BG- diAcFAM

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. BG- diAcFAM is a SNAP-tag substrate containg diAcFAM dye. It forms a covalent bond with the SNAP-tag protein, ensuring stable labeling for long-term tracking. DiAcFAM ( diacetylfluorescein, 494Ex/526Em after hydrolysis) is a fluorescein derivative where the fluorescein molecule is modified with two acetyl groups. This modification makes it non-fluorescent in its initial state (a "pro-fluorophore"), as the acetylation masks the hydroxyl groups critical for fluorescein’s fluorescence. When used in applications like protein labeling, diAcFAM is typically supplied as a cell-permeable ligand that, once inside cells, can be hydrolyzed by intracellular esterases to release the fluorescent fluorescein core. This activation process results in a bright green fluorescence, making it useful for tracking proteins or other biomolecules in live cells.

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.1c00259

Documents 

Datasheet          MSDS

Citations

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