Product List

MPG Human

N-Methylpurine-DNA Glycosylase Human Recombinant

MPG Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 306 amino acids (1-298 a.a.) and having a molecular mass of 33.9kDa (Molecular weight on SDS-PAGE will appear higher).
MPG is fused to an 8 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Shipped with Ice Packs
Cat. No.
BT22669
Source
Escherichia Coli.
Appearance
Sterile filtered colorless solution.

MUG E.Coli

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

MUG Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 191 amino acids (1-168) and having a molecular mass of 21.1kDa. MUG is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT22740
Source
E.coli.
Appearance
Sterile Filtered colorless solution.

MUTM E.Coli

Formamidopyrimidine-DNA Glycosylase E.Coli Recombinant

MUTM Recombinant produced in E. coli is a single polypeptide chain containing 289 amino acids (1-269) and having a molecular mass of 32.4kDa.
MUTM is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT22849
Source
E.coli.
Appearance
Sterile Filtered colorless solution.

MutY E.Coli

Adenine DNA Glycosylase E.Coli Recombinant

MutY Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 373 amino acids (1-350) and having a molecular mass of 41.5kDa. MutY is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT22921
Source
E.coli.
Appearance
Sterile Filtered colorless solution.

OGG1 Human

8-Oxoguanine DNA Glycosylase Human Recombinant

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.
Shipped with Ice Packs
Cat. No.
BT22991
Source
Escherichia Coli.
Appearance
Sterile filtered colourless solution.

OGG1 Mouse

8-Oxoguanine DNA Glycosylase Mouse Recombinant

OGG1 Mouse Recombinant 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 41.3kDa. OGG1 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques. 

Shipped with Ice Packs
Cat. No.
BT23089
Source
Escherichia Coli.
Appearance
Sterile filtered colourless solution.

SMUG1 Human

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

SMUG1 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 293 amino acids (1-270) and having a molecular mass of 32.3kDa.
SMUG1 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT23155
Source
E.coli.
Appearance
Sterile Filtered colorless solution.

TDG Human

Thymine-DNA Glycosylase Human Recombinant

TDG Human Recombinant produced in E. coli is a single polypeptide chain containing 433 amino acids (1-410) and having a molecular mass of 48.4 kDa.
TDG is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT23206
Source
E.coli.
Appearance
Sterile Filtered colorless solution.

UNG

Uracil DNA Glycosilase

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

UNG E.Coli

Uracil DNA Glycosylase E.Coli Recombinant

UNG E.Coli Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 252 amino acids (1-229 a.a) and having a molecular mass of 28.1kDa.
UNG is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT23365
Source
Escherichia Coli.
Appearance
Sterile Filtered clear solution.

Introduction

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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