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AB87413

Recombinant human GLO1 protein

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(2 Publications)

Recombinant human GLO1 protein is a Human Full Length protein, expressed in Escherichia coli, with >90%, suitable for SDS-PAGE, FuncS.

View Alternative Names

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

1 Images
SDS-PAGE - Recombinant human GLO1 protein (AB87413)
  • SDS-PAGE

Unknown

SDS-PAGE - Recombinant human GLO1 protein (AB87413)

ab87413 on 15% SDS-PAGE (3μg)

Key facts

Purity

>90% SDS-PAGE

Expression system

Escherichia coli

Tags

Tag free

Applications

SDS-PAGE, FuncS

applications

Biologically active

Yes

Biological activity

Specific activity: >0.4 units/mg (please enquire for specific batch value). One unit will form 1.0 μmol of S-lactoylglutathione from methylglyoxal and reduced glutathione per minute at pH 7.5, at 25°C. Specific activity was expressed in units/mg of protein.

Accession

Q04760

Animal free

No

Carrier free

No

Species

Human

Storage buffer

pH: 8 Constituents: 10% Glycerol (glycerin, glycerine), 0.316% Tris HCl, 0.0154% (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>" } } }
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Product details

Activity Assay

  • Final assay concentrations:In 1.5ml reaction mix, the final concentrations are 79 mM potassium phosphate, 0.033%(w/v) reduced glutathine, 0.003% (w/v) bovine serum albumin, 0.033% methylglyoxal(w/v) and recombinant gyloxalase l (0.5ug, 1ug, 2ug).
  • 1. Prepare protein-free reaction buffer without recombinant protein into suitable container (for each protein concentration).
  • 2. Equilibrate protein-free reaction buffer to 25°C and monitor at A240nm (absorbance) until the value is constant, using a spectrophotometer.
  • 3. Dilute various concentrations of recombinant gyloxalase l (0.5ug, 1ug, 2ug) in 50ul of 10mM potassium phosphate buffer with 0.1% (wv) BSA, pH7.4.
  • Add 50ul of recombinant glyoxalase I solution to 1.45ml reaction buffer.
  • Immediately mix by inversion and record the increase at A240nm for 5 minutes
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Sequence info

[{"sequence":"MAEPQPPSGGLTDEAALSCCSDADPSTKDFLLQQTMLRVKDPKKSLDFYTRVLGMTLIQKCDFPIMKFSLYFLAYEDKNDIPKEKDEKIAWALSRKATLELTHNWGTEDDETQSYHNGNSDPRGFGHIGIAVPDVYSACKRFEELGVKFVKKPDDGKMKGLAFIQDPDGYWIEILNPNKMATLM","proteinLength":"Full Length","predictedMolecularWeight":null,"actualMolecularWeight":null,"aminoAcidEnd":0,"aminoAcidStart":0,"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

Purified by 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

For this product, it's our understanding that no specific protocols are required. You can visit:
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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 (2)

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

Cell reports 32:108160 PubMed32966793

2020

Phosphorylation of T107 by CamKIIδ Regulates the Detoxification Efficiency and Proteomic Integrity of Glyoxalase 1.

Applications

Unspecified application

Species

Unspecified reactive species

Jakob Morgenstern,Sylvia Katz,Jutta Krebs-Haupenthal,Jessy Chen,Alireza Saadatmand,Fabiola Garcia Cortizo,Alexandra Moraru,Johanna Zemva,Marta Campos Campos,Aurelio Teleman,Johannes Backs,Peter Nawroth,Thomas Fleming

The Prostate 77:1528-1538 PubMed28929505

2017

High-Level Glyoxalase 1 (GLO1) expression is linked to poor prognosis in prostate cancer.

Applications

Unspecified application

Species

Unspecified reactive species

Christoph Burdelski,Rami Shihada,Andrea Hinsch,Alexander Angerer,Cosima Göbel,Emily Friedrich,Claudia Hube-Magg,Susanne Burdak-Rothkamm,Martina Kluth,Ronald Simon,Christina Möller-Koop,Guido Sauter,Franzika Büscheck,Corinna Wittmer,Till S Clauditz,Till Krech,Maria C Tsourlakis,Sarah Minner,Markus Graefen,Thorsten Schlomm,Waldemar Wilczak,Frank Jacobsen
View all publications
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Product promise

We are committed to supporting your work with high-quality reagents, and we're here for you every step of the way. In the unlikely event that one of our products does not perform as expected, you're protected by our Product Promise.
For full details, please see our Terms & Conditions
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Associated Products

Select an associated product type
Alternative Product
Proteins & Peptides

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