Article

Production and comprehensive quality control of recombinant human Interleukin-1beta: a case study for a process development strategy.

QIAGEN GmbH, Qiagen Strasse 1, 40724 Hilden, Germany.
Protein Expression and Purification (impact factor: 1.59). 03/2008; 57(2):244-54. DOI:10.1016/j.pep.2007.09.019
Source: PubMed

ABSTRACT We describe an efficient strategy to produce high-quality proteins by using a single large IMAC chromatography column and enzymatic His-tag removal via the TAGZyme system in pilot scale. Numerous quality assays demonstrated a high purity of the final product, the human cytokine Interleukin-1beta (IL-1beta). The protein preparation was apparently free of host cell proteins, endotoxins, protease, and aggregates. The N-terminal amino acid sequence of IL-1beta was in full agreement with the natural mature form of IL-1beta. The homogeneity of the product was further shown by X-ray structure determination which confirmed the previously solved structure of the protein. We propose the applied workflow as a strategy for industrial production of protein-based biopharmaceuticals.

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Keywords

applied workflow
 
efficient strategy
 
enzymatic His-tag removal
 
full agreement
 
high-quality proteins
 
homogeneity
 
host cell proteins
 
human cytokine Interleukin-1beta
 
industrial production
 
N-terminal amino acid sequence
 
Numerous quality assays
 
protein preparation
 
purity
 
single large IMAC chromatography column
 
TAGZyme system
 
X-ray structure determination