GLO1 Human

Glyoxalase-I Human Recombinant
Cat. No.
BT23620
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.
Shipped with Ice Packs
In Stock

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
GLO1, an enzyme encoded by the GLO1 gene located on chromosome 6p21.3-p21.1, catalyzes the detoxification of methylglyoxal (MG) into S-lactoyl-glutathione. This enzymatic reaction is crucial for cellular protection against MG-induced damage. GLO1 is implicated in various biological processes, including cellular detoxification, inflammation, and the pathogenesis of diseases like autism, mood disorders, and cancer. Its upregulation in tumor cells highlights its potential as a therapeutic target.
Description
Recombinant human Glyoxalase-I, expressed in E. coli, is a non-glycosylated polypeptide chain comprising 184 amino acids with a molecular weight of 20.7 kDa. The protein is purified to a high degree using proprietary chromatographic methods.
Physical Appearance
The product is a clear, colorless, and sterile-filtered solution.
Formulation
Glyoxalase-1 is supplied in a solution buffered with 20mM Tris-HCl (pH 8.0), 1mM DTT (reducing agent), and 10% glycerol (cryoprotectant).
Stability
For short-term storage (up to 4 weeks), the product can be stored at 4°C. For extended storage, freezing at -20°C is recommended. The addition of a carrier protein (0.1% HSA or BSA) is advised for long-term storage to maintain protein stability. Repeated freeze-thaw cycles should be avoided to prevent protein degradation.
Purity
The purity of Glyoxalase-1 is determined to be greater than 90% using SDS-PAGE analysis.
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

Structure and Function

Glyoxalase-I is a 21 kDa isomerase enzyme that catalyzes the formation of S-D-lactoylglutathione from the hemimercaptal adduct formed spontaneously between methylglyoxal and reduced glutathione (GSH) . This reaction is the first step in the glyoxalase pathway, which ultimately converts methylglyoxal into D-lactate, a less harmful compound .

Importance in Cellular Metabolism

The glyoxalase pathway, which includes Glyoxalase-I and Glyoxalase-II, is evolutionarily conserved and plays a significant role in maintaining cellular homeostasis by detoxifying methylglyoxal . By converting methylglyoxal to D-lactate, Glyoxalase-I helps protect cells from glycation and oxidative stress, which can damage proteins, nucleic acids, and lipids .

Recombinant Human Glyoxalase-I

Recombinant human Glyoxalase-I is produced using E. coli expression systems. The recombinant protein typically includes an N-terminal Met and a 6-His tag for purification purposes . It is often used in research to study the enzyme’s function, structure, and role in various diseases, including diabetes and cancer .

Applications in Research

Recombinant Glyoxalase-I is valuable in biochemical research for several reasons:

  • Studying Enzyme Kinetics: Researchers use it to understand the enzyme’s catalytic mechanisms and substrate specificity.
  • Drug Development: It serves as a target for developing inhibitors that could potentially treat diseases associated with high levels of methylglyoxal.
  • Disease Research: Understanding how Glyoxalase-I functions can provide insights into its role in conditions like diabetes, where methylglyoxal levels are elevated .

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