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Documenti fondamentali

ABE1372

Sigma-Aldrich

Anti-OGG1 Antibody

from rabbit, purified by affinity chromatography

Sinonimo/i:

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

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About This Item

Codice UNSPSC:
12352203
eCl@ss:
32160702
NACRES:
NA.41

Origine biologica

rabbit

Livello qualitativo

Forma dell’anticorpo

affinity isolated antibody

Tipo di anticorpo

primary antibodies

Clone

polyclonal

Purificato mediante

affinity chromatography

Reattività contro le specie

human

tecniche

western blot: suitable

N° accesso NCBI

N° accesso UniProt

Condizioni di spedizione

wet ice

modifica post-traduzionali bersaglio

unmodified

Informazioni sul gene

human ... OGG1(4968)

Descrizione generale

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.

Immunogeno

Recombinant protein corresponding to human OGG1.

Applicazioni

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).

Qualità

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.

Descrizione del bersaglio

~38 kDa observed

Stato fisico

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

Stoccaggio e stabilità

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

Altre note

Concentration: Please refer to lot specific datasheet.

Esclusione di responsabilità

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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Codice della classe di stoccaggio

10 - Combustible liquids

Classe di pericolosità dell'acqua (WGK)

WGK 2

Punto d’infiammabilità (°F)

Not applicable

Punto d’infiammabilità (°C)

Not applicable


Certificati d'analisi (COA)

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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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