CP-BCN

SNAP-tag is a self-labeling protein derived from human O6-alkylguanine-DNA-alkyltransferase. At 20 kDa, SNAP-tag is smaller than HaloTag (33 kDa), potentially reducing interference with the tagged protein’s function. SNAP-tag reacts with covalently with benzylguanine (BG)or chloropyrimidine (CP) derivatives, forming a stable thioether bonds that ensures durability for long-term experiments or harsh conditions. SNAP-tag can be used alongside other tags like CLIP-tag for multicolor labeling. Chloropyrimidine (CP) derivatives generally exhibit better cell permeability compared to their benzylguanine (BG) derivatives. CP-BCN is a SNAP-tag substrate containg BCN moiety for click chemistry applications. BCN (bicyclo[6.1.0]non-4-yne) is a strained cyclooctyne used in click chemistry for copper-free bioconjugation reactions. Through the SPAAC (Strain-Promoted Azide-Alkyne Cycloaddition) reaction, BCN reacts efficiently with azides to form stable 1,2,3-triazole linkages, making it a valuable tool for molecular biology, imaging, and drug development.

References

Wilhelm, J., Kuhn, S., Tarnawski, M., Gotthard, G., Tunnermann, J., Tanzer, T., Karpenko, J., Mertes, N., Xue, L., Uhrig, U., Reinstein, J., Hiblot, J., & Johnsson, K. (2021). Kinetic and Structural Characterization of the Self-Labeling Protein Tags HaloTag7, SNAP-tag, and CLIP-tag. Biochemistry, 60(33), 2560–2575. https://doi.org/10.1021/acs.biochem.1c00272

Documents 

Datasheet          MSDS

Citations

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