human recombinant glo (R&D Systems)
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Structured Review
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human recombinant glo
Human Recombinant Glo, supplied by R&D Systems, used in various techniques. Bioz Stars score: 94/100, based on 24 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/product/recombinant+glo/Recombinant+Human+Glyoxalase+I+Protein%2C+CF/pmc13022346-64-3-17
Average 94 stars, based on 24 article reviews
Human Recombinant Glo, supplied by R&D Systems, used in various techniques. Bioz Stars score: 94/100, based on 24 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/product/recombinant+glo/Recombinant+Human+Glyoxalase+I+Protein%2C+CF/pmc13022346-64-3-17
Average 94 stars, based on 24 article reviews
human recombinant glo - by Bioz Stars,
2026-10
94/100 stars
Images
1) Product Images from "Discovery of hydroxytriazole as a potential glyoxalase-I inhibitor utilizing computer-aided drug design techniques"
Article Title: Discovery of hydroxytriazole as a potential glyoxalase-I inhibitor utilizing computer-aided drug design techniques
Journal: Scientific Reports
doi: 10.1038/s41598-026-40497-4
Figure Legend Snippet: The crystal structure of human Glo-I (PDB code 3W0T). ( a ) Schematic representation of the human Glo-I structures (PDB code 3W0T) in cartoon representation, the ligand is shown in balls and sticks and Zn + 2 ions as CPK style gray spheres. ( b ) Surface representation of the human Glo-I structure showing the location of the binding sites at the interface of the two homodimers.
Techniques Used: Binding Assay
Figure Legend Snippet: Schematic representation of the 96-well plate setup for the Glo-I bioassay, used to assess enzyme activity across various test samples.
Techniques Used: Bioassay, Activity Assay
Figure Legend Snippet: ( a ) 3D view of ( HTS06312SC ) in Glo-I active site. ( b ) 2D interactions between ( HTS06312SC ) and Glo-I active site.
Techniques Used:
Figure Legend Snippet: ( a ) 3D view of ( BTB02024SC ) in Glo-I active site. ( b ) 2D interactions between ( BTB02024SC ) and Glo-I.
Techniques Used:
Figure Legend Snippet: ( a ) 3D view of ( SPB07393SC ) in Glo-I active site. ( b ) 2D interactions between ( SPB07393SC ) and Glo-I.
Techniques Used:
Figure Legend Snippet: Structural dynamics of Glo-I RMSD ( a ), ligands RMSD ( b ), Glo-I radius of gyration ( c ), and SASA values ( d ) calculated during the 100 ns of MD trajectories.
Techniques Used:
Figure Legend Snippet: Graph showing the inhibitory activity of selected compounds (1–16) against Glo-I and their corresponding IC50 values.
Techniques Used: Activity Assay
Related Articles
Recombinant:Article Title: Unique Bidentate Chelators of Functionalized Heterocyclic Fluoroquinolones with Dual Anti-Inflammatory and Selective Cytotoxic Effects via a C7-C8 Ethylene Diamine Bridge. Article Snippet: School of Pharmacy, University of Jordan, Queen Ranya Street, Amman, 11942, Jordan; School of Pharmacy, AL-Zaytoonah University of Jordan, Amman, JORDAN; Faculty of Nursing/Head of Allied Health, Al-Balqa Applied University, Amman, Jordan; Department of Medicinal Chemistry and Pharmacognosy, Faculty of Pharmacy, Jordan University of Science and Technology, Irbid P. O.. Box 3030, Jordan; College of Pharmacy, Bilad Alrafidain University, Diyala, Iraq; Department of Basic Sciences and Humanities, Faculty of Science, The American University of Madaba, Jordan; University of Applied Science and Arts Dortmund, FH Dortmund, Dortmund, Germany; Cell Therapy Center, The University of Jordan, Amman 11942, Jordan Article Title: Discovery of a nanomolar inhibitor of the human glyoxalase-I enzyme using structure-based poly-pharmacophore modelling and molecular docking. Article Snippet: The glyoxalase-I (GLO-I) enzyme, which is the initial enzyme of the glyoxalase system that is responsible for the detoxification of