recombinant oga Search Results


94
OriGene biological data oga enzyme inhibition biochemical assay recombinant full length human oga enzyme
Biological Data Oga Enzyme Inhibition Biochemical Assay Recombinant Full Length Human Oga Enzyme, supplied by OriGene, used in various techniques. Bioz Stars score: 94/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/product/recombinant+oga/us12319679-741-0-16?v=OriGene
Average 94 stars, based on 1 article reviews
biological data oga enzyme inhibition biochemical assay recombinant full length human oga enzyme - by Bioz Stars, 2026-07
94/100 stars
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90
R&D Systems gh recombinant human akt1 r d systems lot code
Figure 4. Probing Open and Closed O-GlcNAc Sites on Various Recombinant Proteins Using OGT and B3GALNT2 Each protein was loaded into three consecutive lanes, indicated as lane a, b, and c. Lane a contained the recombinant protein only. Lane b contained additional OGT and UDP-GalNAz for detecting open sites. Lane c contained additional OGT, UDP-GlcNAc, B3GALNT2, and UDP-GalNAz for detecting closed sites. <t>AKT1</t> E. coli was expressed in E. coli. AKT1 Baculo was ex- pressed in Baculovirus. All other proteins were expressed in E. coli. In the lanes indicated with both AKT3 and CK2, samples of AKT3 were loaded first and then chased with samples of CK2 5 min later. All samples were subjected to click chemistry reaction with Click-iT DIBO Alkyne and separated on 4%–20% SDS gradient gels and visualized with TCE under UV (upper panels). The gels were then blotted to nitrocellulose membrane and detected with SA-HRP (lower panels). Recombinant CEBPB is a truncated protein and lacks trypto- phan residues, therefore it is not visible by TCE staining but was detected by OGT and B3GALNT2 staining when probed with SA-HRP. OGT showed some background staining possibly due to self-labeling. By comparing the signal intensities for lanes a, b, and c, it was concluded that AKT1 (both E. coli- and Baculovirus-expressed versions), CK2, CEBPB, and PFKFB3 contained open sites for O-GlcNAcylation.
Gh Recombinant Human Akt1 R D Systems Lot Code, supplied by R&D Systems, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/product/recombinant+oga/pm30100348-107-113-117?v=R%26D+Systems
Average 90 stars, based on 1 article reviews
gh recombinant human akt1 r d systems lot code - by Bioz Stars, 2026-07
90/100 stars
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90
R&D Systems bacteroides thetaiotaomicron o glcnacase
Figure 4. Probing Open and Closed O-GlcNAc Sites on Various Recombinant Proteins Using OGT and B3GALNT2 Each protein was loaded into three consecutive lanes, indicated as lane a, b, and c. Lane a contained the recombinant protein only. Lane b contained additional OGT and UDP-GalNAz for detecting open sites. Lane c contained additional OGT, UDP-GlcNAc, B3GALNT2, and UDP-GalNAz for detecting closed sites. <t>AKT1</t> E. coli was expressed in E. coli. AKT1 Baculo was ex- pressed in Baculovirus. All other proteins were expressed in E. coli. In the lanes indicated with both AKT3 and CK2, samples of AKT3 were loaded first and then chased with samples of CK2 5 min later. All samples were subjected to click chemistry reaction with Click-iT DIBO Alkyne and separated on 4%–20% SDS gradient gels and visualized with TCE under UV (upper panels). The gels were then blotted to nitrocellulose membrane and detected with SA-HRP (lower panels). Recombinant CEBPB is a truncated protein and lacks trypto- phan residues, therefore it is not visible by TCE staining but was detected by OGT and B3GALNT2 staining when probed with SA-HRP. OGT showed some background staining possibly due to self-labeling. By comparing the signal intensities for lanes a, b, and c, it was concluded that AKT1 (both E. coli- and Baculovirus-expressed versions), CK2, CEBPB, and PFKFB3 contained open sites for O-GlcNAcylation.
Bacteroides Thetaiotaomicron O Glcnacase, supplied by R&D Systems, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/product/recombinant+oga/pm22322011-178-6-10?v=R%26D+Systems
Average 90 stars, based on 1 article reviews
bacteroides thetaiotaomicron o glcnacase - by Bioz Stars, 2026-07
90/100 stars
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90
GenScript corporation recombinant proteins aanl6 and oga mutant cpoga d298n
Figure 4. Probing Open and Closed O-GlcNAc Sites on Various Recombinant Proteins Using OGT and B3GALNT2 Each protein was loaded into three consecutive lanes, indicated as lane a, b, and c. Lane a contained the recombinant protein only. Lane b contained additional OGT and UDP-GalNAz for detecting open sites. Lane c contained additional OGT, UDP-GlcNAc, B3GALNT2, and UDP-GalNAz for detecting closed sites. <t>AKT1</t> E. coli was expressed in E. coli. AKT1 Baculo was ex- pressed in Baculovirus. All other proteins were expressed in E. coli. In the lanes indicated with both AKT3 and CK2, samples of AKT3 were loaded first and then chased with samples of CK2 5 min later. All samples were subjected to click chemistry reaction with Click-iT DIBO Alkyne and separated on 4%–20% SDS gradient gels and visualized with TCE under UV (upper panels). The gels were then blotted to nitrocellulose membrane and detected with SA-HRP (lower panels). Recombinant CEBPB is a truncated protein and lacks trypto- phan residues, therefore it is not visible by TCE staining but was detected by OGT and B3GALNT2 staining when probed with SA-HRP. OGT showed some background staining possibly due to self-labeling. By comparing the signal intensities for lanes a, b, and c, it was concluded that AKT1 (both E. coli- and Baculovirus-expressed versions), CK2, CEBPB, and PFKFB3 contained open sites for O-GlcNAcylation.
Recombinant Proteins Aanl6 And Oga Mutant Cpoga D298n, supplied by GenScript corporation, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/product/recombinant+oga/pmc11459509-28-3-19?v=GenScript+corporation
Average 90 stars, based on 1 article reviews
recombinant proteins aanl6 and oga mutant cpoga d298n - by Bioz Stars, 2026-07
90/100 stars
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N/A
OGA Recombinant Protein N-His Tag Lyophilized from Innovative Research is a recombinant protein lyophilized from sterile pbs, ph 7.4.. This preparation has a purity of >95 % as determined by reducing SDS-PAGE. This product has
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N/A
The Recombinant Human O GlcNAcase OGA MGEA5 Protein from Novus Biologicals is derived from E coli The Recombinant Human O GlcNAcase OGA MGEA5 Protein has been validated for the following applications SDS Page
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N/A
Recombinant Mouse MGEA5 full length or partial length protein was expressed.http://www.creativebiomart.net/Recombinant-Mouse-MGEA5-Protein-443917.htm
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N/A
Isoform 1:Cleaves GlcNAc but not GalNAc from O-glycosylated proteins. Can use p-nitrophenyl-beta-GlcNAc and 4-methylumbelliferone-GlcNAc as substrates but not p-nitrophenyl-beta-GalNAc or p-nitrophenyl-alpha-GlcNAc (in vitro) . Does not bind acetyl-CoA and does not have histone acetyltransferase activity.
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N/A
O-GlcNAcase/OGA/MGEA5 Recombinant Protein Antigen
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N/A
Recombinant Rat MGEA5 full length or partial length protein was expressed.http://www.creativebiomart.net/Recombinant-Rat-MGEA5-Protein-452496.htm
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N/A
Recombinant Chicken MGEA5 full length or partial length protein was expressed.http://www.creativebiomart.net/description_416721_12.htm
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Image Search Results


