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GE Healthcare ion exchange mono s columns
Purification of recombinant Mical Redox protein. Coomassie stained bands are shown and the arrowheads point to the His(6)-tagged Mical Redox protein in all gels. ( A ) Mical Redox protein (arrowhead) eluted from Nickel <t>columns</t> was observed in multiple fractions. Cpn60 can also be seen (large band above the Mical Redox protein). The fractions containing Mical Redox protein (e.g., 11–68) were combined to load on to an <t>ion-exchange</t> column. In this particular purification, only fractions 38–59 (black bracket) were combined and used for loading on the ion-exchange column. ( B ) A strong cation exchange <t>Mono</t> <t>S</t> column was used to separate Mical Redox protein (arrowhead) from other contaminating proteins including Cpn60. Fractions enriched with Mical Redox protein (22–25; black bracket) were combined and the buffer system was changed to the storage buffer. ( C ) Mical Redox protein (arrowhead) and purity were checked by running on a gel next to known concentrations of bovine serum albumin (BSA) protein. M, protein markers; I, input; F, flow-through; W, wash.
Ion Exchange Mono S Columns, supplied by GE Healthcare, used in various techniques. Bioz Stars score: 95/100, based on 2 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/result/ion exchange mono s columns/product/GE Healthcare
Average 95 stars, based on 2 article reviews
Price from $9.99 to $1999.99
ion exchange mono s columns - by Bioz Stars, 2022-09
95/100 stars

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1) Product Images from "Enhanced Production of the Mical Redox Domain for Enzymology and F-actin Disassembly Assays"

Article Title: Enhanced Production of the Mical Redox Domain for Enzymology and F-actin Disassembly Assays

Journal: International Journal of Molecular Sciences

doi: 10.3390/ijms22041991

Purification of recombinant Mical Redox protein. Coomassie stained bands are shown and the arrowheads point to the His(6)-tagged Mical Redox protein in all gels. ( A ) Mical Redox protein (arrowhead) eluted from Nickel columns was observed in multiple fractions. Cpn60 can also be seen (large band above the Mical Redox protein). The fractions containing Mical Redox protein (e.g., 11–68) were combined to load on to an ion-exchange column. In this particular purification, only fractions 38–59 (black bracket) were combined and used for loading on the ion-exchange column. ( B ) A strong cation exchange Mono S column was used to separate Mical Redox protein (arrowhead) from other contaminating proteins including Cpn60. Fractions enriched with Mical Redox protein (22–25; black bracket) were combined and the buffer system was changed to the storage buffer. ( C ) Mical Redox protein (arrowhead) and purity were checked by running on a gel next to known concentrations of bovine serum albumin (BSA) protein. M, protein markers; I, input; F, flow-through; W, wash.
Figure Legend Snippet: Purification of recombinant Mical Redox protein. Coomassie stained bands are shown and the arrowheads point to the His(6)-tagged Mical Redox protein in all gels. ( A ) Mical Redox protein (arrowhead) eluted from Nickel columns was observed in multiple fractions. Cpn60 can also be seen (large band above the Mical Redox protein). The fractions containing Mical Redox protein (e.g., 11–68) were combined to load on to an ion-exchange column. In this particular purification, only fractions 38–59 (black bracket) were combined and used for loading on the ion-exchange column. ( B ) A strong cation exchange Mono S column was used to separate Mical Redox protein (arrowhead) from other contaminating proteins including Cpn60. Fractions enriched with Mical Redox protein (22–25; black bracket) were combined and the buffer system was changed to the storage buffer. ( C ) Mical Redox protein (arrowhead) and purity were checked by running on a gel next to known concentrations of bovine serum albumin (BSA) protein. M, protein markers; I, input; F, flow-through; W, wash.

