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SAB4200311

Sigma-Aldrich

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

~1.5 mg/mL, affinity isolated antibody

Sinónimos:

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

Código UNSPSC:
12352203
NACRES:
NA.41

origen biológico

rabbit

conjugado

unconjugated

forma del anticuerpo

affinity isolated antibody

tipo de anticuerpo

primary antibodies

clon

polyclonal

Formulario

buffered aqueous solution

mol peso

antigen ~130 kDa

reactividad de especies

canine, human

concentración

~1.5 mg/mL

técnicas

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

Nº de acceso UniProt

Condiciones de envío

dry ice

temp. de almacenamiento

−20°C

modificación del objetivo postraduccional

unmodified

Información sobre el gen

human ... MGEA5(10724)

Descripción general

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.

Inmunógeno

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.

Aplicación

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)

Acciones bioquímicas o fisiológicas

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).

Forma física

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

Cláusula de descargo de responsabilidad

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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Código de clase de almacenamiento

12 - Non Combustible Liquids

Clase de riesgo para el agua (WGK)

WGK 1

Punto de inflamabilidad (°F)

Not applicable

Punto de inflamabilidad (°C)

Not applicable


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Certificados de análisis (COA)

Lot/Batch Number

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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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