rfp trap bead slurry Search Results


rfp trap bead slurry  (Proteintech)
96
Proteintech rfp trap bead slurry
Rfp Trap Bead Slurry, supplied by Proteintech, used in various techniques. Bioz Stars score: 96/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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Average 96 stars, based on 1 article reviews
rfp trap bead slurry - by Bioz Stars, 2026-03
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α-rfp-trap agarose slurry  (Proteintech)
90
Proteintech α-rfp-trap agarose slurry
Arabidopsis MDL proteins form homo- and in part hetero-oligomeric complexes. A , Y2H assay. Candidate interactions of a previous high-throughput screen were validated by pairwise one-on-one matings using DNA-binding domain (DB) DB-MDL1, -MDL2, and -MDL3 or empty vector (EV) as bait for prey activation domain (AD)-tagged candidate interactors, including EV. Interactions were assayed by growth on selective plates using the HIS3 reporter. The experiment was performed three times with similar results. B and C , split-luciferase assay. cLUC-MDL1, -MDL2, and -MDL3 were transiently co-expressed with nLUC-MDL1, -MDL2, and -MDL3 or nLUC-EV (empty vector) in N. benthamiana . At 1 day post inoculation (dpi) (for cLUC-MDL1 combinations) or 2 dpi (for cLUC-MDL2 and cLUC-MDL3 combinations), plants were sprayed with 1 mM luciferin for the detection of luminescence. B , Quantification of data from the split-luciferase complementation assay. The luminescence of four independent experiments was quantified and is shown as a boxplot . Statistical significance between the interactions of the three MDLs and the EV control was determined with a two-way multipaired ANOVA test (∗∗∗ p < 0.001, ns = not significant). Raw data and exact statistical values for this graph can be found in in the supplemental source data file . C , Representative photographs of N. benthamiana leaves and the emitted luminescence (from blue = low to red = high ). D , co-immunoprecipitation of epitope-tagged MDLs. FLAG-MDL1, -MDL2, and -MDL3 and mCherry-MDL1, -MDL2, and -MDL3 were transiently coexpressed in N. benthamiana . At 2 dpi, proteins were extracted and immunoprecipitation was performed for the mCherry-MDL proteins using <t>α-RFP</t> agarose (capturing mCherry). mCherry-MDL proteins were detected with an α-RFP antibody and FLAG-MDL proteins with a monoclonal α - FLAG antibody. Ponceau staining was used as a loading control. Co-immunoprecipitation was repeated twice with similar results. E , in planta protein-protein interaction of MDL2. Three-week-old transgenic Arabidopsis seedlings stably expressing mCherry-MDL fusion proteins (transgenic lines; “TL”) were used for the immunoprecipitation of mCherry-MDL proteins using α-RFP agarose. mCherry-MDLs were detected with an α-RFP antibody and MDL2 was detected with the monoclonal α-MDL2 antibody ATM 20C8. Ponceau staining was used as a loading control. Co-immunoprecipitation was repeated twice with similar results.
α Rfp Trap Agarose Slurry, supplied by Proteintech, 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/result/α-rfp-trap agarose slurry/product/Proteintech
Average 90 stars, based on 1 article reviews
α-rfp-trap agarose slurry - by Bioz Stars, 2026-03
90/100 stars
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rfp trapa slurry  (Proteintech)
96
Proteintech rfp trapa slurry
Arabidopsis MDL proteins form homo- and in part hetero-oligomeric complexes. A , Y2H assay. Candidate interactions of a previous high-throughput screen were validated by pairwise one-on-one matings using DNA-binding domain (DB) DB-MDL1, -MDL2, and -MDL3 or empty vector (EV) as bait for prey activation domain (AD)-tagged candidate interactors, including EV. Interactions were assayed by growth on selective plates using the HIS3 reporter. The experiment was performed three times with similar results. B and C , split-luciferase assay. cLUC-MDL1, -MDL2, and -MDL3 were transiently co-expressed with nLUC-MDL1, -MDL2, and -MDL3 or nLUC-EV (empty vector) in N. benthamiana . At 1 day post inoculation (dpi) (for cLUC-MDL1 combinations) or 2 dpi (for cLUC-MDL2 and cLUC-MDL3 combinations), plants were sprayed with 1 mM luciferin for the detection of luminescence. B , Quantification of data from the split-luciferase complementation assay. The luminescence of four independent experiments was quantified and is shown as a boxplot . Statistical significance between the interactions of the three MDLs and the EV control was determined with a two-way multipaired ANOVA test (∗∗∗ p < 0.001, ns = not significant). Raw data and exact statistical values for this graph can be found in in the supplemental source data file . C , Representative photographs of N. benthamiana leaves and the emitted luminescence (from blue = low to red = high ). D , co-immunoprecipitation of epitope-tagged MDLs. FLAG-MDL1, -MDL2, and -MDL3 and mCherry-MDL1, -MDL2, and -MDL3 were transiently coexpressed in N. benthamiana . At 2 dpi, proteins were extracted and immunoprecipitation was performed for the mCherry-MDL proteins using <t>α-RFP</t> agarose (capturing mCherry). mCherry-MDL proteins were detected with an α-RFP antibody and FLAG-MDL proteins with a monoclonal α - FLAG antibody. Ponceau staining was used as a loading control. Co-immunoprecipitation was repeated twice with similar results. E , in planta protein-protein interaction of MDL2. Three-week-old transgenic Arabidopsis seedlings stably expressing mCherry-MDL fusion proteins (transgenic lines; “TL”) were used for the immunoprecipitation of mCherry-MDL proteins using α-RFP agarose. mCherry-MDLs were detected with an α-RFP antibody and MDL2 was detected with the monoclonal α-MDL2 antibody ATM 20C8. Ponceau staining was used as a loading control. Co-immunoprecipitation was repeated twice with similar results.
