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  • 93
    Millipore superdex200 10 300gl column
    Superdex200 10 300gl Column, supplied by Millipore, used in various techniques. Bioz Stars score: 93/100, based on 3 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    GE Healthcare superdex 200 increase 10 300 column sd200
    Effects of mutations at R820 and F958 of CHUP1-C on the activity of CHUP1 (A) A schematic illustration of CHUP1 protein showing the functional domains: the hydrophobic region, the coiled-coil domain, the F-actin binding domain, the proline-rich FH1-like domain, and the FH2-like domain. Asterisks indicate R820, which is involved in the association with actin, and F958, which is involved in the dimerization of the FH2-like domain. The positions of the 611–1004 fragment (CHUP1-C) and the 611–982 and 716–982 deletion mutations are indicated by lines below the structure. (B–C) The effect of point mutations R820D and F958D on CHUP1-C dimer structure. (B) The elution profiles of CHUP1-C_WT, R820D, and F958D recombinant proteins were obtained by gel filtration chromatography using a Superdex 200 10/300 column. (C) The protein profiles were confirmed using 10% SDS-PAGE gels. (D–E) Ultracentrifugation assay of actin polymerization. ACT7 (4 µM) was allowed to polymerize in F-buffer containing 8 µM PRF1 and 0.4 µM WT or mutant CHUP1-C. (D) A representative SDS-PAGE gel of supernatant (S) and pellet (P) fractions after ultracentrifugation. (E) A bar graph showing the fraction of ACT7 in the pellet and the supernatant under each condition, with error bars showing SD (N = 3). (F) Immunoblot analysis showing the expression levels of CHUP1-YFP_R820D and CHUP1-YFP_F985D in C1Y_R820D (18-2 and 26-3) and C1Y_F958D (6-5 and 10-1) transgenic plants. The arrowhead and arrow indicate CHUP1 and CHUP1-Y, respectively. * indicates truncated CHUP1 and CHUP1-Y. The details are the same as in   Figure 2A . (G) Chloroplast photorelocation movement in WT,  chup1  mutant ( chup1-3 ), and C1Y_R820D and C1Y_F985D transgenic plants in a  chup1  background. The red light (RL) transmittance in rosette leaves was monitored under different intensities of blue light (BL; 0, 2.8, and 50 µmol m −2  s −1 ) for the indicated periods.
    Superdex 200 Increase 10 300 Column Sd200, supplied by GE Healthcare, used in various techniques. Bioz Stars score: 93/100, based on 281 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    GE Healthcare superdex 200 10 300
    Superdex 200 10/300 gel filtration chromatograph of peak 2 results from ion-exchange chromatography.
    Superdex 200 10 300, supplied by GE Healthcare, used in various techniques. Bioz Stars score: 91/100, based on 840 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    GE Healthcare superdex 200 10 200glcolumn
    Superdex 200 10/300 gel filtration chromatograph of peak 2 results from ion-exchange chromatography.
    Superdex 200 10 200glcolumn, supplied by GE Healthcare, used in various techniques. Bioz Stars score: 90/100, based on 7 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    89
    GE Healthcare superdex 200 10 30
    Superdex 200 10/300 gel filtration chromatograph of peak 2 results from ion-exchange chromatography.
    Superdex 200 10 30, supplied by GE Healthcare, used in various techniques. Bioz Stars score: 89/100, based on 156 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    85
    GE Healthcare superdex 200 10 3000gl
    Superdex 200 10/300 gel filtration chromatograph of peak 2 results from ion-exchange chromatography.
    Superdex 200 10 3000gl, supplied by GE Healthcare, used in various techniques. Bioz Stars score: 85/100, based on 15 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    GE Healthcare superdex 200 10 300column
    Superdex 200 10/300 gel filtration chromatograph of peak 2 results from ion-exchange chromatography.
    Superdex 200 10 300column, supplied by GE Healthcare, used in various techniques. Bioz Stars score: 86/100, based on 10 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    90
    GE Healthcare superdex 200 increase 10 300gl
    Purification procedures. ( a ) The sample is subjected to preliminary purification on a Ni-NTA column, and the purity was analyzed by 12% SDS-PAGE gels. M, molecular weight marker. Lanes 1–5, samples eluted sequentially at different times from the Ni-NTA column. ( b ) FPLC (1 mL HiTrap QHP) chromatogram showing effective separation. The blue line represents the UV absorption at 280 nM and the black line represents the change in the conductance. ( c ) Chromatogram of proteins purified with <t>Superdex</t> 200 increase <t>10/300GL.</t> The blue line represents the UV absorption at 280 nM. ( d ) Analysis of the quality of the g1, g1g2, g1g2g3 and g1g1 proteins after purification on 12% SDS-PAGE gels.
