An improved nonchromatographic method for the purification of recombinant proteins using elastin-like polypeptide-tagged proteases

Proteins fused to the elastin-like polypeptide (ELP) tag can be selectively separated from crude cell extract without chromatography. To avoid the interference of the ELP tag on properties of the target protein, it is necessary to remove the ELP tag from target protein by protease digestion. Therefo...

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Detalles Bibliográficos
Autores principales: Lan, Dongming, Huang, Guangrui, Shao, Hongwei, Zhang, Lichun, Ma, Lixin, Chen, Shangwu, Xu, Anlong
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Elsevier Inc. 2011
Materias:
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Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7094418/
https://www.ncbi.nlm.nih.gov/pubmed/21600185
http://dx.doi.org/10.1016/j.ab.2011.04.034
Descripción
Sumario:Proteins fused to the elastin-like polypeptide (ELP) tag can be selectively separated from crude cell extract without chromatography. To avoid the interference of the ELP tag on properties of the target protein, it is necessary to remove the ELP tag from target protein by protease digestion. Therefore, an additional chromatographic purification step is required to remove the proteases, and this is time- and labor-consuming. Here we demonstrate the utility of the ELP-tagged proteases for cleavage of ELP fusion proteins, allowing one-step removal of the cleaved ELP tag and ELP-tagged proteases without chromatography.

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