GLO1 Mouse

Glyoxalase-I Mouse Recombinant
Cat. No.
BT23758
Source
Sf9, Baculovirus cells.
Synonyms
Lactoylglutathione lyase, Aldoketomutase, Glyoxalase I, Glx I, Ketone-aldehyde mutase, Methylglyoxalase, S-D-lactoylglutathione methylglyoxal lyase.
Appearance
Sterile Filtered colorless solution.
Purity
Greater than 95.0% 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.
Shipped with Ice Packs
In Stock

Description

GLO1 Mouse Recombinant produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 192 amino acids (1-184a.a.) and having a molecular mass of 21.8kDa (Molecular size on SDS-PAGE will appear at approximately 28-40kDa).
GLO1 is expressed with an 8 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.

Product Specs

Introduction
The GLO1 gene encodes for the glyoxalase I enzyme, a critical component of the glyoxalase system. This system plays a vital role in detoxifying methylglyoxal, a reactive metabolite linked to cellular damage and various diseases. GLO1 is implicated in several biological processes, including its association with the human leukocyte antigen (HLA) system, a genetic region crucial for immune responses. Located on chromosome 6p21.3-p21.1, GLO1 exhibits widespread expression, with elevated levels often observed in various tumor cell lines, suggesting its potential role in cancer development. Notably, GLO1 has been identified as a significant susceptibility gene for autism in Taiwanese populations, underscoring its relevance in neurodevelopmental disorders. Furthermore, research suggests a potential link between GLO1 and mood disorders, with dysregulation of this gene possibly contributing to their pathophysiology. In particular, GLO1 overexpression has been observed in kidney tumors, further implicating it in cancer biology.
Description
This product is a recombinant mouse GLO1 protein produced in Sf9 insect cells using a baculovirus expression system. It is a single, glycosylated polypeptide chain that consists of 192 amino acids (amino acids 1-184a.a.) and has a molecular weight of 21.8 kDa. Note that on SDS-PAGE, the apparent molecular size might appear between 28-40 kDa due to glycosylation. This recombinant GLO1 protein is engineered with an 8 amino acid His tag at the C-terminus to facilitate purification, which is achieved through proprietary chromatographic techniques.
Physical Appearance
Clear, colorless solution that has been sterilized by filtration.
Formulation
The GLO1 protein is supplied in a solution with a concentration of 0.5 mg/ml. The solution is buffered using Phosphate Buffered Saline (PBS) at a pH of 7.4 and contains 10% glycerol to enhance protein stability.
Stability
For short-term storage (up to 2-4 weeks), the product can be stored at 4°C. For extended storage, it is recommended to freeze the product at -20°C. To further enhance stability during long-term storage, adding a carrier protein like HSA or BSA at a concentration of 0.1% is advisable. It's important to avoid repeated freezing and thawing as it can negatively impact protein integrity.
Purity
The purity of the GLO1 protein is greater than 95% as determined by SDS-PAGE analysis.
Biological Activity
The specific activity of this GLO1 protein is greater than 210 units/mg. One unit of activity is defined as the amount of enzyme required to catalyze the formation of 1.0 µmol of S-lactoylglutathione from methylglyoxal and reduced glutathione per minute at a pH of 6.5 and a temperature of 25°C.
Synonyms
Lactoylglutathione lyase, Aldoketomutase, Glyoxalase I, Glx I, Ketone-aldehyde mutase, Methylglyoxalase, S-D-lactoylglutathione methylglyoxal lyase.
Source
Sf9, Baculovirus cells.
Amino Acid Sequence
MAEPQPASSG LTDETAFSCC SDPDPSTKDF LLQQTMLRIK DPKKSLDFYT RVLGLTLLQK LDFPAMKFSL YFLAYEDKND IPKDKSEKTA WTFSRKATLE LTHNWGTEDD ETQSYHNGNS DPRGFGHIGI AVPDVYSACK RFEELGVKFV KKPDDGKMKG LAFIQDPDGY WIEILNPNKI ATIILEHHHH HH.

Product Science Overview

Structure and Function

Glyoxalase-I catalyzes the isomerization of the hemithioacetal formed from methylglyoxal and glutathione to S-D-lactoylglutathione. This reaction is the first step in the glyoxalase pathway, which ultimately converts methylglyoxal into D-lactate, a less reactive and more easily excretable compound .

Biological Significance

The detoxification of methylglyoxal is vital because MG can modify proteins and nucleotides, leading to the formation of advanced glycation end-products (AGEs), which are associated with oxidative stress and apoptosis . Elevated levels of MG are particularly problematic in conditions such as diabetes, where high glucose levels lead to increased MG production .

Recombinant Mouse Glyoxalase-I

Recombinant mouse Glyoxalase-I is produced using recombinant DNA technology, which involves inserting the gene encoding GLO1 into an expression system, such as bacteria or yeast, to produce the protein in large quantities. This recombinant protein is used in various research applications to study its structure, function, and role in disease processes .

Research Applications
  1. Disease Mechanisms: Research has linked GLO1 to numerous diseases, including diabetic complications, cancer, and aging . By studying recombinant GLO1, scientists can better understand its role in these conditions and develop potential therapeutic strategies.
  2. Behavioral Studies: Recent findings have also connected GLO1 to behavioral phenotypes, including psychiatric disorders such as anxiety, depression, schizophrenia, and autism . This opens new avenues for exploring the enzyme’s impact on mental health.
  3. Drug Development: Recombinant GLO1 is used in drug screening to identify compounds that can modulate its activity. This is particularly relevant for developing treatments for diseases where MG detoxification is impaired .

Quick Inquiry

Personal Email Detected
Please use an institutional or corporate email address for inquiries. Personal email accounts ( such as Gmail, Yahoo, and Outlook) are not accepted. *
© Copyright 2024 Thebiotek. All Rights Reserved.