    Superdex 200 Increase 10 300gl, supplied by GE Healthcare, used in various techniques. Bioz Stars score: 90/100, based on 43 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    92
    Thermo Fisher superdex 200 10 300 column
    Purification procedures. ( a ) The sample is subjected to preliminary purification on a Ni-NTA column, and the purity was analyzed by 12% SDS-PAGE gels. M, molecular weight marker. Lanes 1–5, samples eluted sequentially at different times from the Ni-NTA column. ( b ) FPLC (1 mL HiTrap QHP) chromatogram showing effective separation. The blue line represents the UV absorption at 280 nM and the black line represents the change in the conductance. ( c ) Chromatogram of proteins purified with <t>Superdex</t> 200 increase <t>10/300GL.</t> The blue line represents the UV absorption at 280 nM. ( d ) Analysis of the quality of the g1, g1g2, g1g2g3 and g1g1 proteins after purification on 12% SDS-PAGE gels.
    Superdex 200 10 300 Column, supplied by Thermo Fisher, used in various techniques. Bioz Stars score: 92/100, based on 27 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    GE Healthcare superdex 200 10 30 column
    Oligomeric assembly of recombinant ClpP1 and ClpP2 . 75 μg of recombinant ClpP1 (upper panel, solid line) or ClpP2 (middle panel, solid line) produced independently or in the presence of ClpP2 (upper panel, dashed line) and ClpP1 (middle panel, dashed line) respectively were loaded on a superdex 200 10/30 column as described in the Methods section. In the lower panel, 75 μg of ClpP1 were mixed with 75 μg of ClpP2 and incubated 2 h at room temperature before being loaded on the superdex 200 column. Arrowheads indicate the elution of molecular mass standards with their molecular mass in kDa and the deduced apparent molecular masses are shown under the corresponding protein names.
    Superdex 200 10 30 Column, supplied by GE Healthcare, used in various techniques. Bioz Stars score: 90/100, based on 676 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    GE Healthcare superdex 200 10 60 column
    Oligomeric assembly of recombinant ClpP1 and ClpP2 . 75 μg of recombinant ClpP1 (upper panel, solid line) or ClpP2 (middle panel, solid line) produced independently or in the presence of ClpP2 (upper panel, dashed line) and ClpP1 (middle panel, dashed line) respectively were loaded on a superdex 200 10/30 column as described in the Methods section. In the lower panel, 75 μg of ClpP1 were mixed with 75 μg of ClpP2 and incubated 2 h at room temperature before being loaded on the superdex 200 column. Arrowheads indicate the elution of molecular mass standards with their molecular mass in kDa and the deduced apparent molecular masses are shown under the corresponding protein names.
    Superdex 200 10 60 Column, supplied by GE Healthcare, used in various techniques. Bioz Stars score: 85/100, based on 42 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    GE Healthcare superdex 200 10 300gl column
    Oligomeric assembly of recombinant ClpP1 and ClpP2 . 75 μg of recombinant ClpP1 (upper panel, solid line) or ClpP2 (middle panel, solid line) produced independently or in the presence of ClpP2 (upper panel, dashed line) and ClpP1 (middle panel, dashed line) respectively were loaded on a superdex 200 10/30 column as described in the Methods section. In the lower panel, 75 μg of ClpP1 were mixed with 75 μg of ClpP2 and incubated 2 h at room temperature before being loaded on the superdex 200 column. Arrowheads indicate the elution of molecular mass standards with their molecular mass in kDa and the deduced apparent molecular masses are shown under the corresponding protein names.
    Superdex 200 10 300gl Column, supplied by GE Healthcare, used in various techniques. Bioz Stars score: 88/100, based on 127 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    GE Healthcare superdex 200 hr10 10 column
    Oligomeric assembly of recombinant ClpP1 and ClpP2 . 75 μg of recombinant ClpP1 (upper panel, solid line) or ClpP2 (middle panel, solid line) produced independently or in the presence of ClpP2 (upper panel, dashed line) and ClpP1 (middle panel, dashed line) respectively were loaded on a superdex 200 10/30 column as described in the Methods section. In the lower panel, 75 μg of ClpP1 were mixed with 75 μg of ClpP2 and incubated 2 h at room temperature before being loaded on the superdex 200 column. Arrowheads indicate the elution of molecular mass standards with their molecular mass in kDa and the deduced apparent molecular masses are shown under the corresponding protein names.
    Superdex 200 Hr10 10 Column, supplied by GE Healthcare, used in various techniques. Bioz Stars score: 85/100, based on 8 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Image Search Results


