![Purification of recombinant DGAT1 from E. coli with Ni-NTA and amylose... | Download Scientific Diagram Purification of recombinant DGAT1 from E. coli with Ni-NTA and amylose... | Download Scientific Diagram](https://www.researchgate.net/publication/51482880/figure/fig5/AS:202696624742409@1425338049434/Purification-of-recombinant-DGAT1-from-E-coli-with-Ni-NTA-and-amylose-resin-affinity.png)
Purification of recombinant DGAT1 from E. coli with Ni-NTA and amylose... | Download Scientific Diagram
![Purification of hetero-oligomeric protein variants using a modified tandem affinity purification approach - ScienceDirect Purification of hetero-oligomeric protein variants using a modified tandem affinity purification approach - ScienceDirect](https://ars.els-cdn.com/content/image/1-s2.0-S2666166722009157-fx1.jpg)
Purification of hetero-oligomeric protein variants using a modified tandem affinity purification approach - ScienceDirect
![Challenges and opportunities in the purification of recombinant tagged proteins. - Abstract - Europe PMC Challenges and opportunities in the purification of recombinant tagged proteins. - Abstract - Europe PMC](https://europepmc.org/articles/PMC7125906/bin/gr2.jpg)
Challenges and opportunities in the purification of recombinant tagged proteins. - Abstract - Europe PMC
![Expression and Purification of Maltose‐Binding Protein Fusions - Riggs - 1994 - Current Protocols in Molecular Biology - Wiley Online Library Expression and Purification of Maltose‐Binding Protein Fusions - Riggs - 1994 - Current Protocols in Molecular Biology - Wiley Online Library](https://currentprotocols.onlinelibrary.wiley.com/cms/asset/d292a1be-b3ee-4e66-ad1b-0968a4ec4196/cpmb1606-fig-0002-m.jpg)
Expression and Purification of Maltose‐Binding Protein Fusions - Riggs - 1994 - Current Protocols in Molecular Biology - Wiley Online Library
![Presence and removal of a contaminating NADH oxidation activity in recombinant maltose-binding protein fusion proteins expressed in Escherichia coli | BioTechniques Presence and removal of a contaminating NADH oxidation activity in recombinant maltose-binding protein fusion proteins expressed in Escherichia coli | BioTechniques](https://www.future-science.com/cms/10.2144/0000113822/asset/images/medium/figure1.gif)
Presence and removal of a contaminating NADH oxidation activity in recombinant maltose-binding protein fusion proteins expressed in Escherichia coli | BioTechniques
![Protein and antibody purification followed by immunoprecipitation of MYB and GATA zinc finger-type maize proteins with magnetic beads - ScienceDirect Protein and antibody purification followed by immunoprecipitation of MYB and GATA zinc finger-type maize proteins with magnetic beads - ScienceDirect](https://ars.els-cdn.com/content/image/1-s2.0-S266616672200329X-fx1.jpg)
Protein and antibody purification followed by immunoprecipitation of MYB and GATA zinc finger-type maize proteins with magnetic beads - ScienceDirect
![6 Outline of an MBP-based pull-down assay. The procedure on the left... | Download Scientific Diagram 6 Outline of an MBP-based pull-down assay. The procedure on the left... | Download Scientific Diagram](https://www.researchgate.net/publication/358125891/figure/fig4/AS:1171839426543618@1656399699689/Outline-of-an-MBP-based-pull-down-assay-The-procedure-on-the-left-shows-the-control.png)
6 Outline of an MBP-based pull-down assay. The procedure on the left... | Download Scientific Diagram
![Highly efficient soluble expression, purification and characterization of recombinant Aβ42 from Escherichia coli - RSC Advances (RSC Publishing) DOI:10.1039/C8RA00042E Highly efficient soluble expression, purification and characterization of recombinant Aβ42 from Escherichia coli - RSC Advances (RSC Publishing) DOI:10.1039/C8RA00042E](https://pubs.rsc.org/image/article/2018/RA/c8ra00042e/c8ra00042e-f2_hi-res.gif)
Highly efficient soluble expression, purification and characterization of recombinant Aβ42 from Escherichia coli - RSC Advances (RSC Publishing) DOI:10.1039/C8RA00042E
![One-step affinity purification of fusion proteins with optimal monodispersity and biological activity: application to aggregation-prone HPV E6 proteins | Microbial Cell Factories | Full Text One-step affinity purification of fusion proteins with optimal monodispersity and biological activity: application to aggregation-prone HPV E6 proteins | Microbial Cell Factories | Full Text](https://media.springernature.com/m685/springer-static/image/art%3A10.1186%2Fs12934-018-1039-z/MediaObjects/12934_2018_1039_Fig1_HTML.png)
One-step affinity purification of fusion proteins with optimal monodispersity and biological activity: application to aggregation-prone HPV E6 proteins | Microbial Cell Factories | Full Text
![A designed fusion tag for soluble expression and selective separation of extracellular domains of fibroblast growth factor receptors | Scientific Reports A designed fusion tag for soluble expression and selective separation of extracellular domains of fibroblast growth factor receptors | Scientific Reports](https://media.springernature.com/full/springer-static/image/art%3A10.1038%2Fs41598-021-01029-4/MediaObjects/41598_2021_1029_Fig1_HTML.png)
A designed fusion tag for soluble expression and selective separation of extracellular domains of fibroblast growth factor receptors | Scientific Reports
![Construction of redesigned pMAL expression vector for easy and fast purification of active native antimicrobial peptides | bioRxiv Construction of redesigned pMAL expression vector for easy and fast purification of active native antimicrobial peptides | bioRxiv](https://www.biorxiv.org/content/biorxiv/early/2021/05/26/2021.05.26.445771/F4.large.jpg)
Construction of redesigned pMAL expression vector for easy and fast purification of active native antimicrobial peptides | bioRxiv
![MPs | Free Full-Text | A Cost-Effective Immobilization Method for MBP Fusion Proteins on Microtiter Plates Using a Gelatinized Starch–Agarose Mixture and Its Application for Convenient Protein–Protein Interaction Analysis MPs | Free Full-Text | A Cost-Effective Immobilization Method for MBP Fusion Proteins on Microtiter Plates Using a Gelatinized Starch–Agarose Mixture and Its Application for Convenient Protein–Protein Interaction Analysis](https://pub.mdpi-res.com/mps/mps-06-00044/article_deploy/html/images/mps-06-00044-ag-550.jpg?1682322678)
MPs | Free Full-Text | A Cost-Effective Immobilization Method for MBP Fusion Proteins on Microtiter Plates Using a Gelatinized Starch–Agarose Mixture and Its Application for Convenient Protein–Protein Interaction Analysis
![An efficient method for FITC labelling of proteins using tandem affinity purification. - Abstract - Europe PMC An efficient method for FITC labelling of proteins using tandem affinity purification. - Abstract - Europe PMC](https://europepmc.org/articles/PMC6294648/bin/bsr-38-bsr20181764-g2.jpg)
An efficient method for FITC labelling of proteins using tandem affinity purification. - Abstract - Europe PMC
![Recombinant protein expression and purification: A comprehensive review of affinity tags and microbial applications - Young - 2012 - Biotechnology Journal - Wiley Online Library Recombinant protein expression and purification: A comprehensive review of affinity tags and microbial applications - Young - 2012 - Biotechnology Journal - Wiley Online Library](https://onlinelibrary.wiley.com/cms/asset/6a755c46-a6a9-450b-af7d-d6c89a7b9c59/mfig001.jpg)