SAB4200311
Anti-O-GlcNAcase (OGA) (C-terminal region) antibody produced in rabbit
~1.5 mg/mL, affinity isolated antibody
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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
UNSPSC Code:
12352203
NACRES:
NA.41
Recommended Products
biological source
rabbit
Quality Level
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.
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)
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.
WGK
WGK 1
Flash Point(F)
Not applicable
Flash Point(C)
Not applicable
Regulatory Information
常规特殊物品
Certificates of Analysis (COA)
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Hexosamine Biosynthetic Pathway and Glycosylation Regulate Cell Migration in Melanoma Cells
de Queiroz RM, et al.
Frontiers in Oncology, 9 (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)
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)
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)
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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