    Effects of mutations at R820 and F958 of CHUP1-C on the activity of CHUP1 (A) A schematic illustration of CHUP1 protein showing the functional domains: the hydrophobic region, the coiled-coil domain, the F-actin binding domain, the proline-rich FH1-like domain, and the FH2-like domain. Asterisks indicate R820, which is involved in the association with actin, and F958, which is involved in the dimerization of the FH2-like domain. The positions of the 611–1004 fragment (CHUP1-C) and the 611–982 and 716–982 deletion mutations are indicated by lines below the structure. (B–C) The effect of point mutations R820D and F958D on CHUP1-C dimer structure. (B) The elution profiles of CHUP1-C_WT, R820D, and F958D recombinant proteins were obtained by gel filtration chromatography using a Superdex 200 10/300 column. (C) The protein profiles were confirmed using 10% SDS-PAGE gels. (D–E) Ultracentrifugation assay of actin polymerization. ACT7 (4 µM) was allowed to polymerize in F-buffer containing 8 µM PRF1 and 0.4 µM WT or mutant CHUP1-C. (D) A representative SDS-PAGE gel of supernatant (S) and pellet (P) fractions after ultracentrifugation. (E) A bar graph showing the fraction of ACT7 in the pellet and the supernatant under each condition, with error bars showing SD (N = 3). (F) Immunoblot analysis showing the expression levels of CHUP1-YFP_R820D and CHUP1-YFP_F985D in C1Y_R820D (18-2 and 26-3) and C1Y_F958D (6-5 and 10-1) transgenic plants. The arrowhead and arrow indicate CHUP1 and CHUP1-Y, respectively. * indicates truncated CHUP1 and CHUP1-Y. The details are the same as in   Figure 2A . (G) Chloroplast photorelocation movement in WT,  chup1  mutant ( chup1-3 ), and C1Y_R820D and C1Y_F985D transgenic plants in a  chup1  background. The red light (RL) transmittance in rosette leaves was monitored under different intensities of blue light (BL; 0, 2.8, and 50 µmol m −2  s −1 ) for the indicated periods.