cytotoxic α-ketoaldehydes, such as methylglyoxal, has been approved as a valid target in cancer therapy.. Overexpression of GLO-I has been observed in several types of carcinomas, including breast, colorectal, prostate, and bladder cancer.. In this work we aimed to identify potential GLO-I inhibitors via employing different structure-based drug design techniques including structure-based poly-pharmacophore modelling, virtual screening, and molecular docking. Article Title: Discovery of a nanomolar glyoxalase-I inhibitor using integrated ligand-based pharmacophore modeling and molecular docking Article Snippet: The glyoxalase system, which is composed of two zinc metalloenzymes, glyoxalase I (GLO-I) and glyoxalase II (GLO-II) and a catalytic amount of GSH, has a pivotal role in the detoxification of cytotoxic methylglyoxal (MG), a glycolytic side product.. Recent studies have revealed the overexpression of GLO-I in various cancer types such as breast carcinoma, invasive bladder, colon, prostate, and lung cancers.. Consequently, GLO-I has become a validated target for the development of novel anticancer agents. Article Title: Lead optimization and biological evaluation of diazenylbenzenesulfonamides inhibitors against glyoxalase-I enzyme as potential anticancer agents. Article Snippet: In a previous report, we described the discovery of (E)-5-((8-hydroxyquinolin-5-yl)diazenyl)-2-methylbenzenesulfonamide as a potent inhibitor of GLO-I enzyme with IC50 of 1.28 ± 0.12 μM.. Herein, lead optimization of this compound was achieved through targeting the central zinc atom and hydrophilic amino acid residues in the active site of the enzyme.. Among the synthesized compounds, compound TS010 showed the most potent inhibitory activity with IC50 of 0.57 ± 0.04 μM. Concentration Assay:Article Title: Unique Bidentate Chelators of Functionalized Heterocyclic Fluoroquinolones with Dual Anti-Inflammatory and Selective Cytotoxic Effects via a C7-C8 Ethylene Diamine Bridge. Article Snippet: School of Pharmacy, University of Jordan, Queen Ranya Street, Amman, 11942, Jordan; School of Pharmacy, AL-Zaytoonah University of Jordan, Amman, JORDAN; Faculty of Nursing/Head of Allied Health, Al-Balqa Applied University, Amman, Jordan; Department of Medicinal Chemistry and Pharmacognosy, Faculty of Pharmacy, Jordan University of Science and Technology, Irbid P. O.. Box 3030, Jordan; College of Pharmacy, Bilad Alrafidain University, Diyala, Iraq; Department of Basic Sciences and Humanities, Faculty of Science, The American University of Madaba, Jordan; University of Applied Science and Arts Dortmund, FH Dortmund, Dortmund, Germany; Cell Therapy Center, The University of Jordan, Amman 11942, Jordan In Vitro:Article Title: Unique Bidentate Chelators of Functionalized Heterocyclic Fluoroquinolones with Dual Anti-Inflammatory and Selective Cytotoxic Effects via a C7-C8 Ethylene Diamine Bridge. Article Snippet: School of Pharmacy, University of Jordan, Queen Ranya Street, Amman, 11942, Jordan; School of Pharmacy, AL-Zaytoonah University of Jordan, Amman, JORDAN; Faculty of Nursing/Head of Allied Health, Al-Balqa Applied University, Amman, Jordan; Department of Medicinal Chemistry and Pharmacognosy, Faculty of Pharmacy, Jordan University of Science and Technology, Irbid P. O.. Box 3030, Jordan; College of Pharmacy, Bilad Alrafidain University, Diyala, Iraq; Department of Basic Sciences and Humanities, Faculty of Science, The American University of Madaba, Jordan; University of Applied Science and Arts Dortmund, FH Dortmund, Dortmund, Germany; Cell Therapy Center, The University of Jordan, Amman 11942, Jordan Article Title: Discovery of a nanomolar inhibitor of the human glyoxalase-I enzyme using structure-based poly-pharmacophore modelling and molecular docking. Article Snippet: The glyoxalase-I (GLO-I) enzyme, which is the initial enzyme of the glyoxalase system that is responsible