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protein a purification  (Gold Biotechnology Inc)
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Gold Biotechnology Inc protein a purification
Protein A Purification, supplied by Gold Biotechnology Inc, used in various techniques. Bioz Stars score: 95/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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strep affinity protein purification  (IBA Lifesciences)
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<t>Purification</t> and assembly of a synthetic cohesin–dockerin scaffold complex. (A) The molecular design of all fusion proteins used for the development of the plastic-targeting complex. A plastic-targeting complex was designed using three cohesins from cellulosomal proteins (CipC, CipA, OlpB) and fused to LCIM3 on both termini. A control scaffold lacking LCIM3 was also constructed. Dockerins from Cel5A, Cel48S, and CipA were fused to distinct fluorophores via native linkers. Scaffold constructs carried an N-terminal Strep II tag; dockerin fusions had a C-terminal 6×His tag. (B) Assembly of the dockerin–cohesin complex was validated by pull-down experiments targeting the scaffold backbone using MagStrep® Strep-Tactin® XT beads. Lanes to the left of the dotted line show the purified protein fusions used for complex assembly. Lanes to the right of the dotted line represent pull-down results. The first four lanes on the right demonstrate that only the scaffold binds to the Strep-Tactin XT beads when each protein is incubated individually. When all four proteins are incubated together, the fluorophore–dockerin fusions co-elute with the scaffold (elute lane) in the Strep-Tactin XT pull-down.
Strep Affinity Protein Purification, supplied by IBA Lifesciences, 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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strep affinity protein purification - by Bioz Stars, 2026-04
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protein g resin purification kit  (GenScript corporation)
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<t>Purification</t> and assembly of a synthetic cohesin–dockerin scaffold complex. (A) The molecular design of all fusion proteins used for the development of the plastic-targeting complex. A plastic-targeting complex was designed using three cohesins from cellulosomal proteins (CipC, CipA, OlpB) and fused to LCIM3 on both termini. A control scaffold lacking LCIM3 was also constructed. Dockerins from Cel5A, Cel48S, and CipA were fused to distinct fluorophores via native linkers. Scaffold constructs carried an N-terminal Strep II tag; dockerin fusions had a C-terminal 6×His tag. (B) Assembly of the dockerin–cohesin complex was validated by pull-down experiments targeting the scaffold backbone using MagStrep® Strep-Tactin® XT beads. Lanes to the left of the dotted line show the purified protein fusions used for complex assembly. Lanes to the right of the dotted line represent pull-down results. The first four lanes on the right demonstrate that only the scaffold binds to the Strep-Tactin XT beads when each protein is incubated individually. When all four proteins are incubated together, the fluorophore–dockerin fusions co-elute with the scaffold (elute lane) in the Strep-Tactin XT pull-down.
Protein G Resin Purification Kit, 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
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glutathione sepharose 4b gst-tagged protein purification resin  (Danaher Inc)
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<t>Purification</t> and assembly of a synthetic cohesin–dockerin scaffold complex. (A) The molecular design of all fusion proteins used for the development of the plastic-targeting complex. A plastic-targeting complex was designed using three cohesins from cellulosomal proteins (CipC, CipA, OlpB) and fused to LCIM3 on both termini. A control scaffold lacking LCIM3 was also constructed. Dockerins from Cel5A, Cel48S, and CipA were fused to distinct fluorophores via native linkers. Scaffold constructs carried an N-terminal Strep II tag; dockerin fusions had a C-terminal 6×His tag. (B) Assembly of the dockerin–cohesin complex was validated by pull-down experiments targeting the scaffold backbone using MagStrep® Strep-Tactin® XT beads. Lanes to the left of the dotted line show the purified protein fusions used for complex assembly. Lanes to the right of the dotted line represent pull-down results. The first four lanes on the right demonstrate that only the scaffold binds to the Strep-Tactin XT beads when each protein is incubated individually. When all four proteins are incubated together, the fluorophore–dockerin fusions co-elute with the scaffold (elute lane) in the Strep-Tactin XT pull-down.
Glutathione Sepharose 4b Gst Tagged Protein Purification Resin, supplied by Danaher Inc, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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hislink tm protein purification resin  (Promega)
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Promega hislink tm protein purification resin
<t>Purification</t> and assembly of a synthetic cohesin–dockerin scaffold complex. (A) The molecular design of all fusion proteins used for the development of the plastic-targeting complex. A plastic-targeting complex was designed using three cohesins from cellulosomal proteins (CipC, CipA, OlpB) and fused to LCIM3 on both termini. A control scaffold lacking LCIM3 was also constructed. Dockerins from Cel5A, Cel48S, and CipA were fused to distinct fluorophores via native linkers. Scaffold constructs carried an N-terminal Strep II tag; dockerin fusions had a C-terminal 6×His tag. (B) Assembly of the dockerin–cohesin complex was validated by pull-down experiments targeting the scaffold backbone using MagStrep® Strep-Tactin® XT beads. Lanes to the left of the dotted line show the purified protein fusions used for complex assembly. Lanes to the right of the dotted line represent pull-down results. The first four lanes on the right demonstrate that only the scaffold binds to the Strep-Tactin XT beads when each protein is incubated individually. When all four proteins are incubated together, the fluorophore–dockerin fusions co-elute with the scaffold (elute lane) in the Strep-Tactin XT pull-down.
Hislink Tm Protein Purification Resin, supplied by Promega, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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hislink tm protein purification resin - by Bioz Stars, 2026-04
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protein a 472 purification  (Gold Biotechnology Inc)