    Journal: bioRxiv

    Article Title: CHLOROPLAST UNUSUAL POSITIONING 1 is a new type of actin nucleation factor in plants

    doi: 10.1101/2020.01.14.905984

    Figure Lengend Snippet: Effects of mutations at R820 and F958 of CHUP1-C on the activity of CHUP1 (A) A schematic illustration of CHUP1 protein showing the functional domains: the hydrophobic region, the coiled-coil domain, the F-actin binding domain, the proline-rich FH1-like domain, and the FH2-like domain. Asterisks indicate R820, which is involved in the association with actin, and F958, which is involved in the dimerization of the FH2-like domain. The positions of the 611–1004 fragment (CHUP1-C) and the 611–982 and 716–982 deletion mutations are indicated by lines below the structure. (B–C) The effect of point mutations R820D and F958D on CHUP1-C dimer structure. (B) The elution profiles of CHUP1-C_WT, R820D, and F958D recombinant proteins were obtained by gel filtration chromatography using a Superdex 200 10/300 column. (C) The protein profiles were confirmed using 10% SDS-PAGE gels. (D–E) Ultracentrifugation assay of actin polymerization. ACT7 (4 µM) was allowed to polymerize in F-buffer containing 8 µM PRF1 and 0.4 µM WT or mutant CHUP1-C. (D) A representative SDS-PAGE gel of supernatant (S) and pellet (P) fractions after ultracentrifugation. (E) A bar graph showing the fraction of ACT7 in the pellet and the supernatant under each condition, with error bars showing SD (N = 3). (F) Immunoblot analysis showing the expression levels of CHUP1-YFP_R820D and CHUP1-YFP_F985D in C1Y_R820D (18-2 and 26-3) and C1Y_F958D (6-5 and 10-1) transgenic plants. The arrowhead and arrow indicate CHUP1 and CHUP1-Y, respectively. * indicates truncated CHUP1 and CHUP1-Y. The details are the same as in Figure 2A . (G) Chloroplast photorelocation movement in WT, chup1 mutant ( chup1-3 ), and C1Y_R820D and C1Y_F985D transgenic plants in a chup1 background. The red light (RL) transmittance in rosette leaves was monitored under different intensities of blue light (BL; 0, 2.8, and 50 µmol m −2 s −1 ) for the indicated periods.

    Article Snippet: The eluted CHUP1-C was further purified in a buffer (10 mM HEPES pH 7.4, 100 mM NaCl, 2 mM MgCl2 , 1 mM DTT) by size-exclusion chromatography using a Superdex 200 10/300 column (GE Healthcare).

    Techniques: Activity Assay, Functional Assay, Binding Assay, Recombinant, Filtration, Chromatography, SDS Page, Mutagenesis, Expressing, Transgenic Assay

    Superdex 200 10/300 gel filtration chromatograph of peak 2 results from ion-exchange chromatography.

    Journal: Molecules : A Journal of Synthetic Chemistry and Natural Product Chemistry

    Article Title: High Hydrostatic Pressure (HHP)-Induced Structural Modification of Patatin and Its Antioxidant Activities

    doi: 10.3390/molecules22030438

    Figure Lengend Snippet: Superdex 200 10/300 gel filtration chromatograph of peak 2 results from ion-exchange chromatography.

    Article Snippet: DEAE-sepharose fast flow and superdex 200 10/300 were obtained from (GE Healthcare BioScience, Stockholm, Sweden).

    Techniques: Filtration, Ion Exchange Chromatography

    Analysis of the ∆NTE O interaction with oxFRPcc. a A fixed concentration of ∆NTE O was titrated by increasing amounts of oxFRPcc (indicated in µM per dimer); the samples (100 µl) were analyzed using a Superdex 200 Increase 10/300 column in the absence of reducing agents. Arrows indicate the direction of titration. b The binding curve obtained upon quantification of the amplitude of the ∆NTE O –oxFRPcc peak presented in a , in comparison with the curve for FRPwt (identical conditions). c Pairwise distance distribution functions for ∆NTE O , oxFRPcc dimer, and their complex obtained using GNOM. d One of the possible conformations of the ∆NTE O –oxFRPcc complex (1:2) consistent with the SAXS data and complementary information, shown as the CORAL-derived atomistic model overlaid with the best fitting GASBOR-derived ab initio bead model. Dashed circle in d marks the tentative FRP binding site located on the β-sheet of the OCP-CTD, normally occupied by NTE in OCP O . e The fit of the CORAL model to the SAXS data with the associated residuals (∆/σ). f Hypothetical 2:2 binding on top of the 1:2 complex suggested by crosslinking experiments. Although two tentative OCP-binding sites on the head domains of FRP may coexist, the 2:2 binding leads to a clash between OCP molecules (marked by a red dashed circle). In the dissociable FRPwt, such a binding may provoke FRP monomerization and formation of the 1:1 heterocomplexes to relieve tension caused by the clashing OCP molecules. In oxFRPcc, this is not possible because of the covalent interface stabilization by disulfides

