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AB206792

Recombinant human GLO1 protein

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(1 Publication)

Recombinant human GLO1 protein is a Human Full Length protein, in the 1 to 184 aa range, expressed in Escherichia coli, with >90%, < 1 EU/µg endotoxin level, suitable for SDS-PAGE, FuncS, Mass Spec.

View Alternative Names

Lactoylglutathione lyase, Aldoketomutase, Glyoxalase I, Ketone-aldehyde mutase, Methylglyoxalase, S-D-lactoylglutathione methylglyoxal lyase, Glx I, GLO1

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SDS-PAGE - Recombinant human GLO1 protein (AB206792)
  • SDS-PAGE

Supplier Data

SDS-PAGE - Recombinant human GLO1 protein (AB206792)

15% SDS-PAGE analysis of ab206792 (3μg).

Key facts

Purity

>90% SDS-PAGE

Endotoxin level

< 1 EU/µg

Expression system

Escherichia coli

Tags

Tag free

Applications

FuncS, Mass Spec, SDS-PAGE

applications

Biologically active

Yes

Biological activity

Specific activity: > 400 units/mg. One unit will form 1.0μmol of S-lactoylgutathione from methylglyoxal and reduced glutathione per minute at pH6.5 at 25°C.

Accession

Q04760

Animal free

No

Carrier free

No

Species

Human

Storage buffer

pH: 8 Constituents: 10% Glycerol (glycerin, glycerine), 0.32% Tris HCl, 0.02% (R*,R*)-1,4-Dimercaptobutan-2,3-diol

storage-buffer

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Reactivity data

{ "title": "Reactivity Data", "filters": { "stats": ["", "Reactivity", "Dilution Info", "Notes"] }, "values": { "SDS-PAGE": { "reactivity":"TESTED_AND_REACTS", "dilution-info":"", "notes":"<p></p>" }, "FuncS": { "reactivity":"TESTED_AND_REACTS", "dilution-info":"", "notes":"<p></p>" }, "Mass Spec": { "reactivity":"TESTED_AND_REACTS", "dilution-info":"", "notes":"<p></p>" } } }
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Sequence info

[{"sequence":"MAEPQPPSGGLTDEAALSCCSDADPSTKDFLLQQTMLRVKDPKKSLDFYTRVLGMTLIQKCDFPIMKFSLYFLAYEDKNDIPKEKDEKIAWALSRKATLELTHNWGTEDDETQSYHNGNSDPRGFGHIGIAVPDVYSACKRFEELGVKFVKKPDDGKMKGLAFIQDPDGYWIEILNPNKMATLM","proteinLength":"Full Length","predictedMolecularWeight":"20.7 kDa","actualMolecularWeight":null,"aminoAcidEnd":184,"aminoAcidStart":1,"nature":"Recombinant","expressionSystem":"Escherichia coli","accessionNumber":"Q04760","tags":[]}]
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Properties and storage information

Shipped at conditions
Blue Ice
Appropriate short-term storage duration
1-2 weeks
Appropriate short-term storage conditions
+4°C
Appropriate long-term storage conditions
-20°C
Aliquoting information
Upon delivery aliquot
Storage information
Avoid freeze / thaw cycle
True
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Supplementary information

This supplementary information is collated from multiple sources and compiled automatically.

The GLO1 protein also known as glyoxalase I plays an important role in cellular metabolism by detoxifying methylglyoxal a byproduct of glycolysis. It catalyzes the conversion of methylglyoxal into S-D-lactoylglutathione using glutathione as a cofactor. This enzyme has a mass of approximately 29 kDa and is expressed in various tissues throughout the body with higher levels found in the liver and kidney. Glyoxalase I (GLO1) expression is increased in response to stress conditions indicating its role in cellular defense mechanisms.
Biological function summary

Glyoxalase I is important for maintaining cellular homeostasis by mitigating harmful compounds. It forms part of the glyoxalase system which includes glyoxalase II functioning downstream of GLO1. This system prevents the accumulation of advanced glycation end-products (AGEs) which are implicated in cellular aging and dysfunction. By reducing the levels of methylglyoxal GLO1 supports normal physiological processes and protects cellular integrity.

Pathways

Glyoxalase I is an important component of the glyoxalase pathway. This pathway integrates into the detoxification network working alongside other important enzymes such as superoxide dismutase and catalase. These relationships highlight its function in cellular oxidative stress responses. GLO1's activity impacts pathways related to glycolysis and overall energy metabolism due to its role in reducing metabolic byproducts.

GLO1 has significant implications in diabetic complications and cancer. In diabetes increased methylglyoxal can worsen tissue damage making GLO1's role protective against advanced glycation end-product formation. In cancer GLO1 is overexpressed contributing to cellular proliferation and survival. Its interaction with proteins such as Hsp70 in cancer illustrates the adaptive mechanisms that tumor cells use for progression and chemoresistance.
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Specifications

Form

Liquid

Additional notes

ab206792 was purified using conventional chromatography techniques.

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General info

Function

Catalyzes the conversion of hemimercaptal, formed from methylglyoxal and glutathione, to S-lactoylglutathione (PubMed : 20454679, PubMed : 23122816, PubMed : 9705294). Involved in the regulation of TNF-induced transcriptional activity of NF-kappa-B (PubMed : 19199007). Required for normal osteoclastogenesis (By similarity).

Sequence similarities

Belongs to the glyoxalase I family.

Post-translational modifications

Glutathionylation at Cys-139 inhibits enzyme activity.. Phosphorylated at Thr-107 in the presence of CaMK2. However, this is a consensus site for phosphorylation by CK2 so phosphorylation may be mediated by CK2 rather than CaMK2. Phosphorylation is induced by TNF and suppresses the TNF-induced transcriptional activity of NF-kappa-B.. Exists in a nitric oxide (NO)-modified form. The exact nature of the modification is unknown, but it suppresses the TNF-induced transcriptional activity of NF-kappa-B.

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Product protocols

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Target data

Catalyzes the conversion of hemimercaptal, formed from methylglyoxal and glutathione, to S-lactoylglutathione (PubMed : 20454679, PubMed : 23122816, PubMed : 9705294). Involved in the regulation of TNF-induced transcriptional activity of NF-kappa-B (PubMed : 19199007). Required for normal osteoclastogenesis (By similarity).
See full target information GLO1
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Publications (1)

Recent publications for all applications. Explore the full list and refine your search

Frontiers in cell and developmental biology 9:800098 PubMed35047509

2022

Identification of the Host Substratome of -Secreted Casein Kinase 1 Using a SILAC-Based Quantitative Mass Spectrometry Assay.

Applications

Unspecified application

Species

Unspecified reactive species

Despina Smirlis,Florent Dingli,Valentin Sabatet,Aileen Roth,Uwe Knippschild,Damarys Loew,Gerald F Späth,Najma Rachidi
View all publications
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