TMP3-TMR

The TMP-tag is based on the tight binding between trimethoprim (TMP), a synthetic antibiotic, and Escherichia coli dihydrofolate reductase (eDHFR), a small enzyme with a high affinity for TMP. By fusing eDHFR to a protein of interest and introducing TMP linked to a probe—such as a fluorescent dye, biotin, or other functional group—researchers can selectively label and study proteins in their native cellular environment. TMP3-TMR is a third-generation covalent TMP-tag designed for improved efficiency in protein labeling and interaction studies. It is based on a proximity-induced covalent Michael addition between an engineered cysteine (Cys) residue in Escherichia coli dihydrofolate reductase (eDHFR) and optimized trimethoprim (TMP)-acrylamide conjugates with minimal linker lengths. Compared to earlier iterations, TMP3-TMR offers enhanced membrane permeability, particularly when conjugated with fluorogenic spirocyclic rhodamine dyes. TMR dye (555Ex/585Em) provides strong red fluorescence, enabling researchers to visualize and track the protein of interest in live cells or tissue using fluorescence microscopy or imaging systems.

References

Mo, J., Chen, J., Shi, Y., Sun, J., Wu, Y., Liu, T., Zhang, J., Zheng, Y., Li, Y., & Chen, Z. (2022). Third-Generation Covalent TMP-Tag for Fast Labeling and Multiplexed Imaging of Cellular Proteins. Angewandte Chemie - International Edition, 61(36). https://doi.org/10.1002/anie.202207905

Documents 

Datasheet          MSDS

Citations

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