    Journal: Nature Communications

    Article Title: OCP–FRP protein complex topologies suggest a mechanism for controlling high light tolerance in cyanobacteria

    doi: 10.1038/s41467-018-06195-0

    Figure Lengend Snippet: Analysis of the ∆NTE O interaction with oxFRPcc. a A fixed concentration of ∆NTE O was titrated by increasing amounts of oxFRPcc (indicated in µM per dimer); the samples (100 µl) were analyzed using a Superdex 200 Increase 10/300 column in the absence of reducing agents. Arrows indicate the direction of titration. b The binding curve obtained upon quantification of the amplitude of the ∆NTE O –oxFRPcc peak presented in a , in comparison with the curve for FRPwt (identical conditions). c Pairwise distance distribution functions for ∆NTE O , oxFRPcc dimer, and their complex obtained using GNOM. d One of the possible conformations of the ∆NTE O –oxFRPcc complex (1:2) consistent with the SAXS data and complementary information, shown as the CORAL-derived atomistic model overlaid with the best fitting GASBOR-derived ab initio bead model. Dashed circle in d marks the tentative FRP binding site located on the β-sheet of the OCP-CTD, normally occupied by NTE in OCP O . e The fit of the CORAL model to the SAXS data with the associated residuals (∆/σ). f Hypothetical 2:2 binding on top of the 1:2 complex suggested by crosslinking experiments. Although two tentative OCP-binding sites on the head domains of FRP may coexist, the 2:2 binding leads to a clash between OCP molecules (marked by a red dashed circle). In the dissociable FRPwt, such a binding may provoke FRP monomerization and formation of the 1:1 heterocomplexes to relieve tension caused by the clashing OCP molecules. In oxFRPcc, this is not possible because of the covalent interface stabilization by disulfides

    Article Snippet: Oligomeric state of FRP species and their interaction with various OCP forms were analyzed by SEC on either Superdex 200 Increase 10/300 or Superdex 200 Increase 5/150 columns (both GE Healthcare) operated using a ProStar 325 chromatographic system (Varian) with simultaneous UV/vis detection.

    Techniques: Concentration Assay, Titration, Binding Assay, Derivative Assay

    FRP mutants with the predefined oligomeric structure. a Overall view on the 4JDX structure of the Synechocystis FRP dimer with two subunits colored by yellow and cyan. b Close-up of the subunit interface showing positions of L49 residues (salmon sticks and semitransparent spheres) mutated to Glu to provoke dimer dissociation. c Close-up of the subunit interface showing positions of L33 (orange sticks) and I43 (slate sticks) residues as optimal candidates (Cβ atoms separated by ~6.5 Å) for the intersubunit disulfide crosslinking. Analysis of the quarternary structure of the engineered FRP mutants using native PAGE ( d ) and chemical crosslinking followed by SDS-PAGE ( e ). FRPwt and oxFRPcc were crosslinked in the presence of GA (+ lanes); control samples (− lanes) did not include GA. f Analytical SEC on a Superdex 200 Increase 10/300 column of the engineered FRP mutants at different FRP concentrations (indicated in µM per monomer) under reducing conditions. g The dependence of the apparent M w for the FRP-L49E, oxFRPcc, and redFRPcc on loaded protein concentration as calculated from column calibration

