2x protein loading buffer Search Results


2xlaemmmli  (Santa Cruz Biotechnology)
93
Santa Cruz Biotechnology 2xlaemmmli
2xlaemmmli, supplied by Santa Cruz Biotechnology, used in various techniques. Bioz Stars score: 93/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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2 x laemmli buffer  (Bio-Rad)
97
Bio-Rad 2 x laemmli buffer
2 X Laemmli Buffer, supplied by Bio-Rad, used in various techniques. Bioz Stars score: 97/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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2x protein loading buffer  (LI-COR)
96
LI-COR 2x protein loading buffer
2x Protein Loading Buffer, supplied by LI-COR, 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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2x laemmli buffer  (Bio-Rad)
99
Bio-Rad 2x laemmli buffer
2x Laemmli Buffer, supplied by Bio-Rad, used in various techniques. Bioz Stars score: 99/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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2x sds bromophenol blue protein lysis buffer  (Bio-Rad)
96
Bio-Rad 2x sds bromophenol blue protein lysis buffer
2x Sds Bromophenol Blue Protein Lysis Buffer, supplied by Bio-Rad, 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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2x sds loading buffer  (Bio-Rad)
98
Bio-Rad 2x sds loading buffer
2x Sds Loading Buffer, 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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2x nupage lds protein sample buffer  (Thermo Fisher)
99
Thermo Fisher 2x nupage lds protein sample buffer
2x Nupage Lds Protein Sample Buffer, supplied by Thermo Fisher, used in various techniques. Bioz Stars score: 99/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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vbs  (Santa Cruz Biotechnology)
96
Santa Cruz Biotechnology vbs
Fig. 3 Comparisons of DR3 and DR3 half-site binding effects on natural agonist- and synthetic-agonist- <t>bound</t> <t>heterodimer</t> complexes. Schematic representations illustrate differential experiments of VDRRXRα: ligand complex verse VDRRXRα: ligand: DNA complex (on the left). Consolidated differential HDX data are mapped onto the VDRRXRα heterodimer structure model in ribbon when the complex is bound to different ligands and DNA <t>VBS</t> (on the right). Conformational changes of 1,25D3-bound heterodimer upon binding of a DR3 (Supplementary Fig. 1b, d, column (v)) and b DR3 half-site (Supplementary Fig. 1b, d, column (vi)). Conformational changes of Cmpd1 bound heterodimer upon binding of c DR3 (Supplementary Fig. 1b, d, column (vii)) and d DR3 half-site (Supplementary Fig. 1b, d, column (viii)). Conformational changes of Cmpd2 bound heterodimer upon binding of e DR3 (Supplementary Fig. 1b, d, column (ix)) and f DR3 half-site (Supplementary Fig. 1b, d, column (x)). Percentages of deuterium differences are coded as Fig. 1. Dark gray, no statistically significant changes between compared conditions; light gray, regions that have no sequence coverage and include proline residue that has no amide hydrogen exchange activity; purple, 1,25D3 ligand; black, DNA VBSs
Vbs, supplied by Santa Cruz Biotechnology, used in various techniques. Bioz Stars score: 96/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/product/2x+protein+loading+buffer/pm29030554-340-14-27?v=Santa+Cruz+Biotechnology
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2x laemmli buffer  (Thermo Fisher)
99
Thermo Fisher 2x laemmli buffer
Fig. 3 Comparisons of DR3 and DR3 half-site binding effects on natural agonist- and synthetic-agonist- <t>bound</t> <t>heterodimer</t> complexes. Schematic representations illustrate differential experiments of VDRRXRα: ligand complex verse VDRRXRα: ligand: DNA complex (on the left). Consolidated differential HDX data are mapped onto the VDRRXRα heterodimer structure model in ribbon when the complex is bound to different ligands and DNA <t>VBS</t> (on the right). Conformational changes of 1,25D3-bound heterodimer upon binding of a DR3 (Supplementary Fig. 1b, d, column (v)) and b DR3 half-site (Supplementary Fig. 1b, d, column (vi)). Conformational changes of Cmpd1 bound heterodimer upon binding of c DR3 (Supplementary Fig. 1b, d, column (vii)) and d DR3 half-site (Supplementary Fig. 1b, d, column (viii)). Conformational changes of Cmpd2 bound heterodimer upon binding of e DR3 (Supplementary Fig. 1b, d, column (ix)) and f DR3 half-site (Supplementary Fig. 1b, d, column (x)). Percentages of deuterium differences are coded as Fig. 1. Dark gray, no statistically significant changes between compared conditions; light gray, regions that have no sequence coverage and include proline residue that has no amide hydrogen exchange activity; purple, 1,25D3 ligand; black, DNA VBSs
2x Laemmli Buffer, supplied by Thermo Fisher, used in various techniques. Bioz Stars score: 99/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/product/2x+protein+loading+buffer/bio_rxiv__2021__02__26__433000-53-11-44?v=Thermo+Fisher
Average 99 stars, based on 1 article reviews
