MUTM E.Coli

Formamidopyrimidine-DNA Glycosylase E.Coli Recombinant

Recombinantly produced in E. coli, MUTM is a single polypeptide chain consisting of 289 amino acids (specifically, amino acids 1 to 269). It possesses a molecular mass of 32.4kDa. For purification purposes, a 20 amino acid His-tag is fused to the N-terminus of MUTM, followed by purification using proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT22849
Source
E.coli.
Appearance
A clear and sterile solution.

MutY E.Coli

Adenine DNA Glycosylase E.Coli Recombinant

MutY Recombinant, produced in E.coli, is a single polypeptide chain of 373 amino acids (amino acids 1-350) with a molecular weight of 41.5kDa. It is purified using proprietary chromatographic techniques and is not glycosylated. The recombinant MutY protein has a 23 amino acid His-tag attached to its N-terminus.
Shipped with Ice Packs
Cat. No.
BT22921
Source
E.coli.
Appearance
A clear, colorless solution that has been sterilized by filtration.

OGG1 Human

8-Oxoguanine DNA Glycosylase Human Recombinant

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.
Shipped with Ice Packs
Cat. No.
BT22991
Source
Escherichia Coli.
Appearance
A clear, colorless solution that has been sterilized by filtration.

OGG1 Mouse

8-Oxoguanine DNA Glycosylase Mouse Recombinant

Recombinant Mouse OGG1, produced in E. coli, is a single, non-glycosylated polypeptide chain comprising 368 amino acids (1-345 a.a.) with a molecular weight of 41.3 kDa. The protein is fused to a 23 amino acid His-tag at the N-terminus and purified using proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT23089
Source
Escherichia Coli.
Appearance
A sterile, colorless solution.

SMUG1 Human

Single-Strand-Selective Monofunctional Uracil-DNA Glycosylase 1 Human Recombinant

Recombinantly produced in E. coli, SMUG1 Human Recombinant is a single, non-glycosylated polypeptide chain. It comprises 293 amino acids (1-270) and has a molecular weight of 32.3 kDa. The protein includes a 23 amino acid His-tag fused at the N-terminus. Purification is achieved through proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT23155
Source
E.coli.
Appearance
A clear, colorless solution, free from any particulate matter.

MPG Human

N-Methylpurine-DNA Glycosylase Human Recombinant

This product consists of the recombinant human MPG protein, expressed in E. coli and purified to a high degree. The protein is a single, non-glycosylated polypeptide chain with a molecular weight of 33.9 kDa. It contains 306 amino acids, including an 8-amino acid His-tag at the N-terminus. The protein has been purified using proprietary chromatographic techniques to ensure its high quality.
Shipped with Ice Packs
Cat. No.
BT22669
Source
Escherichia Coli.
Appearance
Clear, colorless solution that has been sterilized by filtration.

MUG E.Coli

G/U Mismatch-Specific DNA Glycosylase E.Coli Recombinant

Recombinantly produced in E.coli, MUG is a single, non-glycosylated polypeptide chain consisting of 191 amino acids (1-168) and possessing a molecular mass of 21.1kDa. A 23 amino acid His-tag is fused to the N-terminus of MUG, which undergoes purification using proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT22740
Source
E.coli.
Appearance
A clear, sterile-filtered solution.

TDG Human

Thymine-DNA Glycosylase Human Recombinant

Recombinant human TDG, expressed in E. coli, is a single polypeptide chain consisting of 433 amino acids (residues 1-410) with a molecular weight of 48.4 kDa. A 23 amino acid His-tag is fused to the N-terminus for purification using proprietary chromatographic methods.
Shipped with Ice Packs
Cat. No.
BT23206
Source
E.coli.
Appearance
A clear, sterile-filtered solution.

UNG

Uracil DNA Glycosilase

E. coli Uracil DNA Glycosilase (UNG) catalyzes the release of free uracil from uracil-containing DNA. UNG efficiently hydrolyzes uracil from single-stranded or double-stranded DNA, but not from oligomers (6 or fewer bases).
Shipped with Ice Packs
Cat. No.
BT23291
Source
Escherichia Coli strain that carries the UNG gene from E.coli.
Appearance
Colorless, sterile-filtered solution.

UNG E.Coli

Uracil DNA Glycosylase E.Coli Recombinant

This product consists of a recombinant UNG enzyme derived from E. coli. Produced as a single, non-glycosylated polypeptide chain, it encompasses 252 amino acids, including a 23 amino acid His-tag located at the N-terminus. The molecular weight of the recombinant protein is 28.1kDa. Purification is achieved using proprietary chromatographic techniques to ensure a high level of purity.
Shipped with Ice Packs
Cat. No.
BT23365
Source
Escherichia Coli.
Appearance
The product appears as a clear solution that has undergone sterile filtration.
Definition and Classification

Glycosylases are a class of enzymes that hydrolyze glycosyl compounds. They are a type of hydrolase (EC 3.2) and are divided into two main groups: glycosidases, which hydrolyze O- and S-glycosyl compounds (EC 3.2.1), and enzymes that hydrolyze N-glycosyl compounds (EC 3.2.2) . Glycosylases play a crucial role in the base excision repair (BER) pathway, which is responsible for repairing damaged DNA bases .

Biological Properties

Glycosylases are widely expressed across different tissues and organisms. They are found in all kingdoms of life, from bacteria to humans . In humans, glycosylases are involved in various cellular processes, including DNA repair and the regulation of gene expression . They are typically localized in the nucleus and cytoplasm, where they interact with DNA and other cellular components .

Biological Functions

The primary function of glycosylases is to recognize and excise damaged bases from DNA, initiating the BER pathway . This process is essential for maintaining genome stability and preventing mutations that could lead to diseases such as cancer . Glycosylases also play a role in immune responses by recognizing and repairing DNA damage caused by pathogens . Additionally, they are involved in the regulation of gene expression through the removal of methylated bases, which can affect chromatin structure and transcription .

Modes of Action

Glycosylases operate by flipping the damaged base out of the DNA helix into an active site pocket, where it is excised . This mechanism allows for the sensitive detection of even minor base irregularities . Monofunctional glycosylases use an activated water molecule to cleave the N-glycosidic bond, while bifunctional glycosylases use an amine residue as a nucleophile . The excised base is then replaced through a series of downstream signaling cascades involving other BER enzymes .

Regulatory Mechanisms

The expression and activity of glycosylases are tightly regulated at multiple levels. Transcriptional regulation involves various transcription factors that bind to the promoter regions of glycosylase genes . Post-translational modifications, such as phosphorylation and ubiquitination, also play a role in modulating glycosylase activity and stability . Additionally, glycosylases can be regulated through interactions with other proteins and cellular components .

Applications

Glycosylases have numerous applications in biomedical research and clinical settings. They are used as diagnostic tools for detecting DNA damage and mutations . In therapeutic strategies, glycosylase inhibitors are being explored as potential anticancer agents . These enzymes are also employed in the study of gene expression and epigenetic modifications .

Role in the Life Cycle

Throughout the life cycle, glycosylases play a critical role in maintaining genome integrity from development to aging . During development, they ensure the proper repair of DNA damage, which is crucial for normal growth and differentiation . In aging, glycosylases help mitigate the accumulation of DNA damage that can lead to age-related diseases . Their activity is also essential in preventing the onset and progression of various diseases, including cancer .

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