GLO1 Human, Active

Glyoxalase-I Human Recombinant, Active
Cat. No.
BT23683
Source
Escherichia Coli.
Synonyms
GLYI, GLOD1, GLO1, Glyoxalase-1, Lactoylglutathione lyase, Methylglyoxalase, Aldoketomutase, Ketone-aldehyde mutase, Glyoxalase I, S-D-lactoylglutathione methylglyoxal lyase, Glx I.
Appearance
Sterile filtered colorless solution.
Purity
Greater than 90.0% as determined by SDS-PAGE.
Usage
THE BioTek'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

Glyoxalase-I Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 184 amino acids and having a molecular mass of 20.7 kDa.
Glyoxalase-1 is purified by proprietary chromatographic techniques.

Product Specs

Introduction
The enzyme GLO1 plays a crucial role in detoxifying methylglyoxal, a harmful byproduct of metabolism. It achieves this by catalyzing the formation of S-lactoyl-glutathione from the reaction between methylglyoxal and reduced glutathione. GLO1 is genetically linked to the Human Leukocyte Antigen (HLA) complex and resides on chromosome 6p21.3-p21.1. Its expression is widespread across various tissues and cell types, including tumor cells where it often exhibits elevated levels. Studies suggest a potential connection between GLO1 and autism susceptibility in specific populations. Additionally, research implicates GLO1 in the biological mechanisms underlying mood disorders. Notably, increased GLO1 expression has been observed in kidney tumor cases.
Description
Recombinant human Glyoxalase-I, expressed in E. coli, is a single polypeptide chain protein. This non-glycosylated protein consists of 184 amino acids, resulting in a molecular weight of 20.7 kDa. The purification process involves proprietary chromatographic methods to ensure high purity.
Physical Appearance
The product appears as a clear, colorless solution that has been sterilized by filtration.
Formulation
The Glyoxalase-1 protein is supplied in a solution containing 20mM Tris-HCl buffer at pH 8, 1mM DTT (reducing agent), and 10% glycerol (stabilizer).
Stability
For short-term storage (up to 4 weeks), the product can be kept at refrigerated temperature (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 (0.1%) is advisable. It's crucial to minimize repeated freezing and thawing of the product to maintain its integrity.
Purity
The purity of the Glyoxalase-1 protein is determined using SDS-PAGE analysis, which confirms it to be greater than 90%.
Biological Activity
The specific activity of the enzyme is measured to be greater than 400 units per milligram of protein. One unit is defined as the amount of enzyme required to catalyze the formation of 1.0 micromole of S-lactoylglutathione from methylglyoxal and reduced glutathione in one minute at a pH of 6.5 and a temperature of 25°C.
Synonyms
GLYI, GLOD1, GLO1, Glyoxalase-1, Lactoylglutathione lyase, Methylglyoxalase, Aldoketomutase, Ketone-aldehyde mutase, Glyoxalase I, S-D-lactoylglutathione methylglyoxal lyase, Glx I.
Source
Escherichia Coli.
Amino Acid Sequence
MAEPQPPSGG LTDEAALSCC SDADPSTKDF LLQQTMLRVK DPKKSLDFYT RVLGMTLIQK CDFPIMKFSL YFLAYEDKND IPKEKDEKIAWALSRKATLE LTHNWGTEDD ETQSYHNGNS DPRGFGHIGI AVPDVYSACK RFEELGVKFV KKPDDGKMKG LAFIQDPDGY WIEILNPNKM ATLM.

Product Science Overview

Introduction

Glyoxalase-I (GLO1), also known as lactoylglutathione lyase or methylglyoxalase, is an enzyme that plays a crucial role in the detoxification of methylglyoxal (MG), a cytotoxic by-product of glycolysis. This enzyme is part of the glyoxalase system, which includes Glyoxalase-I and Glyoxalase-II (GLO2), and is evolutionarily conserved across various species .

Structure and Function

Glyoxalase-I is a metalloenzyme that catalyzes the conversion of the hemimercaptal adduct, formed spontaneously between methylglyoxal and reduced glutathione (GSH), into S-D-lactoylglutathione . This reaction is the first step in the glyoxalase pathway, which ultimately converts methylglyoxal into D-lactate, a less toxic compound .

The human recombinant form of Glyoxalase-I is produced using E. coli expression systems and is often tagged with a 6-His tag for purification purposes . The recombinant enzyme retains its activity and is used in various biochemical assays to study its function and regulation.

Biological Importance

The glyoxalase pathway serves as an important line of defense against glycation and oxidative stress in living organisms. By maintaining steady-state levels of methylglyoxal and other reactive dicarbonyl compounds, Glyoxalase-I helps protect cells from the harmful effects of these reactive species .

Applications

Recombinant human Glyoxalase-I is widely used in research to understand its role in cellular metabolism and its potential implications in various diseases. For instance, elevated levels of methylglyoxal and impaired glyoxalase activity have been linked to diabetes, cancer, and neurodegenerative diseases . Therefore, studying Glyoxalase-I can provide insights into the mechanisms underlying these conditions and potentially lead to the development of therapeutic strategies.

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GLO1 Human
Glyoxalase-I Human Recombinant
Cat. No.
BT23620
Source
Escherichia Coli.
THE BIOTEK
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