ArticlePloS one2021
A highly efficient method for the production and purification of recombinant human CXCL8.
Article in PloS one, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.
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Who cites it
6 citing papers in PubMed, 7 citations in OpenAlex.
- SpyCEP dismantles neutrophil immunity via disorder-driven chemokine remodeling and GAG targeting.Proceedings of the National Academy of Sciences of the United States of America · 2026Article
- The Small Ubiquitin-Like Modifier SUMO-3 Acts as a Neutrophil Chemoattractant via the Chemokine Receptors CXCR1 and CXCR2.Journal of innate immunity · 2026Article
- Beyond Purification: Evolving Roles of Fusion Tags in Biotechnology.Current issues in molecular biology · 2025Review
- The N-terminal ELRThe Journal of biological chemistry · 2025Article
- New insight into a simple high-yielding method for the production of fully folded and functional recombinant human CCL5.Scientific reports · 2024Article
- CXCL17 binds efficaciously to glycosaminoglycans with the potential to modulate chemokine signaling.Frontiers in immunology · 2023Article
Corrections and comments
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Authors and funding
6 authors at 1 institution in 1 country.
Funding
Abstract
Chemokines play diverse and fundamental roles in the immune system and human disease, which has prompted their structural and functional characterisation. Production of recombinant chemokines that are folded and bioactive is vital to their study but is limited by the stringent requirements of a native N-terminus for receptor activation and correct disulphide bonding required to stabilise the chemokine fold. Even when expressed as fusion proteins, overexpression of chemokines in E. coli tends to result in the formation of inclusion bodies, generating the additional steps of solubilisation and refolding. Here we present a novel method for producing soluble chemokines in relatively large amounts via a simple two-step purification procedure with no requirements for refolding. CXCL8 produced by this method has the correct chemokine fold as determined by NMR spectroscopy and in chemotaxis assays was indistinguishable from commercially available chemokines. We believe that this protocol significantly streamlines the generation of recombinant chemokines.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.