Recombinant Human N-Glycosylase/OGG1 (N-GST) #abs04300

abs04300-10ug

1-2 Weeks

161

abs04300-50ug

1-2 Weeks

482

abs04300-500ug

1-2 Weeks

2353

abs04300-1mg

1-2 Weeks

3201

Description

Our E.coli expression system is responsible for the production of Recombinant Human N-Glycosylase, which consists of the Met1-Gly345 gene expressed with a GST tag at the N-terminus. Our aim is to create highly similar content by rearranging the original text to provide accurate information.

Other names

DNA repair enzymes play a crucial role in maintaining the integrity of our genetic code. One such enzyme is N-Glycosylase/DNA Lyase, which is responsible for detecting and removing damaged bases from the DNA strand. Specifically, it targets the oxidized base 8-Oxoguanine, which can result from exposure to reactive oxygen species found in our environment.
8-Oxoguanine DNA Glycosylase acts as both a glycosylase and a lyase, meaning it not only removes the damaged base but also breaks the phosphodiester backbone of the DNA strand. This creates a gap in the DNA, which is then repaired by another enzyme called DNA-(Apurinic or Apyrimidinic Site) Lyase, also known as AP Lyase. AP Lyase is responsible for removing any remaining sugar phosphate residue and ensuring the strand is completely repaired.
OGG1 is a well-known example of 8-Oxoguanine DNA Glycosylase, and it plays a critical role in protecting against mutations that can lead to cancer and other diseases. Other examples of this type of enzyme include MMH and MUTM, which are important for repairing different types of DNA damage.
In summary, DNA repair enzymes such as N-Glycosylase/DNA Lyase, 8-Oxoguanine DNA Glycosylase, and DNA-(Apurinic or Apyrimidinic Site) Lyase are essential for maintaining the integrity of our genetic code. Without them, mutations and other types of DNA damage could accumulate, leading to a wide range of health problems.

Source

Escherichia coli.

Format

This is a solution that has been filtered with 0.2 μm and consists of 20mM TrisHCl, 100mM NaCl, 1mM DTT, 1mM EDTA, 50% Glycerol, with a pH of 7.8.

Properties

aa_sequence

SPMILGYWKIKGLVQPTRLLLEYLEEKYEEHLYERDEGDKWRNKKFELGLEFPNLPYYIDGDVKLT QSMAIIRYIADKHNMLGGCPKERAEISMLEGAVLDIRYGVSRIAYSKDFETLKVDFLSKLPEMLK MFEDRLCHKTYLNGDHVTHPDFMLYDALDVVLYMDPMCLDAFPKLVCFKKRIEAIPQIDKYLKSS KYIAWPLQGWQATFGGGDHPPKSDLVPRGSMPARALLPRRMGHRTLASTPALWASIPCPRSELRL DLVLPSGQSFRWREQSPAHWSGVLADQVWTLTQTEEQLHCTVYRGDKSQASRPTPDELEAVRKYF QLDVTLAQLYHHWGSVDSHFQEVAQKFQGVRLLRQDPIECLFSFICSSNNNIARITGMVERLCQAF GPRLIQLDDVTYHGFPSLQALAGPEVEAHLRKLGLGYRARYVSASARAILEEQGGLAWLQQLRE SSYEEAHKALCILPGVGTKVADCICLMALDKPQAVPVDVHMWHIAQRDYSWHPTTSQAKGPSPQT NKELGNFFRSLWGPYAGWAQAVLFSADLRQSRHAQEPPAKRRKGSKGPEG.

Concentration

Based on our analysis using SDS-PAGE, we can confirm that the purity of the compound is greater than 95%. To be precise, we arrived at this conclusion by reducing the sample on the gel.

Endotoxin_level

According to the LAL test, the level of contamination is below 0.1 ng/μg (1 IEU/μg).

Stability & Storage

To maintain the stability of lyophilized protein, it is recommended to store it at temperatures lower than -20°C. However, if needed, it can be kept at room temperature for a maximum duration of 3 weeks. When preparing the protein solution from lyophilized form, it can be stored at temperatures between 4-7°C for a short span of 2-7 days. It's better to aliquot samples into smaller portions and freeze them at temperatures lower than -20°C for long-term storage, for up to three months. This is an easy and effective way to preserve the stability of protein samples, ensuring their usability for future research.

Target

Background

Human N-Glycosylase/DNA Lyase is a DNA repair enzyme, which incises DNA at 8-oxoG residues, and excises 7,8-dihydro-8-oxoguanine and 2,6-diamino-4-hydroxy-5-N-methylformamidopyrimidine (FAPY) from damage DNA. DGG1 has a β-lyase activity that nicks DNA 3' to the lesion.

Accession

O15527