ArticleNature communications2019
The ALFA-tag is a highly versatile tool for nanobody-based bioscience applications.
Article in Nature communications, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 393 papers.
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Who cites it
393 citing papers in PubMed.
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- Self-Blinking Dye Restores Efficient Use of Nanobodies in Single-Molecule Localization Microscopy.Nano letters · 2026Article
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- Quantitative comparison of methodologies for translation site imaging in living cells.RNA (New York, N.Y.) · 2026Article
- GPLD1 is a scavenger carrier mediating lysosomal degradation of extracellular aberrant proteins.Life science alliance · 2026Article
- Lysine deficiency within a conserved lysine desert is critical for EEL-1/HUWE1 to support ubiquitin proteasome system function.PLoS genetics · 2026Article
- Engineering viral protease-operated nanobodies for programmable and orthogonal control of protein function.Nature communications · 2026Article
- Bacterial surface display enables lysis-independent joint host-pathogen single-cell profiling.bioRxiv : the preprint server for biology · 2026Article
- Thousandfold Expansion Microscopy.bioRxiv : the preprint server for biology · 2026Article
333 more citing papers are in PubMed but not listed here.
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Authors and funding
11 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Specialized epitope tags are widely used for detecting, manipulating or purifying proteins, but often their versatility is limited. Here, we introduce the ALFA-tag, a rationally designed epitope tag that serves a remarkably broad spectrum of applications in life sciences while outperforming established tags like the HA-, FLAG®- or myc-tag. The ALFA-tag forms a small and stable α-helix that is functional irrespective of its position on the target protein in prokaryotic and eukaryotic hosts. We characterize a nanobody (NbALFA) binding ALFA-tagged proteins from native or fixed specimen with low picomolar affinity. It is ideally suited for super-resolution microscopy, immunoprecipitations and Western blotting, and also allows in vivo detection of proteins. We show the crystal structure of the complex that enabled us to design a nanobody mutant (NbALFA
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