For advanced users with novel probes interested in working with SNAP-tag technologies, a complete line of building blocks are available for linkage of the core benzylguanine (BG) and benzylcytosine (BC) and CoA moieties to activated esters, primary amines and thiol groups. The variety of functional groups allows a choice of chemical coupling approaches to suit the molecule or surface to be coupled. Use building blocks to make novel SNAP-, CLIP-, ACP- and MCP-tag substrates. Couple onto surfaces such as Biacore® chips or microarrays for specific protein immobilization (1). Couple onto peptides or DNA oligomers to tag proteins (2). Couple onto new fluorophores or affinity reagents for specific protein labeling (3). Labeling is gentle, precise, and versatile: one label is covalently bound under biological conditions in a defined position. Each fusion protein can be labeled with different probes for different applications.

Product	NEB #	Structure	Application	Size
BG-NH2	#S9148S		SNAP-tag substrate. Suitable for linkage to NHS esters and other activated carboxylic esters.	2 mg
CBG-NH2	#S9149S		SNAP-tag substrate. Improved water solubility. Particularly suited for fusion protein immobilization on solid surfaces.	2 mg
BG-PEG-NH2	#S9150S		SNAP-tag substrate. PEG-linker gives superior flexibility. Particularly suited for modification with affinity ligands.	2 mg
BG-GLA	#S9155S		SNAP-tag substrate. General purpose building block. Requires activation to couple to another functional group.	2 mg
BG-GLA-NHS	#S9151S		SNAP-tag substrate. Activated as NHS ester. Reacts with primary amines.	2 mg
BG-Maleimide	#S9153S		SNAP-tag substrate. Activated as maleimide. Reacts with thiols.	2 mg
BC-NH2	#S9236S		CLIP-tag substrate. Suitable for linkage to NHS esters and other activated carboxylic esters.	2 mg
CoA-SH	#S9352S		ACP- and MCP-tag substrate. Suitable for linkage to maleimides and iodoacetamides.	2 mg

References

1. Sielaff, I., Arnold, A., Godin, G. et al. (2006) ChemBioChem, 7, 194-202.
2. Stein, V., Sielaff, I., Johnsson, K. and HOllfelder, F. (2007) ChemBioChem, 8, 2191-2194.
3. Kindermann, M., Sielaff, I. and Johnsson, K. (2006) Bioorg. Med. Chem. Lett. 14, 2725-2728.
4. Bannwarth, M., Correa, I.R. Jr., Sztretye, M. et al. (2009) ACS Chem. Biol., 4, 179-190.
5. Tomat, E., Nolan, E.M., Jaworski, J. and Lippard, S.J. (2008) J. Am. Chem. Soc., 130, 15776-15777.
6. Mao, S., Benninger, R.K.P., Yan, Y. et al. (2008) Biophysical Journal 94, 4515-4524.