TMP-POM 7c

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. TMP-POM 7c is a trimethoprim (TMP)-based PROTAC (proteolysis-targeting chimera) designed to modulate protein activity through targeted degradation. In a study, researchers fused Escherichia coli dihydrofolate reductase (eDHFR) to a chimeric antigen receptor (CAR) and demonstrated that this fusion does not disrupt cell signaling or the CAR’s cytotoxic function. The introduction of TMP-POM 7c, which leverages the high-affinity TMP-eDHFR interaction, enables reversible and dose-dependent inhibition of CAR activity by recruiting the proteasome.

References

Lee, I. K., Sharma, N., Noguera-Ortega, E., Liousia, M., Baroja, M. L., Etersque, J. M., Pham, J., Sarkar, S., Carreno, B. M., Linette, G. P., Puré, E., Albelda, S. M., & Sellmyer, M. A. (2023). A genetically encoded protein tag for control and quantitative imaging of CAR T cell therapy. Molecular Therapy, 31(12), 3564–3578. https://doi.org/10.1016/j.ymthe.2023.10.020

Documents 

Datasheet          MSDS

Citations

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