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strep affinity protein purification  (IBA Lifesciences)


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    IBA Lifesciences strep affinity protein purification
    <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 286 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/product/strep+affinity+protein+purification/Strep-Tactin+XT+4Flow+resin/pmc12558382-65-5-12
    Average 96 stars, based on 286 article reviews
    strep affinity protein purification - by Bioz Stars, 2026-09
    96/100 stars

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    1) Product Images from "Plastic-binding peptides as anchors for protein scaffolds on synthetic plastics: opportunities and challenges"

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

    Journal: RSC Advances

    doi: 10.1039/d5ra06185g

    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.
    Figure Legend 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.

    Techniques Used: Purification, Control, Construct, Incubation

    Related Articles

    Protein Purification:

    Article Title: Plastic-binding peptides as anchors for protein scaffolds on synthetic plastics: opportunities and challenges
    Article Snippet: Restriction enzymes, DNA polymerase, and other enzymes and reagents for cloning were purchased from New England Biolabs and Thermo Fischer Scientific, USA. .. Strep-Tactin®XT 4Flow® resin (2-5010-025) for strep affinity protein purification was purchased from IBA lifesciences. .. HisPurTM Ni-NTA Resin (88222) from Thermo Fischer was used for Ni 2+ affinity purification of recombinant proteins.



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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.
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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