UNG E.Coli

Uracil DNA Glycosylase E.Coli Recombinant
Cat. No.
BT23365
Source
Escherichia Coli.
Synonyms
UDG, b2580, JW2564, EC 3.2.2.27, DGU, UNG15, HIGM5, Uracil-DNA Glycosylase 1, EC 3.2.2, HIGM4, UNG2.
Appearance
Sterile Filtered clear solution.
Purity
Greater than 90.0% as determined by SDS-PAGE.
Usage
Prospec's products are furnished for LABORATORY RESEARCH USE ONLY. They may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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Description

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.

Product Specs

Introduction
Uracil-DNA glycosylase (UNG) plays a crucial role in DNA repair by specifically identifying and removing uracil bases from DNA strands. This action is vital in preventing mutations that can occur due to cytosine deamination or the incorporation of dUMP during DNA synthesis. By initiating the base-excision repair (BER) pathway, UNG helps maintain the integrity of the DNA sequence. Dysfunctional UNG activity can have significant health implications, potentially leading to conditions such as congenital rubella or immunodeficiency with hyper IgM type 4.
Description
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.
Physical Appearance
The product appears as a clear solution that has undergone sterile filtration.
Formulation
The UNG protein is provided at a concentration of 0.5mg/ml in a buffer solution containing 20mM Tris-HCl (pH 8.0) and 10% glycerol.
Stability
For short-term storage (up to four weeks), the product can be kept at 4°C. For extended storage, it is recommended to store the product frozen at -20°C. The addition of a carrier protein like HSA or BSA (0.1%) is advised for long-term storage. To maintain product integrity, it is crucial to minimize freeze-thaw cycles.
Purity
The purity of the UNG enzyme is greater than 90% as determined by SDS-PAGE analysis.
Synonyms
UDG, b2580, JW2564, EC 3.2.2.27, DGU, UNG15, HIGM5, Uracil-DNA Glycosylase 1, EC 3.2.2, HIGM4, UNG2.
Source
Escherichia Coli.
Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSMANELTW HDVLAEEKQQ PYFLNTLQTV ASERQSGVTI YPPQKDVFNA FRFTELGDVK VVILGQDPYH GPGQAHGLAF SVRPGIAIPP SLLNMYKELE NTIPGFTRPN HGYLESWARQ GVLLLNTVLT VRAGQAHSHA SLGWETFTDK VISLINQHRE GVVFLLWGSH AQKKGAIIDK QRHHVLKAPH PSPLSAHRGF FGCNHFVLAN QWLEQRGETP IDWMPVLPAE SE

Product Science Overview

Introduction

Uracil DNA Glycosylase (UDG), also known as uracil-N-glycosylase (UNG), is an enzyme that plays a crucial role in the DNA repair mechanism. It is responsible for the removal of uracil from DNA molecules, which can arise due to the deamination of cytosine or the incorporation of dUMP (deoxyuridine monophosphate) instead of dTMP (deoxythymidine monophosphate) during DNA replication. The recombinant form of this enzyme, produced in Escherichia coli (E. coli), is widely used in various molecular biology applications.

Structure and Function

UDG is a monofunctional glycosylase that catalyzes the hydrolysis of the N-glycosidic bond between the uracil base and the sugar-phosphate backbone of DNA. This action results in the release of free uracil and the creation of an abasic site (AP site) in the DNA strand. The enzyme is active on both single-stranded and double-stranded DNA but does not act on RNA or native, uracil-free DNA .

Production and Purification

The recombinant UDG is typically produced in E. coli strains that carry the UDG gene. The enzyme is expressed as a single, non-glycosylated polypeptide chain containing 252 amino acids, with a molecular mass of approximately 28.1 kDa . The production process involves the use of proprietary chromatographic techniques to purify the enzyme to a high degree of purity .

Applications

UDG has several important applications in molecular biology, including:

  1. PCR Contamination Prevention: UDG is used to prevent carryover contamination in PCR (Polymerase Chain Reaction) by degrading any uracil-containing DNA from previous reactions.
  2. Site-Directed Mutagenesis: The enzyme is employed in site-directed mutagenesis procedures to increase the efficiency of introducing specific mutations into DNA sequences.
  3. DNA Repair Studies: UDG is used in studies related to DNA repair mechanisms to understand the role of uracil removal in maintaining genomic integrity.
Reaction Conditions and Stability

UDG operates optimally at a pH of 8.0 and does not require divalent cations for its activity . The enzyme is inhibited by high ionic strength (>200 mM) and remains partially active even after heat treatment at 95°C for 10 minutes . For effective use, it is recommended to add a uracil glycosylase inhibitor to prevent degradation of the product DNA .

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THE BIOTEK
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