Rfp Trapa Slurry, supplied by Proteintech, used in various techniques. Bioz Stars score: 96/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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rfp trap m slurry  (Bio-Rad)
98
Bio-Rad rfp trap m slurry
Arabidopsis MDL proteins form homo- and in part hetero-oligomeric complexes. A , Y2H assay. Candidate interactions of a previous high-throughput screen were validated by pairwise one-on-one matings using DNA-binding domain (DB) DB-MDL1, -MDL2, and -MDL3 or empty vector (EV) as bait for prey activation domain (AD)-tagged candidate interactors, including EV. Interactions were assayed by growth on selective plates using the HIS3 reporter. The experiment was performed three times with similar results. B and C , split-luciferase assay. cLUC-MDL1, -MDL2, and -MDL3 were transiently co-expressed with nLUC-MDL1, -MDL2, and -MDL3 or nLUC-EV (empty vector) in N. benthamiana . At 1 day post inoculation (dpi) (for cLUC-MDL1 combinations) or 2 dpi (for cLUC-MDL2 and cLUC-MDL3 combinations), plants were sprayed with 1 mM luciferin for the detection of luminescence. B , Quantification of data from the split-luciferase complementation assay. The luminescence of four independent experiments was quantified and is shown as a boxplot . Statistical significance between the interactions of the three MDLs and the EV control was determined with a two-way multipaired ANOVA test (∗∗∗ p < 0.001, ns = not significant). Raw data and exact statistical values for this graph can be found in in the supplemental source data file . C , Representative photographs of N. benthamiana leaves and the emitted luminescence (from blue = low to red = high ). D , co-immunoprecipitation of epitope-tagged MDLs. FLAG-MDL1, -MDL2, and -MDL3 and mCherry-MDL1, -MDL2, and -MDL3 were transiently coexpressed in N. benthamiana . At 2 dpi, proteins were extracted and immunoprecipitation was performed for the mCherry-MDL proteins using <t>α-RFP</t> agarose (capturing mCherry). mCherry-MDL proteins were detected with an α-RFP antibody and FLAG-MDL proteins with a monoclonal α - FLAG antibody. Ponceau staining was used as a loading control. Co-immunoprecipitation was repeated twice with similar results. E , in planta protein-protein interaction of MDL2. Three-week-old transgenic Arabidopsis seedlings stably expressing mCherry-MDL fusion proteins (transgenic lines; “TL”) were used for the immunoprecipitation of mCherry-MDL proteins using α-RFP agarose. mCherry-MDLs were detected with an α-RFP antibody and MDL2 was detected with the monoclonal α-MDL2 antibody ATM 20C8. Ponceau staining was used as a loading control. Co-immunoprecipitation was repeated twice with similar results.
Rfp Trap M Slurry, supplied by Bio-Rad, used in various techniques. Bioz Stars score: 98/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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Average 98 stars, based on 1 article reviews
rfp trap m slurry - by Bioz Stars, 2026-03
98/100 stars
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Arabidopsis MDL proteins form homo- and in part hetero-oligomeric complexes. A , Y2H assay. Candidate interactions of a previous high-throughput screen were validated by pairwise one-on-one matings using DNA-binding domain (DB) DB-MDL1, -MDL2, and -MDL3 or empty vector (EV) as bait for prey activation domain (AD)-tagged candidate interactors, including EV. Interactions were assayed by growth on selective plates using the HIS3 reporter. The experiment was performed three times with similar results. B and C , split-luciferase assay. cLUC-MDL1, -MDL2, and -MDL3 were transiently co-expressed with nLUC-MDL1, -MDL2, and -MDL3 or nLUC-EV (empty vector) in N. benthamiana . At 1 day post inoculation (dpi) (for cLUC-MDL1 combinations) or 2 dpi (for cLUC-MDL2 and cLUC-MDL3 combinations), plants were sprayed with 1 mM luciferin for the detection of luminescence. B , Quantification of data from the split-luciferase complementation assay. The luminescence of four independent experiments was quantified and is shown as a boxplot . Statistical significance between the interactions of the three MDLs and the EV control was determined with a two-way multipaired ANOVA test (∗∗∗ p < 0.001, ns = not significant). Raw data and exact statistical values for this graph can be found in in the supplemental source data file . C , Representative photographs of N. benthamiana leaves and the emitted luminescence (from blue = low to red = high ). D , co-immunoprecipitation of epitope-tagged MDLs. FLAG-MDL1, -MDL2, and -MDL3 and mCherry-MDL1, -MDL2, and -MDL3 were transiently coexpressed in N. benthamiana . At 2 dpi, proteins were extracted and immunoprecipitation was performed for the mCherry-MDL proteins using α-RFP agarose (capturing mCherry). mCherry-MDL proteins were detected with an α-RFP antibody and FLAG-MDL proteins with a monoclonal α - FLAG antibody. Ponceau staining was used as a loading control. Co-immunoprecipitation was repeated twice with similar results. E , in planta protein-protein interaction of MDL2. Three-week-old transgenic Arabidopsis seedlings stably expressing mCherry-MDL fusion proteins (transgenic lines; “TL”) were used for the immunoprecipitation of mCherry-MDL proteins using α-RFP agarose. mCherry-MDLs were detected with an α-RFP antibody and MDL2 was detected with the monoclonal α-MDL2 antibody ATM 20C8. Ponceau staining was used as a loading control. Co-immunoprecipitation was repeated twice with similar results.

