Proteomics is critically dependent on optimal sample preparation. Particularly, the interface
between protein digestion and mass spectrometric analysis has a large influence on the …

Detergents are commonly used in protein–chemistry protocols and may be necessary for
protein extraction, solubilization, and denaturation; however, their presence interferes with …

The relative quantification of protein expression levels in different cell samples through the
utilization of stable isotope dilution has become a standard method in the field of proteomics …

Immobilized metal affinity chromatography (IMAC) is a technique primarily used in research
and development laboratories to purify proteins containing engineered histidine tags …

His‐tag affinity purification is one of the most commonly used methods to purify recombinant
proteins expressed in E. coli. One drawback of using the His‐tag is the co‐purification of …

A tag comprising four to six histidines genetically fused to the protein of interest (His-tag) has
been widely used to purify proteins by immobilized metal-ion affinity chromatography …

In the drug-discovery setting, the development of new peptide and protein-based
biopharmaceuticals attracts increased attention from the pharmaceutical industry and …

We have developed a generic procedure to purify proteins expressed at their natural level
under native conditions using a novel tandem affinity purification (TAP) tag. The TAP tag …

Since the dawn of time, or at least the dawn of recombinant DNA technology (which for many
of today's scientists is the same thing), investigators have been cloning and expressing …

Ni-NTA affinity purification of His-tagged proteins is a bind-wash-elute procedure that can be
performed under native or denaturing conditions. Here, protocols for purification of His …