Site-specific protein cleavage is essential for many protein-production protocols and
typically requires proteases. We report the development of a chemical protein-cleavage …

The peptide sequence NDKTHC was previously investigated as a site for efficient, specific
cleavage of a fusion protein by cupric ions using a humanized γ1 Fab′ as a model protein …

Today, proteins are typically overexpressed using solubility-enhancing fusion tags that allow
for affinity chromatographic purification and subsequent removal by site-specific protease …

The peptide sequence NDKTHC was investigated as a site for efficient, specific cleavage of
a fusion protein by cupric ions using a humanised γ1 Fab′ as a model protein. The native …

Fusion expression is a common practice for recombinant protein production. Some fusion
tags confer solubility on the target protein whereas others provide affinity handles that …

Protein purification typically involves expressing a recombinant gene comprising a target
protein fused to a suitable affinity tag. After purification, it is often desirable to remove the …

The present purification protocol applies to target proteins that are fused to a double tag,
such as NusA–His6, through a linker that includes a protease-recognition sequence. It …

Where an affinity tag has served its purpose it may become desirable to remove it from the
protein of interest. This chapter describes the removal of such fusion partners from the …

The total synthesis of long proteins requires the assembly of multiple fragments through
successive ligations. The need for intermediate purification steps is a strong limitation …

High-throughput protein expression and purification has a central, pivotal role in structural
genomics. In fact, crystallographic-quality protein production on the scale required to …