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 …

A novel protein purification system has been developed which enables purification of free
recombinant proteins in a single chromatographic step. The system utilizes a modified …

We describe a new affinity purification tag called Car9 that confers proteins to which it is
fused micromolar affinity for unmodified silica. When appended to the C‐terminus of …

Current non-gel techniques for analyzing proteomes rely heavily on mass spectrometric
analysis of enzymatically digested protein mixtures. Prior to analysis, a highly complex …

Proteins with N-terminal cysteine can undergo native chemical ligation and are useful for
site-specific N-terminal labeling or protein semisynthesis. Recombinant production of these …

Protein ligases of defined substrate specificity are versatile tools for protein engineering.
Upon completion of the reaction, the products of currently reported protein ligases contain …

In recent years, there has been an explosion of interest in protein-assembly technologies
such as native chemical ligation (NCL)[1] and expressed protein ligation (EPL).[2] NCL …

Molecular biology has been revolutionized by the miniaturization and parallelization of DNA
sequencing assays previously performed on bulk samples. Many of these technologies rely …

The use of affinity tags to purify recombinant proteins is ubiquitous in molecular biology.
However, tag removal after purification still remains a challenge. The most commonly used …

To understand gene function, the encoding DNA or mRNA transcript can be manipulated
and the consequences observed. However, these approaches do not have a direct effect on …