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2x native trisglycine  (Thermo Fisher)
95
Thermo Fisher 2x native trisglycine
Fig. 3 Comparisons of DR3 and DR3 half-site binding effects on natural agonist- and synthetic-agonist- <t>bound</t> <t>heterodimer</t> complexes. Schematic representations illustrate differential experiments of VDRRXRα: ligand complex verse VDRRXRα: ligand: DNA complex (on the left). Consolidated differential HDX data are mapped onto the VDRRXRα heterodimer structure model in ribbon when the complex is bound to different ligands and DNA <t>VBS</t> (on the right). Conformational changes of 1,25D3-bound heterodimer upon binding of a DR3 (Supplementary Fig. 1b, d, column (v)) and b DR3 half-site (Supplementary Fig. 1b, d, column (vi)). Conformational changes of Cmpd1 bound heterodimer upon binding of c DR3 (Supplementary Fig. 1b, d, column (vii)) and d DR3 half-site (Supplementary Fig. 1b, d, column (viii)). Conformational changes of Cmpd2 bound heterodimer upon binding of e DR3 (Supplementary Fig. 1b, d, column (ix)) and f DR3 half-site (Supplementary Fig. 1b, d, column (x)). Percentages of deuterium differences are coded as Fig. 1. Dark gray, no statistically significant changes between compared conditions; light gray, regions that have no sequence coverage and include proline residue that has no amide hydrogen exchange activity; purple, 1,25D3 ligand; black, DNA VBSs
2x Native Trisglycine, supplied by Thermo Fisher, used in various techniques. Bioz Stars score: 95/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/product/2x+protein+loading+buffer/10__1096_slash_fj__201902093r-74-9-15?v=Thermo+Fisher
Average 95 stars, based on 1 article reviews
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onetaq 2x master mix  (New England Biolabs)
96
New England Biolabs onetaq 2x master mix
Fig. 3 Comparisons of DR3 and DR3 half-site binding effects on natural agonist- and synthetic-agonist- <t>bound</t> <t>heterodimer</t> complexes. Schematic representations illustrate differential experiments of VDRRXRα: ligand complex verse VDRRXRα: ligand: DNA complex (on the left). Consolidated differential HDX data are mapped onto the VDRRXRα heterodimer structure model in ribbon when the complex is bound to different ligands and DNA <t>VBS</t> (on the right). Conformational changes of 1,25D3-bound heterodimer upon binding of a DR3 (Supplementary Fig. 1b, d, column (v)) and b DR3 half-site (Supplementary Fig. 1b, d, column (vi)). Conformational changes of Cmpd1 bound heterodimer upon binding of c DR3 (Supplementary Fig. 1b, d, column (vii)) and d DR3 half-site (Supplementary Fig. 1b, d, column (viii)). Conformational changes of Cmpd2 bound heterodimer upon binding of e DR3 (Supplementary Fig. 1b, d, column (ix)) and f DR3 half-site (Supplementary Fig. 1b, d, column (x)). Percentages of deuterium differences are coded as Fig. 1. Dark gray, no statistically significant changes between compared conditions; light gray, regions that have no sequence coverage and include proline residue that has no amide hydrogen exchange activity; purple, 1,25D3 ligand; black, DNA VBSs
Onetaq 2x Master Mix, supplied by New England Biolabs, used in various techniques. Bioz Stars score: 96/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/product/2x+protein+loading+buffer/bio_rxiv__2020__07__22__216143-155-38-42?v=New+England+Biolabs
Average 96 stars, based on 1 article reviews
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2x native sample buffer  (Bio-Rad)
95
Bio-Rad 2x native sample buffer
Fig. 3 Comparisons of DR3 and DR3 half-site binding effects on natural agonist- and synthetic-agonist- <t>bound</t> <t>heterodimer</t> complexes. Schematic representations illustrate differential experiments of VDRRXRα: ligand complex verse VDRRXRα: ligand: DNA complex (on the left). Consolidated differential HDX data are mapped onto the VDRRXRα heterodimer structure model in ribbon when the complex is bound to different ligands and DNA <t>VBS</t> (on the right). Conformational changes of 1,25D3-bound heterodimer upon binding of a DR3 (Supplementary Fig. 1b, d, column (v)) and b DR3 half-site (Supplementary Fig. 1b, d, column (vi)). Conformational changes of Cmpd1 bound heterodimer upon binding of c DR3 (Supplementary Fig. 1b, d, column (vii)) and d DR3 half-site (Supplementary Fig. 1b, d, column (viii)). Conformational changes of Cmpd2 bound heterodimer upon binding of e DR3 (Supplementary Fig. 1b, d, column (ix)) and f DR3 half-site (Supplementary Fig. 1b, d, column (x)). Percentages of deuterium differences are coded as Fig. 1. Dark gray, no statistically significant changes between compared conditions; light gray, regions that have no sequence coverage and include proline residue that has no amide hydrogen exchange activity; purple, 1,25D3 ligand; black, DNA VBSs
2x Native Sample Buffer, supplied by Bio-Rad, used in various techniques. Bioz Stars score: 95/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/product/2x+protein+loading+buffer/pmc10421544-55-19-24?v=Bio-Rad
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Image Search Results