Techniques Used: Purification, Recombinant, Staining

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  • 95
    GE Healthcare ion exchange mono s columns
    Purification of recombinant Mical Redox protein. Coomassie stained bands are shown and the arrowheads point to the His(6)-tagged Mical Redox protein in all gels. ( A ) Mical Redox protein (arrowhead) eluted from Nickel <t>columns</t> was observed in multiple fractions. Cpn60 can also be seen (large band above the Mical Redox protein). The fractions containing Mical Redox protein (e.g., 11–68) were combined to load on to an <t>ion-exchange</t> column. In this particular purification, only fractions 38–59 (black bracket) were combined and used for loading on the ion-exchange column. ( B ) A strong cation exchange <t>Mono</t> <t>S</t> column was used to separate Mical Redox protein (arrowhead) from other contaminating proteins including Cpn60. Fractions enriched with Mical Redox protein (22–25; black bracket) were combined and the buffer system was changed to the storage buffer. ( C ) Mical Redox protein (arrowhead) and purity were checked by running on a gel next to known concentrations of bovine serum albumin (BSA) protein. M, protein markers; I, input; F, flow-through; W, wash.
    Ion Exchange Mono S Columns, supplied by GE Healthcare, 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/result/ion exchange mono s columns/product/GE Healthcare
    Average 95 stars, based on 1 article reviews
    Price from $9.99 to $1999.99
    ion exchange mono s columns - by Bioz Stars, 2022-09
    95/100 stars
      Buy from Supplier

    94
    GE Healthcare mono s b3bp smr ion exchange column
    Superimpositions among the TmMutS2-dsDNA/-FWJ-DNA SAXS models and the <t>Smr</t> structure/model. ( A ) The left structure is the monomeric Smr domain of H. sapiens <t>B3bp</t> (B3bp-Smr), and the right model is the predicted monomeric Smr domain of TmMutS2 (TmS2-Smr). ( B ) Superimpositions of the TmMutS2-dsDNA/-FWJ-DNA SAXS model to the B3bp-Smr structure and the TmS2-Smr model. ( C ) Superimpositions of the TmMutS2-dsDNA/-FWJ-DNA SAXS model to the B3bp-exSmr SAXS model (green mesh). The B3bp-Smr structure (red) fits well with the B3bp-exSmr SAXS model.
    Mono S B3bp Smr Ion Exchange Column, supplied by GE Healthcare, 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/result/mono s b3bp smr ion exchange column/product/GE Healthcare
    Average 94 stars, based on 1 article reviews
    Price from $9.99 to $1999.99
    mono s b3bp smr ion exchange column - by Bioz Stars, 2022-09
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    94
    GE Healthcare ion exchange chromatography
    Superimpositions among the TmMutS2-dsDNA/-FWJ-DNA SAXS models and the <t>Smr</t> structure/model. ( A ) The left structure is the monomeric Smr domain of H. sapiens <t>B3bp</t> (B3bp-Smr), and the right model is the predicted monomeric Smr domain of TmMutS2 (TmS2-Smr). ( B ) Superimpositions of the TmMutS2-dsDNA/-FWJ-DNA SAXS model to the B3bp-Smr structure and the TmS2-Smr model. ( C ) Superimpositions of the TmMutS2-dsDNA/-FWJ-DNA SAXS model to the B3bp-exSmr SAXS model (green mesh). The B3bp-Smr structure (red) fits well with the B3bp-exSmr SAXS model.
    Ion Exchange Chromatography, supplied by GE Healthcare, 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/result/ion exchange chromatography/product/GE Healthcare
    Average 94 stars, based on 1 article reviews
    Price from $9.99 to $1999.99
    ion exchange chromatography - by Bioz Stars, 2022-09
    94/100 stars
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    93
    GE Healthcare ion exchange mono q column
    Superimpositions among the TmMutS2-dsDNA/-FWJ-DNA SAXS models and the <t>Smr</t> structure/model. ( A ) The left structure is the monomeric Smr domain of H. sapiens <t>B3bp</t> (B3bp-Smr), and the right model is the predicted monomeric Smr domain of TmMutS2 (TmS2-Smr). ( B ) Superimpositions of the TmMutS2-dsDNA/-FWJ-DNA SAXS model to the B3bp-Smr structure and the TmS2-Smr model. ( C ) Superimpositions of the TmMutS2-dsDNA/-FWJ-DNA SAXS model to the B3bp-exSmr SAXS model (green mesh). The B3bp-Smr structure (red) fits well with the B3bp-exSmr SAXS model.
    Ion Exchange Mono Q Column, supplied by GE Healthcare, used in various techniques. Bioz Stars score: 93/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/ion exchange mono q column/product/GE Healthcare
    Average 93 stars, based on 1 article reviews
    Price from $9.99 to $1999.99
    ion exchange mono q column - by Bioz Stars, 2022-09
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    Purification of recombinant Mical Redox protein. Coomassie stained bands are shown and the arrowheads point to the His(6)-tagged Mical Redox protein in all gels. ( A ) Mical Redox protein (arrowhead) eluted from Nickel columns was observed in multiple fractions. Cpn60 can also be seen (large band above the Mical Redox protein). The fractions containing Mical Redox protein (e.g., 11–68) were combined to load on to an ion-exchange column. In this particular purification, only fractions 38–59 (black bracket) were combined and used for loading on the ion-exchange column. ( B ) A strong cation exchange Mono S column was used to separate Mical Redox protein (arrowhead) from other contaminating proteins including Cpn60. Fractions enriched with Mical Redox protein (22–25; black bracket) were combined and the buffer system was changed to the storage buffer. ( C ) Mical Redox protein (arrowhead) and purity were checked by running on a gel next to known concentrations of bovine serum albumin (BSA) protein. M, protein markers; I, input; F, flow-through; W, wash.

