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Key Documents

ABE1372

Sigma-Aldrich

Anti-OGG1 Antibody

from rabbit, purified by affinity chromatography

Synonyme(s) :

N-glycosylase/DNA lyase, 1.8-oxoguanine DNA glycosylase, DNA-(apurinic or apyrimidinic site) lyase, AP lyase

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About This Item

Code UNSPSC :
12352203
eCl@ss :
32160702
Nomenclature NACRES :
NA.41

Source biologique

rabbit

Niveau de qualité

Forme d'anticorps

affinity isolated antibody

Type de produit anticorps

primary antibodies

Clone

polyclonal

Produit purifié par

affinity chromatography

Espèces réactives

human

Technique(s)

western blot: suitable

Numéro d'accès NCBI

Numéro d'accès UniProt

Conditions d'expédition

wet ice

Modification post-traductionnelle de la cible

unmodified

Informations sur le gène

human ... OGG1(4968)

Description générale

The protein named N-glycosylase/DNA lyase or alternatively, 8-oxoguanine (8-OxoG) DNA glycosylase or AP lyase, and encoded by the gene named OGG1/MMH/MUTM/OGH1, is a DNA repair enzyme that incises DNA at 8-oxoG residues and excises 7,8-dihydro-8-oxoguanine and 2,6-diamino-4-hydroy-5-N-methylformamidopyrimidine (FAPY) from damaged DNA. OGG1 also has beta-lyase activity that nicks DNA 3′ to the lesion. OGG1 is localized to the nucleus and nucleoplasm; in UVA-irradiated cells it can be found in the nuclear speckles. There is also an isoform found in the mitochondrion. Interestingly, OGG1 appears to be play a critical role in repairing mtDNA damage; mtDNA damage is linked to mitochondrial dysfunction, increased oxidative stress, and insulin resistance in muscle cells, and studies using OGG1 knockouts or over expressing OGG1 demonstrate that OGG1 is important for proper mtDNA damage repair and that disruption of OGG1 can lead to increased mtROS (reactive oxygen species) production and subsequent regulation of downstream events leading to insulin resistance in skeletal muscle. OGG1, or rather defects in OGG1 function, are also associated with a number of carcinomas, particularly Renal Cell Carcinomas of various cell types.

Immunogène

Recombinant protein corresponding to human OGG1.

Application

Research Category
Epigenetics & Nuclear Function
Research Sub Category
Nuclear Receptors
This Anti-OGG1 Antibody is validated for use in Western Blotting for the detection of OGG1.
Western Blotting Analysis: A representative lot detected recombinant protein OGG1 (Bjoras, M., et al. (1997). EMBO. 16(20):6314–6322).
Western Blotting Analysis: A representative lot detected OGG1 in Melphalan-resistant cells (Sousa, M., et al. (2013). PLOS One. 8(2):e55493).

Qualité

Evaluated by Western Blotting in recombinant protein OGG1.

Western Blotting Analysis: A 1:1,000 dilution of this antibody detected recombinant protein OGG1 in 1 µg of cell lysate.

Description de la cible

~38 kDa observed

Forme physique

Affinity purified
Purified rabbit polyclonal in buffer containing PBS with 0.05% sodium azide.

Stockage et stabilité

Stable for 1 year at 2-8°C from date of receipt.

Autres remarques

Concentration: Please refer to lot specific datasheet.

Clause de non-responsabilité

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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Code de la classe de stockage

10 - Combustible liquids

Classe de danger pour l'eau (WGK)

WGK 2

Point d'éclair (°F)

Not applicable

Point d'éclair (°C)

Not applicable


Certificats d'analyse (COA)

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Consulter la Bibliothèque de documents

M Bjorâs et al.
The EMBO journal, 16(20), 6314-6322 (1997-10-08)
The guanine modification 7,8-dihydro-8-oxoguanine (8-oxoG) is a potent premutagenic lesion formed spontaneously at high frequencies in the genomes of aerobic organisms. We have characterized a human DNA repair glycosylase for 8-oxoG removal, hOGH1 (human yeast OGG1 homologue), by molecular cloning
Mirta M L Sousa et al.
PloS one, 8(2), e55493-e55493 (2013-02-14)
Alterations in checkpoint and DNA repair pathways may provide adaptive mechanisms contributing to acquired drug resistance. Here, we investigated the levels of proteins mediating DNA damage signaling and -repair in RPMI8226 multiple myeloma cells and its Melphalan-resistant derivative 8226-LR5. We

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