Fig. 3 Comparisons of DR3 and DR3 half-site binding effects on natural agonist- and synthetic-agonist- bound heterodimer complexes. Schematic representations illustrate differential experiments of VDRRXRα: ligand complex verse VDRRXRα: ligand: DNA complex (on the left). Consolidated differential HDX data are mapped onto the VDRRXRα heterodimer structure model in ribbon when the complex is bound to different ligands and DNA VBS (on the right). Conformational changes of 1,25D3-bound heterodimer upon binding of a DR3 (Supplementary Fig. 1b, d, column (v)) and b DR3 half-site (Supplementary Fig. 1b, d, column (vi)). Conformational changes of Cmpd1 bound heterodimer upon binding of c DR3 (Supplementary Fig. 1b, d, column (vii)) and d DR3 half-site (Supplementary Fig. 1b, d, column (viii)). Conformational changes of Cmpd2 bound heterodimer upon binding of e DR3 (Supplementary Fig. 1b, d, column (ix)) and f DR3 half-site (Supplementary Fig. 1b, d, column (x)). Percentages of deuterium differences are coded as Fig. 1. Dark gray, no statistically significant changes between compared conditions; light gray, regions that have no sequence coverage and include proline residue that has no amide hydrogen exchange activity; purple, 1,25D3 ligand; black, DNA VBSs

Journal: Nature communications

Article Title: HDX reveals the conformational dynamics of DNA sequence specific VDR co-activator interactions.

doi: 10.1038/s41467-017-00978-7

Figure Lengend Snippet: Fig. 3 Comparisons of DR3 and DR3 half-site binding effects on natural agonist- and synthetic-agonist- bound heterodimer complexes. Schematic representations illustrate differential experiments of VDRRXRα: ligand complex verse VDRRXRα: ligand: DNA complex (on the left). Consolidated differential HDX data are mapped onto the VDRRXRα heterodimer structure model in ribbon when the complex is bound to different ligands and DNA VBS (on the right). Conformational changes of 1,25D3-bound heterodimer upon binding of a DR3 (Supplementary Fig. 1b, d, column (v)) and b DR3 half-site (Supplementary Fig. 1b, d, column (vi)). Conformational changes of Cmpd1 bound heterodimer upon binding of c DR3 (Supplementary Fig. 1b, d, column (vii)) and d DR3 half-site (Supplementary Fig. 1b, d, column (viii)). Conformational changes of Cmpd2 bound heterodimer upon binding of e DR3 (Supplementary Fig. 1b, d, column (ix)) and f DR3 half-site (Supplementary Fig. 1b, d, column (x)). Percentages of deuterium differences are coded as Fig. 1. Dark gray, no statistically significant changes between compared conditions; light gray, regions that have no sequence coverage and include proline residue that has no amide hydrogen exchange activity; purple, 1,25D3 ligand; black, DNA VBSs

Article Snippet: Full-length VDRRXRα heterodimer (10 μM, 20 μl) in protein buffer was incubated with respective VBS (2X molar ratio) or anti VDR antibody (5 μl, 200 μg/ml, sc-13133, Santa Cruz Biotechnology) for 30 min on ice before mixing with 5 μl Hi-Density TBE sample buffer (Invitrogen).

