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 …

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 …

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

This unit provides protocols for some commonly used methods of site‐specific cleavage of
fusion proteins. The first three protocols describe enzymatic cleavage of proteins using …

Improved ways to cleave peptide chains at engineered sites easily and specifically would
form useful tools for biochemical research. Uses of such methods include the activation or …

Addition of an N‐terminal fusion partner can greatly aid the expression and purification of a
recombinant protein in Escherichia coli. We investigated two genetically engineered …

Fusion of proteins to the Fc region of IgG is widely used to express cellular receptors and
other extracellular proteins, but cleavage of the fusion partner is sometimes required for …

In the affinity purification of recombinant fusion proteins, the rate-limiting step is usually the
efficient proteolytic cleavage and removal of the affinity tail and the protease from the …

It is documented that the tobacco etch virus protease (TEVp) variant TEVp 3M is less efficient
in cleaving the fusion protein bound to Ni-NTA resin at relatively low temperature. Here, we …