for the detoxification of cytotoxic α-ketoaldehydes, such as methylglyoxal, has been approved as a valid target in cancer therapy.. Overexpression of GLO-I has been observed in several types of carcinomas, including breast, colorectal, prostate, and bladder cancer.. In this work we aimed to identify potential GLO-I inhibitors via employing different structure-based drug design techniques including structure-based poly-pharmacophore modelling, virtual screening, and molecular docking. Article Title: Discovery of a nanomolar glyoxalase-I inhibitor using integrated ligand-based pharmacophore modeling and molecular docking Article Snippet: The glyoxalase system, which is composed of two zinc metalloenzymes, glyoxalase I (GLO-I) and glyoxalase II (GLO-II) and a catalytic amount of GSH, has a pivotal role in the detoxification of cytotoxic methylglyoxal (MG), a glycolytic side product.. Recent studies have revealed the overexpression of GLO-I in various cancer types such as breast carcinoma, invasive bladder, colon, prostate, and lung cancers.. Consequently, GLO-I has become a validated target for the development of novel anticancer agents. Article Title: Lead optimization and biological evaluation of diazenylbenzenesulfonamides inhibitors against glyoxalase-I enzyme as potential anticancer agents. Article Snippet: In a previous report, we described the discovery of (E)-5-((8-hydroxyquinolin-5-yl)diazenyl)-2-methylbenzenesulfonamide as a potent inhibitor of GLO-I enzyme with IC50 of 1.28 ± 0.12 μM.. Herein, lead optimization of this compound was achieved through targeting the central zinc atom and hydrophilic amino acid residues in the active site of the enzyme.. Among the synthesized compounds, compound TS010 showed the most potent inhibitory activity with IC50 of 0.57 ± 0.04 μM. Activity Assay:Article Title: Discovery of a nanomolar inhibitor of the human glyoxalase-I enzyme using structure-based poly-pharmacophore modelling and molecular docking. Article Snippet: The glyoxalase-I (GLO-I) enzyme, which is the initial enzyme of the glyoxalase system that is responsible for the detoxification of cytotoxic α-ketoaldehydes, such as methylglyoxal, has been approved as a valid target in cancer therapy.. Overexpression of GLO-I has been observed in several types of carcinomas, including breast, colorectal, prostate, and bladder cancer.. In this work we aimed to identify potential GLO-I inhibitors via employing different structure-based drug design techniques including structure-based poly-pharmacophore modelling, virtual screening, and molecular docking. Article Title: Lead optimization and biological evaluation of diazenylbenzenesulfonamides inhibitors against glyoxalase-I enzyme as potential anticancer agents. Article Snippet: In a previous report, we described the discovery of (E)-5-((8-hydroxyquinolin-5-yl)diazenyl)-2-methylbenzenesulfonamide as a potent inhibitor of GLO-I enzyme with IC50 of 1.28 ± 0.12 μM.. Herein, lead optimization of this compound was achieved through targeting the central zinc atom and hydrophilic amino acid residues in the active site of the enzyme.. Among the synthesized compounds, compound TS010 showed the most potent inhibitory activity with IC50 of 0.57 ± 0.04 μM. Spectrophotometry:Article Title: Lead optimization and biological evaluation of diazenylbenzenesulfonamides inhibitors against glyoxalase-I enzyme as potential anticancer agents. Article Snippet: In a previous report, we described the discovery of (E)-5-((8-hydroxyquinolin-5-yl)diazenyl)-2-methylbenzenesulfonamide as a potent inhibitor of GLO-I enzyme with IC50 of 1.28 ± 0.12 μM.. Herein, lead optimization of this compound was achieved through targeting the central zinc atom and hydrophilic amino acid residues in the active site of the enzyme.. Among the synthesized compounds, compound TS010 showed the most potent inhibitory activity with IC50 of 0.57 ± 0.04 μM. |