Traditionally, protein interactions have been identified using a variety of methods including; yeast two hybrid screens (Y2H), co-immunoprecipitation (CoIP) using antibodies against endogenous proteins or epitope tags, and the use of affinity tags .
The study of intracellular protein interactions have been challenged with the ability to efficiently capture and preserve protein complexes, especially when attempting to isolate weak or transient interactions. To overcome these challenges, the HaloTag® Mammalian Pull-Down and Labeling System was developed. The system takes advantage of the properties of the HaloTag® fusion protein which forms a highly specific and covalent bond with the HaloLink™ Resin, allowing rapid and efficient capture of dilute protein complexes directly from mammalian cellular lysates (Figure 1).
The rapid binding along with the low non-specific binding properties of the HaloLink™ Resin improve the rate of successful complex capture and identification of binary and higher order macromolecular protein complexes.
The system also includes a fluorescent HaloTag® ligand which allows both detection as well as the ability to perform complementary live cells imaging studies of the same HaloTag® fusion protein.
Additional information regarding this new system can be found on the Promega web site.
Latest posts by Gary Kobs (see all)
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