ArticleApplied microbiology and biotechnology2024
Improved recombinant expression of soluble cathepsin B and L in Escherichia coli.
Article in Applied microbiology and biotechnology, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.
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Who cites it
3 citing papers in PubMed.
- Establishment of an Indirect ELISA Detection Method for Porcine Circovirus 3 Based on Soluble Cap Protein.Veterinary sciences · 2026Article
- Expression of Recombinant Hirudin in Bacteria and Yeast: A Comparative Approach.Methods and protocols · 2025Article
- Biochemical analyses of cystatin-C dimers and cathepsin-B reveals a trypsin-driven feedback mechanism in acute pancreatitis.Nature communications · 2025Article
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7 authors.
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Abstract
Cysteine cathepsins such as cathepsin B and L play an important role in numerous diseases like acute pancreatitis or SARS-CoV-2 and therefore have high potential for the development of new therapeutics. To be able to screen for potent and selective inhibitors sufficient amounts of protein are required. Here, we present an easy and efficient protocol for the recombinant expression of soluble and active murine cathepsin B and L. For this, we used the strain E. coli SHuffle® T7 Express which is capable of forming disulfide bridges in the cytoplasm. The enzymes were purified by immobilized nickel ion-affinity chromatography. Using different constructs and media, expression levels were significantly improved and expression yields of 80 ± 2 mg L
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