    Journal: Nature Communications

    Article Title: OCP–FRP protein complex topologies suggest a mechanism for controlling high light tolerance in cyanobacteria

    doi: 10.1038/s41467-018-06195-0

    Figure Lengend Snippet: FRP mutants with the predefined oligomeric structure. a Overall view on the 4JDX structure of the Synechocystis FRP dimer with two subunits colored by yellow and cyan. b Close-up of the subunit interface showing positions of L49 residues (salmon sticks and semitransparent spheres) mutated to Glu to provoke dimer dissociation. c Close-up of the subunit interface showing positions of L33 (orange sticks) and I43 (slate sticks) residues as optimal candidates (Cβ atoms separated by ~6.5 Å) for the intersubunit disulfide crosslinking. Analysis of the quarternary structure of the engineered FRP mutants using native PAGE ( d ) and chemical crosslinking followed by SDS-PAGE ( e ). FRPwt and oxFRPcc were crosslinked in the presence of GA (+ lanes); control samples (− lanes) did not include GA. f Analytical SEC on a Superdex 200 Increase 10/300 column of the engineered FRP mutants at different FRP concentrations (indicated in µM per monomer) under reducing conditions. g The dependence of the apparent M w for the FRP-L49E, oxFRPcc, and redFRPcc on loaded protein concentration as calculated from column calibration

    Article Snippet: Oligomeric state of FRP species and their interaction with various OCP forms were analyzed by SEC on either Superdex 200 Increase 10/300 or Superdex 200 Increase 5/150 columns (both GE Healthcare) operated using a ProStar 325 chromatographic system (Varian) with simultaneous UV/vis detection.

    Techniques: Clear Native PAGE, SDS Page, Size-exclusion Chromatography, Protein Concentration

    Physical interaction of the FRP mutants with various OCP forms studied by analytical SEC. Either redFRPcc ( a , b , c ) or FRP-L49E ( d , e , f ) were pre-incubated alone or in the presence of either OCP AA ( a , d ), ∆NTE O ( b , e ), or COCP ( c , f ) and then analyzed by SEC on a Superdex 200 Increase 10/300 column by following either protein-specific or carotenoid-specific absorbance (wavelengths are indicated). Distinct peaks of the complexes are marked by C. Load concentrations of FRP species, OCP AA , ∆NTE O , and COCP were equal to 50, 37, 6, and 8 µM, respectively

    Journal: Nature Communications

    Article Title: OCP–FRP protein complex topologies suggest a mechanism for controlling high light tolerance in cyanobacteria

    doi: 10.1038/s41467-018-06195-0

    Figure Lengend Snippet: Physical interaction of the FRP mutants with various OCP forms studied by analytical SEC. Either redFRPcc ( a , b , c ) or FRP-L49E ( d , e , f ) were pre-incubated alone or in the presence of either OCP AA ( a , d ), ∆NTE O ( b , e ), or COCP ( c , f ) and then analyzed by SEC on a Superdex 200 Increase 10/300 column by following either protein-specific or carotenoid-specific absorbance (wavelengths are indicated). Distinct peaks of the complexes are marked by C. Load concentrations of FRP species, OCP AA , ∆NTE O , and COCP were equal to 50, 37, 6, and 8 µM, respectively

    Article Snippet: Oligomeric state of FRP species and their interaction with various OCP forms were analyzed by SEC on either Superdex 200 Increase 10/300 or Superdex 200 Increase 5/150 columns (both GE Healthcare) operated using a ProStar 325 chromatographic system (Varian) with simultaneous UV/vis detection.

    Techniques: Size-exclusion Chromatography, Incubation

    Oligomerization state and absorption spectra of the WT and tryptophan mutants of Erv1 ( a ) Gel filtration chromatography profiles of the WT (black line) and six tryptphan mutants (as indicated) on a Superdex 200 column. ( b ) UV-visible spectra of the WT and tryptophan mutants.

    Journal: Bioscience Reports

    Article Title: Role of tryptophan residues of Erv1: Trp95 and Trp183 are important for its folding and oxidase function

    doi: 10.1042/BSR20150144

    Figure Lengend Snippet: Oligomerization state and absorption spectra of the WT and tryptophan mutants of Erv1 ( a ) Gel filtration chromatography profiles of the WT (black line) and six tryptphan mutants (as indicated) on a Superdex 200 column. ( b ) UV-visible spectra of the WT and tryptophan mutants.