Techniques: Binding Assay, Sequencing, Residue, Activity Assay

Fig. 5 Activations of VDRRXRα heterodimer with cognate VBS BGLAP and TRPV6 by selective modulator Cmpd3 verse natural ligand 1,25D3. Schematic representations illustrate differential experiments of ligand bound VDRRXRα heterodimer with respect to DNA and SRC1 RID binding (on the left). Differential consolidation HDX data are mapped onto the VDRRXR heterodimer structure model when the complex is bound to different ligands and DNA (shown in ribbon a−d), and SRC1 RID (shown in surface e−h) (on the right). Conformational changes of 1,25D3-bound heterodimer upon binding of a BGLAP VBS (Supplementary Fig. 1b, d, column (xvii)) and b TRPV6 VBS (Supplementary Fig. 1b, d, column (xviii)). Conformational changes of selective modulator Cmpd3 bound heterodimer upon binding of c BGLAP VBS (Supplementary Fig. 1b, d, column (xix)) and d TRPV6 VBS (Supplementary Fig. 1b, d, column (xx)). e Conformational changes of VDRRXRα: 1,25D3: BGLAP complex upon SRC1 RID binding (Supplementary Fig. 1b, d, column (xxi)). f Conformational changes of VDRRXRα: 1,25D3: TRPV6 complex upon SRC1 RID binding (Supplementary Fig. 1b, d, column (xxii)). g Conformational changes of VDRRXRα: Cmpd3: BGLAP complex upon SRC1 RID binding (Supplementary Fig. 1b, d, column (xxiii)). h Conformational changes of VDRRXRα: Cmpd3: TRPV6 complex upon SRC1 RID binding (Supplementary Fig. 1b, d, column (xxiv)). Percentages of deuterium differences are coded as Fig. 1. Dark gray, no statistically significant changes between compared conditions; light gray, regions that have no sequence coverage and include proline residue that has no amide hydrogen exchange activity; black, DNA VBSs; purple, 1,25D3 ligand; pink, Cmpd3. i Differential deuterium uptake plots of peptide aa411−419 from VDR H12 when heterodimer is bound to 1,25D3, DNA and SRC1 RID. j Differential deuterium uptake plots of peptide aa411−419 from VDR H12 when heterodimer is bound to Cmpd3, DNA, and SRC1 RID. The data are plotted as percent deuterium uptake verse time on a logarithmic scale

Journal: Nature communications

Article Title: HDX reveals the conformational dynamics of DNA sequence specific VDR co-activator interactions.

doi: 10.1038/s41467-017-00978-7

Figure Lengend Snippet: Fig. 5 Activations of VDRRXRα heterodimer with cognate VBS BGLAP and TRPV6 by selective modulator Cmpd3 verse natural ligand 1,25D3. Schematic representations illustrate differential experiments of ligand bound VDRRXRα heterodimer with respect to DNA and SRC1 RID binding (on the left). Differential consolidation HDX data are mapped onto the VDRRXR heterodimer structure model when the complex is bound to different ligands and DNA (shown in ribbon a−d), and SRC1 RID (shown in surface e−h) (on the right). Conformational changes of 1,25D3-bound heterodimer upon binding of a BGLAP VBS (Supplementary Fig. 1b, d, column (xvii)) and b TRPV6 VBS (Supplementary Fig. 1b, d, column (xviii)). Conformational changes of selective modulator Cmpd3 bound heterodimer upon binding of c BGLAP VBS (Supplementary Fig. 1b, d, column (xix)) and d TRPV6 VBS (Supplementary Fig. 1b, d, column (xx)). e Conformational changes of VDRRXRα: 1,25D3: BGLAP complex upon SRC1 RID binding (Supplementary Fig. 1b, d, column (xxi)). f Conformational changes of VDRRXRα: 1,25D3: TRPV6 complex upon SRC1 RID binding (Supplementary Fig. 1b, d, column (xxii)). g Conformational changes of VDRRXRα: Cmpd3: BGLAP complex upon SRC1 RID binding (Supplementary Fig. 1b, d, column (xxiii)). h Conformational changes of VDRRXRα: Cmpd3: TRPV6 complex upon SRC1 RID binding (Supplementary Fig. 1b, d, column (xxiv)). Percentages of deuterium differences are coded as Fig. 1. Dark gray, no statistically significant changes between compared conditions; light gray, regions that have no sequence coverage and include proline residue that has no amide hydrogen exchange activity; black, DNA VBSs; purple, 1,25D3 ligand; pink, Cmpd3. i Differential deuterium uptake plots of peptide aa411−419 from VDR H12 when heterodimer is bound to 1,25D3, DNA and SRC1 RID. j Differential deuterium uptake plots of peptide aa411−419 from VDR H12 when heterodimer is bound to Cmpd3, DNA, and SRC1 RID. The data are plotted as percent deuterium uptake verse time on a logarithmic scale

Article Snippet: Full-length VDRRXRα heterodimer (10 μM, 20 μl) in protein buffer was incubated with respective VBS (2X molar ratio) or anti VDR antibody (5 μl, 200 μg/ml, sc-13133, Santa Cruz Biotechnology) for 30 min on ice before mixing with 5 μl Hi-Density TBE sample buffer (Invitrogen).

Techniques: Binding Assay, Sequencing, Residue, Activity Assay