Journal: The Journal of Biological Chemistry

Article Title: Chemokine-like MDL proteins modulate flowering time and innate immunity in plants

doi: 10.1016/j.jbc.2021.100611

Figure Lengend Snippet: Arabidopsis MDL proteins form homo- and in part hetero-oligomeric complexes. A , Y2H assay. Candidate interactions of a previous high-throughput screen were validated by pairwise one-on-one matings using DNA-binding domain (DB) DB-MDL1, -MDL2, and -MDL3 or empty vector (EV) as bait for prey activation domain (AD)-tagged candidate interactors, including EV. Interactions were assayed by growth on selective plates using the HIS3 reporter. The experiment was performed three times with similar results. B and C , split-luciferase assay. cLUC-MDL1, -MDL2, and -MDL3 were transiently co-expressed with nLUC-MDL1, -MDL2, and -MDL3 or nLUC-EV (empty vector) in N. benthamiana . At 1 day post inoculation (dpi) (for cLUC-MDL1 combinations) or 2 dpi (for cLUC-MDL2 and cLUC-MDL3 combinations), plants were sprayed with 1 mM luciferin for the detection of luminescence. B , Quantification of data from the split-luciferase complementation assay. The luminescence of four independent experiments was quantified and is shown as a boxplot . Statistical significance between the interactions of the three MDLs and the EV control was determined with a two-way multipaired ANOVA test (∗∗∗ p < 0.001, ns = not significant). Raw data and exact statistical values for this graph can be found in in the supplemental source data file . C , Representative photographs of N. benthamiana leaves and the emitted luminescence (from blue = low to red = high ). D , co-immunoprecipitation of epitope-tagged MDLs. FLAG-MDL1, -MDL2, and -MDL3 and mCherry-MDL1, -MDL2, and -MDL3 were transiently coexpressed in N. benthamiana . At 2 dpi, proteins were extracted and immunoprecipitation was performed for the mCherry-MDL proteins using α-RFP agarose (capturing mCherry). mCherry-MDL proteins were detected with an α-RFP antibody and FLAG-MDL proteins with a monoclonal α - FLAG antibody. Ponceau staining was used as a loading control. Co-immunoprecipitation was repeated twice with similar results. E , in planta protein-protein interaction of MDL2. Three-week-old transgenic Arabidopsis seedlings stably expressing mCherry-MDL fusion proteins (transgenic lines; “TL”) were used for the immunoprecipitation of mCherry-MDL proteins using α-RFP agarose. mCherry-MDLs were detected with an α-RFP antibody and MDL2 was detected with the monoclonal α-MDL2 antibody ATM 20C8. Ponceau staining was used as a loading control. Co-immunoprecipitation was repeated twice with similar results.

Article Snippet: The protein concentration was determined using the Bradford protein assay and 500 μg of soluble proteins was incubated with 10 μl α-RFP-Trap Agarose slurry (ChromoTek GmbH, Planegg-Martinsried, Germany) for 1 h at 4 °C under constant agitation.

Techniques: Y2H Assay, High Throughput Screening Assay, Binding Assay, Plasmid Preparation, Activation Assay, Luciferase, Immunoprecipitation, Staining, Transgenic Assay, Stable Transfection, Expressing