Advanced purification platform using circularly permuted caspase‐2 for affinity fusion‐tag removal to produce native fibroblast growth factor 2-Reference-Cited by-同舟云学术

Advanced purification platform using circularly permuted caspase‐2 for affinity fusion‐tag removal to produce native fibroblast growth factor 2

Published:2021-01-27 Issue:6 Volume:96 Page:1515-1522
ISSN:0268-2575
Container-title:Journal of Chemical Technology & Biotechnology
language:en
Short-container-title:J Chem Technol Biotechnol

Author:

Lingg Nico¹²^ORCID,Cserjan‐Puschmann Monika¹²,Fischer Andreas¹,Engele Petra¹³,Kröß Christina¹³,Schneider Rainer¹³,Brocard Cécile⁴,Berkemeyer Matthias⁴,Striedner Gerald¹²^ORCID,Jungbauer Alois¹²^ORCID

Affiliation:

1. Austrian Centre of Industrial Biotechnology Vienna Austria

2. Department of Biotechnology University of Natural Resources and Life Sciences Vienna Austria

3. Institute of Biochemistry Center for Molecular Biosciences Innsbruck (CMBI), University of Innsbruck Innsbruck Austria

4. Biopharma Process Science Austria Boehringer Ingelheim RCV GmbH & Co KG Vienna Austria

Funder

Österreichische Forschungsförderungsgesellschaft

Standortagentur Tirol

Publisher

Wiley

Subject

Inorganic Chemistry,Organic Chemistry,Pollution,Waste Management and Disposal,Fuel Technology,Renewable Energy, Sustainability and the Environment,General Chemical Engineering,Biotechnology

Link

https://onlinelibrary.wiley.com/doi/pdf/10.1002/jctb.6666

Reference28 articles.

1. Design of peptide ligands for affinity purification of human growth hormone

2. Inteins as tools for tagless and traceless protein purification

3. An overview of enzymatic reagents for the removal of affinity tags

4. Current strategies for the use of affinity tags and tag removal for the purification of recombinant proteins

5. Histidine affinity tags affect MSP142 structural stability and immunodominance in mice

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