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

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.

journal_name

Protein Expr Purif

journal_title

Protein expression and purification

authors

Block H,Kubicek J,Labahn J,Roth U,Schäfer F

doi

10.1016/j.pep.2007.09.019

subject

Has Abstract

pub_date

2008-02-01 00:00:00

pages

244-54

issue

2

eissn

1046-5928

issn

1096-0279

pii

S1046-5928(07)00239-2

journal_volume

57

pub_type

杂志文章

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