    Article Snippet: The affinity-purified proteins were further separated for use in in vitro studies by gel filtration chromatography using a Superdex 200 (or Superdex 75) 10/30 column connected to an ÄKTA-FPLC system (GE Healthcare) at 4°C in BAE (150 mM NaCl, 50 mM Tris/HCl, 1 mM EDTA, pH 7.4).

    Techniques: Filtration, Chromatography

    Purification procedures. ( a ) The sample is subjected to preliminary purification on a Ni-NTA column, and the purity was analyzed by 12% SDS-PAGE gels. M, molecular weight marker. Lanes 1–5, samples eluted sequentially at different times from the Ni-NTA column. ( b ) FPLC (1 mL HiTrap QHP) chromatogram showing effective separation. The blue line represents the UV absorption at 280 nM and the black line represents the change in the conductance. ( c ) Chromatogram of proteins purified with Superdex 200 increase 10/300GL. The blue line represents the UV absorption at 280 nM. ( d ) Analysis of the quality of the g1, g1g2, g1g2g3 and g1g1 proteins after purification on 12% SDS-PAGE gels.

    Journal: Molecules

    Article Title: Purification and Functional Characterization of the C-Terminal Domain of the β-Actin-Binding Protein AIM1 In Vitro

    doi: 10.3390/molecules23123281

    Figure Lengend Snippet: Purification procedures. ( a ) The sample is subjected to preliminary purification on a Ni-NTA column, and the purity was analyzed by 12% SDS-PAGE gels. M, molecular weight marker. Lanes 1–5, samples eluted sequentially at different times from the Ni-NTA column. ( b ) FPLC (1 mL HiTrap QHP) chromatogram showing effective separation. The blue line represents the UV absorption at 280 nM and the black line represents the change in the conductance. ( c ) Chromatogram of proteins purified with Superdex 200 increase 10/300GL. The blue line represents the UV absorption at 280 nM. ( d ) Analysis of the quality of the g1, g1g2, g1g2g3 and g1g1 proteins after purification on 12% SDS-PAGE gels.

    Article Snippet: The Ni-NTA column, 1 mL HisTrap HP column, 1 mL HiTrap QHP column and Superdex 200 increase 10/300GL were purchased from GE Healthcare.

    Techniques: Purification, SDS Page, Molecular Weight, Marker, Fast Protein Liquid Chromatography

    Oligomeric assembly of recombinant ClpP1 and ClpP2 . 75 μg of recombinant ClpP1 (upper panel, solid line) or ClpP2 (middle panel, solid line) produced independently or in the presence of ClpP2 (upper panel, dashed line) and ClpP1 (middle panel, dashed line) respectively were loaded on a superdex 200 10/30 column as described in the Methods section. In the lower panel, 75 μg of ClpP1 were mixed with 75 μg of ClpP2 and incubated 2 h at room temperature before being loaded on the superdex 200 column. Arrowheads indicate the elution of molecular mass standards with their molecular mass in kDa and the deduced apparent molecular masses are shown under the corresponding protein names.

    Journal: BMC Biochemistry

    Article Title: Assembly and proteolytic processing of mycobacterial ClpP1 and ClpP2

    doi: 10.1186/1471-2091-12-61

    Figure Lengend Snippet: Oligomeric assembly of recombinant ClpP1 and ClpP2 . 75 μg of recombinant ClpP1 (upper panel, solid line) or ClpP2 (middle panel, solid line) produced independently or in the presence of ClpP2 (upper panel, dashed line) and ClpP1 (middle panel, dashed line) respectively were loaded on a superdex 200 10/30 column as described in the Methods section. In the lower panel, 75 μg of ClpP1 were mixed with 75 μg of ClpP2 and incubated 2 h at room temperature before being loaded on the superdex 200 column. Arrowheads indicate the elution of molecular mass standards with their molecular mass in kDa and the deduced apparent molecular masses are shown under the corresponding protein names.

