HaloTag® Technology for Protein Purification, Protein Interactions and Imaging

HaloTag® technology is a powerful tool for functional protein analysis based on the formation of a covalent bond between the HaloTag® protein fusion tag and synthetic chemical ligands. By interchanging ligands, you can control the function and properties of the HaloTag® fusion protein, allowing use of the same construct for protein purification, protein interaction analysis, and cell-based assays for protein translocation, receptor internalization, and protein stability studies.

Available HaloTag® ligands include magnetic and non-magnetic beads, glass slides, cell-permeable and impermeable fluorescent ligands, biotin, and reactive ligands that allow you to build your own custom HaloTag® ligands and surfaces.

HaloTag® Products and Applications

  • E. coli-Based Protein Purification

    Efficiently capture proteins expressed in E. coli as HaloTag® fusions.

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  • Mammalian Cell-based Protein Purification

    Purify fusion proteins directly from mammalian cell culture lysates, even at low expression levels.

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  • Protein Localization, Trafficking and Turnover

    Perform multicolor live- and fixed-cell imaging experiments using a single genetic construct.

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  • Identification of Protein:Protein Interactions

    Capture and purify intracellular binary and higher order protein complexes, including transient or weakly interacting partners.

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  • Detection of Protein:DNA Interactions

    Capture intracellular protein:DNA complexes without using antibodies.

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  • HaloTag® Clones

    Choose from an extensive library of prebuilt HaloTag® human ORF clones.

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HaloTag® Technology in the Literature

Article

KDM4A Lysine Demethylase Induces Site-Specific Copy Gain and Rereplication of Regions Amplified in Tumors

Black, J. et al. (2013). Cell, 154 (3), 541-55.

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Article

HIF1A Employs CDK8-Mediator to Stimulate RNAPII Elongation in Response to Hypoxia

Galbraith et al. (2013). Cell, 153 (6), 1327-39.

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Article

TET2 and TET3 regulate GlcNAcylation and H3K4 methylation through OGT and SET1/COMPASS

Deplus, R. et al. (2013). EMBO J. 32, 645–50.

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