Figure 4. Probing Open and Closed O-GlcNAc Sites on Various Recombinant Proteins Using OGT and B3GALNT2 Each protein was loaded into three consecutive lanes, indicated as lane a, b, and c. Lane a contained the recombinant protein only. Lane b contained additional OGT and UDP-GalNAz for detecting open sites. Lane c contained additional OGT, UDP-GlcNAc, B3GALNT2, and UDP-GalNAz for detecting closed sites. AKT1 E. coli was expressed in E. coli. AKT1 Baculo was ex- pressed in Baculovirus. All other proteins were expressed in E. coli. In the lanes indicated with both AKT3 and CK2, samples of AKT3 were loaded first and then chased with samples of CK2 5 min later. All samples were subjected to click chemistry reaction with Click-iT DIBO Alkyne and separated on 4%–20% SDS gradient gels and visualized with TCE under UV (upper panels). The gels were then blotted to nitrocellulose membrane and detected with SA-HRP (lower panels). Recombinant CEBPB is a truncated protein and lacks trypto- phan residues, therefore it is not visible by TCE staining but was detected by OGT and B3GALNT2 staining when probed with SA-HRP. OGT showed some background staining possibly due to self-labeling. By comparing the signal intensities for lanes a, b, and c, it was concluded that AKT1 (both E. coli- and Baculovirus-expressed versions), CK2, CEBPB, and PFKFB3 contained open sites for O-GlcNAcylation.

