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Article summary:

1. A novel protein purification method has been developed that uses cell-surface display of SUMO-fused recombinant protein and Ulp1 protease.

2. This method is simple and rapid, requiring only cleavage and centrifugation steps.

3. The purified mCherry protein had a purity of over 80%, which could be further improved with ultrafiltration.

Article analysis:

The article is generally reliable in its presentation of the new protein purification method, providing detailed information on the process and results obtained from testing it with mCherry protein. The authors provide evidence for their claims, such as citing previous studies to support their use of SUMO-Ulp1 system for protein purification, as well as providing data on the purity of the purified mCherry protein. However, there are some potential biases in the article that should be noted. For example, while the authors cite previous studies to support their use of SUMO-Ulp1 system for protein purification, they do not explore any possible counterarguments or alternative methods that may be more effective or efficient than this one. Additionally, while they note that conventional purification approaches require complex manipulation steps and are costly, they do not provide any evidence to support this claim or compare their new method to these other approaches in terms of cost or efficiency. Furthermore, while they note that fusion with affinity tags can alter a protein's structure and affect its function, they do not explore any potential risks associated with using this new method or discuss how it may affect a target protein's structure or function. In conclusion, while this article provides an interesting approach to simplifying protein purification processes, it should be read critically in order to identify any potential biases or missing points of consideration before implementing this method in practice.