the HTLV-1 Tax oncoprotein facilitates viral transcription
Groussaud D, et al.
PLoS Pathogens, 13(7), e1006518-e1006518 (2017)
Hexosamine Biosynthetic Pathway and Glycosylation Regulate Cell Migration in Melanoma Cells
de Queiroz RM, et al.
Frontiers in Oncology, 9 (2019)
Nutrient-driven O-GlcNAc cycling-think globally but act locally
Harwood KR and Hanover JA
Journal of Cell Science, 127(9), 1857-1867 (2014)
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