Efficient Isolation, Identification of Intracellular Protein Complexes: HaloTag® Mammalian Pull-Down and Labeling System

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 HaloTag® Mammalian Pull-Down System.

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.

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Gary Kobs

Strategic Marketing Manager at Promega Corporation
Gary earned his B.S. in Bacteriology, UW-Madison in 1982. From 1982–1986 he served as Research Tech at UW-Madison. From 1986 to the present Gary has been with Promega Corporation serving in many capacities including as the very first editor of Promega Notes. He was also Manager Tech Services and Training, Product Manager Restriction/Modifying Enzymes, Product Manager Protein Analysis, and is now Marketing Manager Protein Analysis.

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