OGG1 Human

8-Oxoguanine DNA Glycosylase Human Recombinant
Cat. No.
BT22991
Source
Escherichia Coli.
Synonyms
HMMH, HOGG1, MUTM, OGH1, AP lyase.
Appearance
Sterile filtered colourless solution.
Purity
Greater than 90.0% as determined by SDS-PAGE.
Usage
THE BioTek's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
Shipped with Ice Packs
In Stock

Description

OGG1 Recombinant Human produced in E.Coli is a single, non-glycosylated polypeptide chain containing 368 amino acids (1-345 a.a.) and having a molecular mass of 41.2 kDa. The OGG1 is fused to 23 amino acid His-Tag at N-terminus and purified by proprietary chromatographic techniques.

Product Specs

Introduction
OGG1, a DNA glycosylase enzyme involved in base excision repair, is the primary enzyme responsible for excising 7,8-dihydro-8-oxoguanine (8-oxoG), a mutagenic base byproduct resulting from exposure to reactive oxygen species (ROS). OGG1 exhibits beta lyase activity, nicking DNA 3' to the lesion.
Description
Recombinant Human OGG1, produced in E. coli, is a single, non-glycosylated polypeptide chain of 368 amino acids (specifically, amino acids 1 through 345) with a molecular weight of 41.2 kDa. This OGG1 protein is fused to a 23 amino acid His-Tag at its N-terminus and purified using proprietary chromatographic techniques.
Physical Appearance
A clear, colorless solution that has been sterilized by filtration.
Formulation
A 0.5mg/ml solution prepared in phosphate-buffered saline (PBS) at a pH of 7.4 and supplemented with 40% glycerol.
Stability
For short-term storage (up to 2-4 weeks), the product can be stored at 4°C. For extended storage, it should be frozen at -20°C. The addition of a carrier protein (0.1% HSA or BSA) is recommended for long-term storage. Repeated freezing and thawing of the product should be avoided.
Purity
Purity is determined to be greater than 90.0% by SDS-PAGE analysis.
Synonyms
HMMH, HOGG1, MUTM, OGH1, AP lyase.
Source
Escherichia Coli.
Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH TGSMPARALL PRRMGHRTLA STPALWASIP CPRSELRLDL VLPSGQSFRW REQSPAHWSG VLADQVWTLT QTEEQLHCTV YRGDKSQASR PTPDELEAVR KYFQLDVTLA QLYHHWGSVD SHFQEVAQKF QGVRLLRQDP IECLFSFICS SNNNIARITG MVERLCQAFG PRLIQLDDVT YHGFPSLQAL AGPEVEAHLR KLGLGYRARY VSASARAILE EQGGLAWLQQ LRESSYEEAH KALCILPGVG TKVADCICLM ALDKPQAVPV DVHMWHIAQRDYSWHPTTSQ AKGPSPQTNK ELGNFFRSLW GPYAGWAQAV LFSADLRQCR HAQEPPAKRRKGSKGPEG.

Product Science Overview

Importance of 8-Oxoguanine (8-oxoG)

Among the four DNA bases, guanine is the most susceptible to oxidation. The oxidation product, 8-oxoG, is the most prevalent base lesion found in DNA. If not repaired, 8-oxoG can pair with adenine during DNA replication, leading to G:C to T:A transversion mutations, which can contribute to carcinogenesis and other genetic disorders .

Mechanism of Action

OGG1 initiates the repair process by recognizing and binding to the 8-oxoG lesion. It then excises the damaged base through its glycosylase activity, creating an apurinic/apyrimidinic (AP) site. The enzyme also possesses AP lyase activity, which cleaves the DNA backbone at the AP site, facilitating further repair by other enzymes in the BER pathway .

Recombinant Human OGG1

Recombinant human OGG1 is produced using genetic engineering techniques, where the human OGG1 gene is cloned and expressed in a suitable host, such as Escherichia coli. This allows for the production of large quantities of the enzyme for research and therapeutic purposes .

Applications

Recombinant OGG1 is widely used in research to study DNA repair mechanisms, oxidative stress, and the role of DNA damage in diseases. It is also utilized in developing therapeutic strategies to enhance DNA repair in conditions characterized by oxidative damage .

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