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<t>Purification</t> and assembly of a synthetic cohesin–dockerin scaffold complex. (A) The molecular design of all fusion proteins used for the development of the plastic-targeting complex. A plastic-targeting complex was designed using three cohesins from cellulosomal proteins (CipC, CipA, OlpB) and fused to LCIM3 on both termini. A control scaffold lacking LCIM3 was also constructed. Dockerins from Cel5A, Cel48S, and CipA were fused to distinct fluorophores via native linkers. Scaffold constructs carried an N-terminal Strep II tag; dockerin fusions had a C-terminal 6×His tag. (B) Assembly of the dockerin–cohesin complex was validated by pull-down experiments targeting the scaffold backbone using MagStrep® Strep-Tactin® XT beads. Lanes to the left of the dotted line show the purified protein fusions used for complex assembly. Lanes to the right of the dotted line represent pull-down results. The first four lanes on the right demonstrate that only the scaffold binds to the Strep-Tactin XT beads when each protein is incubated individually. When all four proteins are incubated together, the fluorophore–dockerin fusions co-elute with the scaffold (elute lane) in the Strep-Tactin XT pull-down.
Protein A 472 Purification, supplied by Gold Biotechnology Inc, used in various techniques. Bioz Stars score: 95/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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protein purification  (New England Biolabs)
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<t>Purification</t> and assembly of a synthetic cohesin–dockerin scaffold complex. (A) The molecular design of all fusion proteins used for the development of the plastic-targeting complex. A plastic-targeting complex was designed using three cohesins from cellulosomal proteins (CipC, CipA, OlpB) and fused to LCIM3 on both termini. A control scaffold lacking LCIM3 was also constructed. Dockerins from Cel5A, Cel48S, and CipA were fused to distinct fluorophores via native linkers. Scaffold constructs carried an N-terminal Strep II tag; dockerin fusions had a C-terminal 6×His tag. (B) Assembly of the dockerin–cohesin complex was validated by pull-down experiments targeting the scaffold backbone using MagStrep® Strep-Tactin® XT beads. Lanes to the left of the dotted line show the purified protein fusions used for complex assembly. Lanes to the right of the dotted line represent pull-down results. The first four lanes on the right demonstrate that only the scaffold binds to the Strep-Tactin XT beads when each protein is incubated individually. When all four proteins are incubated together, the fluorophore–dockerin fusions co-elute with the scaffold (elute lane) in the Strep-Tactin XT pull-down.
Protein Purification, supplied by New England Biolabs, 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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ni-ted 6ff (his-tag) protein agarose purification resin c610030–0025  (Sangon Biotech)
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Sangon Biotech ni-ted 6ff (his-tag) protein agarose purification resin c610030–0025
<t>Purification</t> and assembly of a synthetic cohesin–dockerin scaffold complex. (A) The molecular design of all fusion proteins used for the development of the plastic-targeting complex. A plastic-targeting complex was designed using three cohesins from cellulosomal proteins (CipC, CipA, OlpB) and fused to LCIM3 on both termini. A control scaffold lacking LCIM3 was also constructed. Dockerins from Cel5A, Cel48S, and CipA were fused to distinct fluorophores via native linkers. Scaffold constructs carried an N-terminal Strep II tag; dockerin fusions had a C-terminal 6×His tag. (B) Assembly of the dockerin–cohesin complex was validated by pull-down experiments targeting the scaffold backbone using MagStrep® Strep-Tactin® XT beads. Lanes to the left of the dotted line show the purified protein fusions used for complex assembly. Lanes to the right of the dotted line represent pull-down results. The first four lanes on the right demonstrate that only the scaffold binds to the Strep-Tactin XT beads when each protein is incubated individually. When all four proteins are incubated together, the fluorophore–dockerin fusions co-elute with the scaffold (elute lane) in the Strep-Tactin XT pull-down.
Ni Ted 6ff (His Tag) Protein Agarose Purification Resin C610030–0025, supplied by Sangon Biotech, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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his-tag protein purification kit (reductive chelating resin)  (Beyotime)
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Beyotime his-tag protein purification kit (reductive chelating resin)
<t>Purification</t> and assembly of a synthetic cohesin–dockerin scaffold complex. (A) The molecular design of all fusion proteins used for the development of the plastic-targeting complex. A plastic-targeting complex was designed using three cohesins from cellulosomal proteins (CipC, CipA, OlpB) and fused to LCIM3 on both termini. A control scaffold lacking LCIM3 was also constructed. Dockerins from Cel5A, Cel48S, and CipA were fused to distinct fluorophores via native linkers. Scaffold constructs carried an N-terminal Strep II tag; dockerin fusions had a C-terminal 6×His tag. (B) Assembly of the dockerin–cohesin complex was validated by pull-down experiments targeting the scaffold backbone using MagStrep® Strep-Tactin® XT beads. Lanes to the left of the dotted line show the purified protein fusions used for complex assembly. Lanes to the right of the dotted line represent pull-down results. The first four lanes on the right demonstrate that only the scaffold binds to the Strep-Tactin XT beads when each protein is incubated individually. When all four proteins are incubated together, the fluorophore–dockerin fusions co-elute with the scaffold (elute lane) in the Strep-Tactin XT pull-down.
His Tag Protein Purification Kit (Reductive Chelating Resin), supplied by Beyotime, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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his-tag protein purification kit (reductive chelating resin) - by Bioz Stars, 2026-04
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Purification and assembly of a synthetic cohesin–dockerin scaffold complex. (A) The molecular design of all fusion proteins used for the development of the plastic-targeting complex. A plastic-targeting complex was designed using three cohesins from cellulosomal proteins (CipC, CipA, OlpB) and fused to LCIM3 on both termini. A control scaffold lacking LCIM3 was also constructed. Dockerins from Cel5A, Cel48S, and CipA were fused to distinct fluorophores via native linkers. Scaffold constructs carried an N-terminal Strep II tag; dockerin fusions had a C-terminal 6×His tag. (B) Assembly of the dockerin–cohesin complex was validated by pull-down experiments targeting the scaffold backbone using MagStrep® Strep-Tactin® XT beads. Lanes to the left of the dotted line show the purified protein fusions used for complex assembly. Lanes to the right of the dotted line represent pull-down results. The first four lanes on the right demonstrate that only the scaffold binds to the Strep-Tactin XT beads when each protein is incubated individually. When all four proteins are incubated together, the fluorophore–dockerin fusions co-elute with the scaffold (elute lane) in the Strep-Tactin XT pull-down.

Journal: RSC Advances

Article Title: Plastic-binding peptides as anchors for protein scaffolds on synthetic plastics: opportunities and challenges

doi: 10.1039/d5ra06185g

Figure Lengend Snippet: Purification and assembly of a synthetic cohesin–dockerin scaffold complex. (A) The molecular design of all fusion proteins used for the development of the plastic-targeting complex. A plastic-targeting complex was designed using three cohesins from cellulosomal proteins (CipC, CipA, OlpB) and fused to LCIM3 on both termini. A control scaffold lacking LCIM3 was also constructed. Dockerins from Cel5A, Cel48S, and CipA were fused to distinct fluorophores via native linkers. Scaffold constructs carried an N-terminal Strep II tag; dockerin fusions had a C-terminal 6×His tag. (B) Assembly of the dockerin–cohesin complex was validated by pull-down experiments targeting the scaffold backbone using MagStrep® Strep-Tactin® XT beads. Lanes to the left of the dotted line show the purified protein fusions used for complex assembly. Lanes to the right of the dotted line represent pull-down results. The first four lanes on the right demonstrate that only the scaffold binds to the Strep-Tactin XT beads when each protein is incubated individually. When all four proteins are incubated together, the fluorophore–dockerin fusions co-elute with the scaffold (elute lane) in the Strep-Tactin XT pull-down.

Article Snippet: Strep-Tactin®XT 4Flow® resin (2-5010-025) for strep affinity protein purification was purchased from IBA lifesciences.

Techniques: Purification, Control, Construct, Incubation