ArticleProtein expression and purification2006
Novel protein purification system utilizing an N-terminal fusion protein and a caspase-3 cleavable linker.
Article in Protein expression and purification, 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
9 citing papers in PubMed, 16 citations in OpenAlex.
- Production of autolysis-proof Kex2 protease from Candida albicans in Saccharomyces cerevisiae for in vitro processing of fusion proteins.Applied microbiology and biotechnology · 2022Article
- PROFICS: A bacterial selection system for directed evolution of proteases.The Journal of biological chemistry · 2021Article
- Production of Circularly Permuted Caspase-2 for Affinity Fusion-Tag Removal: Cloning, Expression inBiomolecules · 2020Article
- Fusion partners can increase the expression of recombinant interleukins via transient transfection in 2936E cells.Protein science : a publication of the Protein Society · 2010Article
- Robust production of a peptide library using methodological synchronization.Protein expression and purification · 2009Article
- Viral vectors for production of recombinant proteins in plants.Journal of cellular physiology · 2008Review
- Production of active eukaryotic proteins through bacterial expression systems: a review of the existing biotechnology strategies.Molecular and cellular biochemistry · 2008Review
- Rapid folding and unfolding of Apaf-1 CARD.Journal of molecular biology · 2007Article
- pC6-2/caspase-6 system to purify glutathione-S-transferase-free recombinant fusion proteins expressed in Escherichia coli.Nature protocols · 2006Article
Corrections and comments
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
Abstract
Coupled with over-expression in host organisms, fusion protein systems afford economical methods to obtain large quantities of target proteins in a fast and efficient manner. Some proteases used for these purposes cleave C-terminal to their recognition sequences and do not leave extra amino acids on the target. However, they are often inefficient and are frequently promiscuous, resulting in non-specific cleavages of the target protein. To address these issues, we created a fusion protein system that utilizes a highly efficient enzyme and leaves no residual amino acids on the target protein after removal of the affinity tag. We designed a glutathione S-transferase (GST)-fusion protein vector with a caspase-3 consensus cleavage sequence located between the N-terminal GST tag and a target protein. We show that the enzyme efficiently cleaves the fusion protein without leaving excess amino acids on the target protein. In addition, we used an engineered caspase-3 enzyme that is highly stable, has increased activity relative to the wild-type enzyme, and contains a poly-histidine tag that allows for efficient removal of the enzyme after cleavage of the fusion protein. Although we have developed this system using a GST tag, the system is amenable to any commercially available affinity tag.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.