Journal: Cell chemical biology

Article Title: Detecting and Imaging O-GlcNAc Sites Using Glycosyltransferases: A Systematic Approach to Study O-GlcNAc.

doi: 10.1016/j.chembiol.2018.07.007

Figure Lengend Snippet: Figure 4. Probing Open and Closed O-GlcNAc Sites on Various Recombinant Proteins Using OGT and B3GALNT2 Each protein was loaded into three consecutive lanes, indicated as lane a, b, and c. Lane a contained the recombinant protein only. Lane b contained additional OGT and UDP-GalNAz for detecting open sites. Lane c contained additional OGT, UDP-GlcNAc, B3GALNT2, and UDP-GalNAz for detecting closed sites. AKT1 E. coli was expressed in E. coli. AKT1 Baculo was ex- pressed in Baculovirus. All other proteins were expressed in E. coli. In the lanes indicated with both AKT3 and CK2, samples of AKT3 were loaded first and then chased with samples of CK2 5 min later. All samples were subjected to click chemistry reaction with Click-iT DIBO Alkyne and separated on 4%–20% SDS gradient gels and visualized with TCE under UV (upper panels). The gels were then blotted to nitrocellulose membrane and detected with SA-HRP (lower panels). Recombinant CEBPB is a truncated protein and lacks trypto- phan residues, therefore it is not visible by TCE staining but was detected by OGT and B3GALNT2 staining when probed with SA-HRP. OGT showed some background staining possibly due to self-labeling. By comparing the signal intensities for lanes a, b, and c, it was concluded that AKT1 (both E. coli- and Baculovirus-expressed versions), CK2, CEBPB, and PFKFB3 contained open sites for O-GlcNAcylation.

Article Snippet: REAGENT or RESOURCE SOURCE IDENTIFIER Bacterial and Virus Strains E. coli/BL21(DE3) ThermoFisher C6000-03 Chemicals, Peptides, and Recombinant Proteins UDP-GlcNAz (UDP-azido-GlcNAc) R&D Systems Cat#ES104 UDP-GalNAz (UDP-azido-GalNAc) R&D Systems Cat#ES103 Biotin alkyne adduct R&D Systems Cat#ES100 Streptavidin conjugated horseradish peroxidase (strep-HRP) R&D Systems 4800-30-06 UDP-GlcNAc Sigma Aldrich Cat#U4375 Streptavidin, Alexa FluorTM 555 ThermoFisher Scientific Cat#S32355 Click-iT DIBO Alkyne ThermoFisher Scientific Cat#C10412 VisULite MAX ECL Western Blotting Substrate R&D Systems Cat#VL002-200 4’,6-diamidino-2-phenylindole (DAPI) R&D Systems 5748 Benzyl-b-GlcNAc Santa Cruz Biotechnology Cat#sc-221296 OGT substrate peptide AnaSpec Cat#AS-63726 Recombinant human B3GALNT2 R&D Systems Cat#1848-GT Recombinant human Casein Kinase 2a (CK2) R&D Systems Cat#7957-CK Recombinant human O-GlcNAc transferase (OGT) R&D Systems Cat#8446-GT Recombinant B. thetaiotaomicron O-GlcNAcase (OGA) R&D Systems Cat6779-GH Recombinant human AKT1 R&D Systems Lot Code: IPC Recombinant human AKT1 R&D Systems Cat#1775-KS Recombinant human AKT2 R&D Systems Lot Code: IQR Recombinant human AKT3 R&D Systems Lot Code: PIB Recombinant human CEBP b R&D Systems Lot Code: OYK Recombinant human PFKFB3 R&D Systems Cat#8566-BP Recombinant human G6PD R&D Systems Lot Code: DGGC Recombinant human GCK R&D Systems Cat#7840-GK Recombinant human FXR R&D Systems Lot Code: OGV Critical Commercial Assays Glycosyltransferase Activity Kit R&D Systems Cat#EA001 Experimental Models: Cell Lines

Techniques: Recombinant, Membrane, Staining, Labeling