    Journal: International Journal of Molecular Sciences

    Article Title: Enhanced Production of the Mical Redox Domain for Enzymology and F-actin Disassembly Assays

    doi: 10.3390/ijms22041991

    Figure Lengend Snippet: Purification of recombinant Mical Redox protein. Coomassie stained bands are shown and the arrowheads point to the His(6)-tagged Mical Redox protein in all gels. ( A ) Mical Redox protein (arrowhead) eluted from Nickel columns was observed in multiple fractions. Cpn60 can also be seen (large band above the Mical Redox protein). The fractions containing Mical Redox protein (e.g., 11–68) were combined to load on to an ion-exchange column. In this particular purification, only fractions 38–59 (black bracket) were combined and used for loading on the ion-exchange column. ( B ) A strong cation exchange Mono S column was used to separate Mical Redox protein (arrowhead) from other contaminating proteins including Cpn60. Fractions enriched with Mical Redox protein (22–25; black bracket) were combined and the buffer system was changed to the storage buffer. ( C ) Mical Redox protein (arrowhead) and purity were checked by running on a gel next to known concentrations of bovine serum albumin (BSA) protein. M, protein markers; I, input; F, flow-through; W, wash.

    Article Snippet: Ni2+- NTA Columns (HisTrapTM FF), ion-exchange Mono S columns (Mono STM 5/50 GL) and FPLC (AKTA Purifier UPC 10) were from GE Healthcare Bio-Sciences Corporation (Piscataway, NJ, USA).

    Techniques: Purification, Recombinant, Staining

    Superimpositions among the TmMutS2-dsDNA/-FWJ-DNA SAXS models and the Smr structure/model. ( A ) The left structure is the monomeric Smr domain of H. sapiens B3bp (B3bp-Smr), and the right model is the predicted monomeric Smr domain of TmMutS2 (TmS2-Smr). ( B ) Superimpositions of the TmMutS2-dsDNA/-FWJ-DNA SAXS model to the B3bp-Smr structure and the TmS2-Smr model. ( C ) Superimpositions of the TmMutS2-dsDNA/-FWJ-DNA SAXS model to the B3bp-exSmr SAXS model (green mesh). The B3bp-Smr structure (red) fits well with the B3bp-exSmr SAXS model.

    Journal: PLoS ONE

    Article Title: Characterization of Multi-Functional Properties and Conformational Analysis of MutS2 from Thermotoga maritima MSB8

    doi: 10.1371/journal.pone.0034529

    Figure Lengend Snippet: Superimpositions among the TmMutS2-dsDNA/-FWJ-DNA SAXS models and the Smr structure/model. ( A ) The left structure is the monomeric Smr domain of H. sapiens B3bp (B3bp-Smr), and the right model is the predicted monomeric Smr domain of TmMutS2 (TmS2-Smr). ( B ) Superimpositions of the TmMutS2-dsDNA/-FWJ-DNA SAXS model to the B3bp-Smr structure and the TmS2-Smr model. ( C ) Superimpositions of the TmMutS2-dsDNA/-FWJ-DNA SAXS model to the B3bp-exSmr SAXS model (green mesh). The B3bp-Smr structure (red) fits well with the B3bp-exSmr SAXS model.

    Article Snippet: For further purification, each protein was individually applied to a Heparin HitrapTM HP (TmMutS2, TmMutL, and TmRecA) and a Mono S (B3bp-Smr) ion exchange column (GE Healthcare, Denmark) equilibrated with buffer II (50 mM Hepes-NaOH, pH 7.5, 100 mM NaCl, 1 mM dithiothreitol (DTT), 5 mM MgCl2 , 0.5 mM ethylenediaminetetraacetic acid (EDTA), and 5% glycerol).

    Techniques: