![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
![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/figure2.gif)
Presence and removal of a contaminating NADH oxidation activity in recombinant maltose-binding protein fusion proteins expressed in Escherichia coli | BioTechniques
![MS2-MBP-Based Affinity Purification of Nucleus- or Cytoplasm-Localized lncRNA–Protein Complexes Formed In Vivo | SpringerLink MS2-MBP-Based Affinity Purification of Nucleus- or Cytoplasm-Localized lncRNA–Protein Complexes Formed In Vivo | SpringerLink](https://media.springernature.com/lw685/springer-static/image/chp%3A10.1007%2F978-1-0716-3191-1_17/MediaObjects/500891_2_En_17_Fig1_HTML.png)
MS2-MBP-Based Affinity Purification of Nucleus- or Cytoplasm-Localized lncRNA–Protein Complexes Formed In Vivo | SpringerLink
![A versatile new ubiquitin detection and purification tool derived from a bacterial deubiquitylase | bioRxiv A versatile new ubiquitin detection and purification tool derived from a bacterial deubiquitylase | bioRxiv](https://www.biorxiv.org/content/biorxiv/early/2021/12/02/2021.12.02.470885/F2.large.jpg)
A versatile new ubiquitin detection and purification tool derived from a bacterial deubiquitylase | bioRxiv
![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
![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
![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
![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
![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_Fig4_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
![Purification strategy for the ubiquitylated proteins. The main steps... | Download Scientific Diagram Purification strategy for the ubiquitylated proteins. The main steps... | Download Scientific Diagram](https://www.researchgate.net/publication/327812630/figure/fig2/AS:712776943161346@1546950674443/Purification-strategy-for-the-ubiquitylated-proteins-The-main-steps-along-the.png)
Purification strategy for the ubiquitylated proteins. The main steps... | Download Scientific Diagram
![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
![Purification of P5βR2 by amylose resin column chromatography. Soluble... | Download Scientific Diagram Purification of P5βR2 by amylose resin column chromatography. Soluble... | Download Scientific Diagram](https://www.researchgate.net/publication/236076977/figure/fig2/AS:214048642736144@1428044581400/Purification-of-P5bR2-by-amylose-resin-column-chromatography-Soluble-protein-isolated.png)
Purification of P5βR2 by amylose resin column chromatography. Soluble... | Download Scientific Diagram
![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
![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_Fig7_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
![Magnetic nanoparticles for the affinity adsorption of maltose binding protein (MBP) fusion enzymes - Journal of Materials Chemistry (RSC Publishing) DOI:10.1039/C2JM16778F Magnetic nanoparticles for the affinity adsorption of maltose binding protein (MBP) fusion enzymes - Journal of Materials Chemistry (RSC Publishing) DOI:10.1039/C2JM16778F](https://pubs.rsc.org/image/article/2012/JM/c2jm16778f/c2jm16778f-s2.gif)
Magnetic nanoparticles for the affinity adsorption of maltose binding protein (MBP) fusion enzymes - Journal of Materials Chemistry (RSC Publishing) DOI:10.1039/C2JM16778F
![Frontiers | Fusion tags for protein solubility, purification and immunogenicity in Escherichia coli: the novel Fh8 system Frontiers | Fusion tags for protein solubility, purification and immunogenicity in Escherichia coli: the novel Fh8 system](https://www.frontiersin.org/files/Articles/77021/fmicb-05-00063-HTML/image_m/fmicb-05-00063-g003.jpg)