ArticlePolymers2018
Column-Free Purification Methods for Recombinant Proteins Using Self-Cleaving Aggregating Tags.
Article in Polymers, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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Who cites it
10 citing papers in PubMed, 39 citations in OpenAlex.
- Recombinant production of acidophilic L-arabinose isomerase from Lentilactobacillus parakefiri in Bacillus subtilis.Microbial cell factories · 2025Article
- Beyond Purification: Evolving Roles of Fusion Tags in Biotechnology.Current issues in molecular biology · 2025Review
- Enhancing recombinant growth factor and serum protein production for cultivated meat manufacturing.Microbial cell factories · 2025Review
- Highly selective split intein method for efficient separation and purification of recombinant therapeutic proteins from mammalian cell culture fluid.Journal of chromatography. A · 2024Article
- A Convenient Self-Removing Affinity Tag Method for the Simple Purification of Tagless Recombinant Proteins.Current protocols · 2023Article
- Transposase-CRISPR mediated targeted integration (TransCRISTI) in the human genome.Scientific reports · 2022Article
- The Evolution of Intein-Based Affinity Methods as Reflected in 30 years of Patent History.Frontiers in molecular biosciences · 2022Review
- The Inducible Intein-Mediated Self-Cleaving Tag (IIST) System: A Novel Purification and Amidation System for Peptides and Proteins.Molecules (Basel, Switzerland) · 2021Article
- mem-iLID, a fast and economic protein purification method.Bioscience reports · 2021Article
- Column-free purification and coating of SpyCatcher protein on ELISA wells generates universal solid support for capturing of SpyTag-fusion protein from the non-purified condition.Protein expression and purification · 2020Article
Corrections and comments
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Authors and funding
5 authors at 1 institution in 1 country.
Funding
Abstract
Conventional column chromatography processes to purify recombinant proteins are associated with high production costs and slow volumetric throughput at both laboratory and large scale. Non-chromatographic purifications based on selective aggregating tags have the potential to reduce costs with acceptable protein yields. A significant drawback, however, is that current proteolytic approaches for post-purification tag removal after are expensive and non-scalable. To address this problem, we have developed two non-chromatographic purification strategies that use either the elastin-like polypeptide (ELP) tag or the β-roll tag (BRT17) in combination with an engineered split intein for tag removal. The use of the split intein eliminates premature cleavage during expression and provides controlled cleavage under mild conditions after purification. These self-cleaving aggregating tags were used to efficiently purify β-lactamase (β-lac), super-folder green fluorescent protein (sfGFP), streptokinase (SK) and maltose binding protein (MBP), resulting in increased yields compared to previous ELP and BRT17-based methods. Observed yields of purified targets for both systems typically ranged from approximately 200 to 300 micrograms per milliliter of cell culture, while overall recoveries ranged from 10 to 85 percent and were highly dependent on the target protein.
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Registered trials
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