    Article Snippet: Size exclusion chromatography SEC was carried out at room temperature on a Superdex 200 10/30 column (GE Healthcare) equilibrated with 25 mM Tris-HCl, pH 7.5, 150 mM KCl, and 1 mM DTT.

    Techniques: Recombinant, Produced, Incubation

    ClpP1 and ClpP2 interact with  E. coli  ClpP and inhibit its peptidase activity . (A) Hydrolysis of the Suc-LY-Amc peptide was carried out as described in the Methods section with 5 μg (black triangles) or 10 μg (all other samples) of the indicated purified proteins produced in BL21(DE3) (closed symbols) or in SG1146a cells (open symbols). (B) Size-exclusion chromatography of recombinant ClpP2 purified from BL21(DE3) when expressed as the  clpP1-clpP2(his) 6  operon. 500 μg of purified ClpP2(His) 6  was loaded on a Superdex 200 10/30 column as described in the Methods section. Arrowheads indicate the elution of molecular mass standards with their molecular mass in kDa. The horizontal bar indicates the fractions that were collected and pooled for measurement of peptidase activity in Figure 1C. (C) Hydrolysis of the Suc-LY-Amc peptide by 10 μg of the recombinant ClpP2(His) 6  purified by SEC as described in (B) after 2 (black circles), 17 (black triangles), and 50 (black squares) days of storage at 4°C. (D) Hydrolysis of the Suc-LY-Amc peptide by 10 μg of total extracts of SG1146a cells overexpressing the pET26b plasmid (open circles) or BL21(DE3) cells overexpressing the pET26b plasmid (black circles), the pET26b plasmid carrying the  clpP1(his) 6  (black squares) or the  clpP2(his) 6  (black triangles) open reading frames, or the  clpP1-clpP2(his) 6  operon (black diamonds).

    Journal: BMC Biochemistry

    Article Title: Assembly and proteolytic processing of mycobacterial ClpP1 and ClpP2

    doi: 10.1186/1471-2091-12-61

    Figure Lengend Snippet: ClpP1 and ClpP2 interact with E. coli ClpP and inhibit its peptidase activity . (A) Hydrolysis of the Suc-LY-Amc peptide was carried out as described in the Methods section with 5 μg (black triangles) or 10 μg (all other samples) of the indicated purified proteins produced in BL21(DE3) (closed symbols) or in SG1146a cells (open symbols). (B) Size-exclusion chromatography of recombinant ClpP2 purified from BL21(DE3) when expressed as the clpP1-clpP2(his) 6 operon. 500 μg of purified ClpP2(His) 6 was loaded on a Superdex 200 10/30 column as described in the Methods section. Arrowheads indicate the elution of molecular mass standards with their molecular mass in kDa. The horizontal bar indicates the fractions that were collected and pooled for measurement of peptidase activity in Figure 1C. (C) Hydrolysis of the Suc-LY-Amc peptide by 10 μg of the recombinant ClpP2(His) 6 purified by SEC as described in (B) after 2 (black circles), 17 (black triangles), and 50 (black squares) days of storage at 4°C. (D) Hydrolysis of the Suc-LY-Amc peptide by 10 μg of total extracts of SG1146a cells overexpressing the pET26b plasmid (open circles) or BL21(DE3) cells overexpressing the pET26b plasmid (black circles), the pET26b plasmid carrying the clpP1(his) 6 (black squares) or the clpP2(his) 6 (black triangles) open reading frames, or the clpP1-clpP2(his) 6 operon (black diamonds).

    Article Snippet: Size exclusion chromatography SEC was carried out at room temperature on a Superdex 200 10/30 column (GE Healthcare) equilibrated with 25 mM Tris-HCl, pH 7.5, 150 mM KCl, and 1 mM DTT.

    Techniques: Activity Assay, Purification, Produced, Size-exclusion Chromatography, Recombinant, Plasmid Preparation