MutY E.Coli

Adenine DNA Glycosylase E.Coli Recombinant

Cat. No.

BT22921

Source

E.coli.

Synonyms

ECK2956, JW2928, mica, mutB, mutY.

Appearance

Sterile Filtered colorless solution.

Purity

Greater than 90% 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.

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Description

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.

Product Specs

Introduction

Adenine DNA glycosylase (mutY) is an enzyme that removes damaged adenine bases from DNA. It acts on mismatched base pairs like A/G, A/8-oxoG, and A/C. MutY also has a minor role in removing damaged guanine bases from G/8-oxoG pairs. This enzyme is crucial for preventing mutations caused by oxidative damage to DNA. Studies show that increasing mutY levels in A549 cells exposed to oxygen and infrared radiation improves their survival rate. MutY is abundant in neurons, where it helps maintain the integrity of mitochondrial DNA, which is vulnerable to damage from reactive oxygen species over a lifetime.

Description

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.

Physical Appearance

A clear, colorless solution that has been sterilized by filtration.

Formulation

The MutY solution is provided at a concentration of 0.25mg/ml in a buffer consisting of 20mM Tris-HCl (pH 8.0), 0.1M NaCl, and 20% glycerol.

Stability

For short-term storage (2-4 weeks), keep the MutY solution refrigerated at 4°C. For longer storage, freeze the solution at -20°C. Adding a carrier protein such as HSA or BSA to a final concentration of 0.1% is recommended for long-term storage. Avoid repeatedly freezing and thawing the solution.

Purity

The purity of MutY is determined to be greater than 90% using SDS-PAGE analysis.

Synonyms

ECK2956, JW2928, mica, mutB, mutY.

Source

E.coli.

Amino Acid Sequence

MGSSHHHHHH SSGLVPRGSH MGSMQASQFS AQVLDWYDKY GRKTLPWQID KTPYKVWLSE VMLQQTQVAT VIPYFERFMA RFPTVTDLAN APLDEVLHLW TGLGYYARAR NLHKAAQQVA TLHGGKFPET FEEVAALPGV GRSTAGAILS LSLGKHFPIL DGNVKRVLAR CYAVSGWPGK KEVENKLWSL SEQVTPAVGV ERFNQAMMDL GAMICTRSKP KCSLCPLQNG CIAAANNSWA LYPGKKPKQT LPERTGYFLL LQHEDEVLLA QRPPSGLWGG LYCFPQFADE ESLRQWLAQR QIAADNLTQL TAFRHTFSHF HLDIVPMWLP VSSFTGCMDE GNALWYNLAQ PPSVGLAAPV ERLLQQLRTG APV.

Product Science Overview

Introduction

Adenine DNA glycosylase is a crucial enzyme involved in the base excision repair (BER) pathway, which is responsible for maintaining the integrity of DNA by correcting oxidative damage. In Escherichia coli (E. coli), this enzyme is encoded by the mutY gene and is commonly referred to as MutY. The recombinant form of this enzyme is produced through genetic engineering techniques to study its structure, function, and potential applications in biotechnology and medicine.

Structure and Function

MutY is a DNA glycosylase that specifically recognizes and removes adenine residues that are mispaired with guanine or 8-oxo-7,8-dihydroguanine (8-oxoG), a common oxidative lesion. The enzyme catalyzes the hydrolysis of the N-glycosylic bond, generating an apurinic/apyrimidinic (AP) site. This AP site is then processed by other enzymes in the BER pathway to restore the correct DNA sequence.

The enzyme contains several important structural motifs, including a helix-hairpin-helix (HhH) motif and a [4Fe-4S] cluster, which are characteristic of the base excision repair glycosylase superfamily. These structural features are essential for the enzyme’s ability to recognize and excise damaged bases.

Recombinant Production

The recombinant form of adenine DNA glycosylase is produced by cloning the mutY gene into an expression vector, which is then introduced into E. coli cells. The bacteria are cultured under conditions that induce the expression of the enzyme, which is subsequently purified using various chromatographic techniques. This recombinant enzyme is used in various biochemical and structural studies to understand its mechanism of action and to develop potential therapeutic applications.

Biological Significance

MutY plays a critical role in preventing mutations that can arise from oxidative DNA damage. The enzyme’s ability to remove mispaired adenines helps to prevent G:C to T:A transversions, which are a common type of mutation resulting from oxidative stress. By maintaining the integrity of the genome, MutY helps to protect cells from the harmful effects of oxidative damage, which can lead to cancer and other diseases.

Applications

The recombinant adenine DNA glycosylase has several potential applications in biotechnology and medicine. It can be used as a tool in molecular biology research to study DNA repair mechanisms and to develop assays for detecting oxidative DNA damage. Additionally, understanding the structure and function of this enzyme can aid in the development of novel therapeutic strategies for diseases associated with oxidative DNA damage, such as cancer.

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MutY E.Coli

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