The SNAP-tag® system is based on a DNA repair enzyme, O6-alkylguanine-DNA alkyltransferase (AGT). It allows for multiple substrate options to enable color changes. It is highly temperature and fixation stable and can be used in vitro or in vivo. The substrate consists of two parts; the benzylguanine group and the functional group, which can be a fluorophore, biotin or bead. During the labeling reaction, the substituted benzyl group covalently attaches to the SNAP-tag releasing free guanine. Once the fluorophore is coupled to the desired protein, the label fluoresces permitting visualization in living or fixed cells.
SNAP-tag® is a registered trademark of New England Biolabs, Inc.
- Labeling of Proteins in vitro (S9215)
- Cellular Labeling (E9100)
- Cellular Labeling (S9102)
- Cellular Labeling (S9103)
- Cellular Labeling (S9104)
- Cellular Labeling (S9105)
- Cellular Labeling (S9107)
- Cellular Labeling (S9109)
- Cellular Labeling (S9110)
- Cellular Labeling (S9216)
- Cellular Labeling (S9217)
- Cellular Labeling (S9218)
- Cellular Labeling (S9219)
- Cellular Labeling (S9221)
- Cloning of CLIP-tag Fusions in pCLIPf (N9215)
- Cloning of SNAP-tag Fusions in pSNAPf (N9183)
- Cloning of SNAP-tag Fusions in pSNAP-tag(T7)-2 (N9181)
- Expression of CLIPf-Cox8A (N9217)
- Expression of CLIPf-H2B (N9218)
- Expression of CLIP-tag Fusions (N9215)
- Expression of SNAPf Fusions (N9183)
- Expression of SNAPf Fusions in SNAPf-H2B (N9186)
- Expression of SNAP-tag Fusions (N9181)
- Instructions for Cellular Labeling (E9200)
- Instructions for Cellular Labeling (S9215)
- Labeling of Proteins in vitro (S9107)
- Labeling of Proteins in vitro (S9110)
- Labeling of Proteins in vitro (S9220)
- Labeling of Proteins in vitro (S9103)
- Labeling of Proteins in vitro (S9104)
- Labeling of Proteins in vitro (S9105)
- Labeling of Proteins in vitro (S9106)
- Labeling of Proteins in vitro (S9109)
- Labeling of Proteins in vitro (S9216)
- Labeling of Proteins in vitro (S9217)
- Labeling of Proteins in vitro (S9218)
- Labeling of Proteins in vitro (S9219)
- Labeling of Proteins in vitro (S9221)
- Labeling of Proteins in vitro (E9100)
- Labeling of Proteins in vitro (S9102)
- Labeling Proteins in vitro (E9200)
- Use of SNAP-Cell Block with SNAP-Cell Substrates (E9100)
- Use with CLIP-tag substrates (S9220)
- Use with SNAP-Cell Substrates (S9106)
- View the video "Fluorescent Labeling of COS-7 Expressing SNAP-tag Fusion Proteins for Live Cell Imaging" in the Journal of Visualized Experiments (JoVE)
- Labeling and Imaging of Cell Surface Receptors Mediated by SNAP-tag®
- Labeling of Escherichia coli Expressed SNAP-tag® Fusion Proteins
- Simultaneous Fluorescent Labeling of Proteins in Living Cells
- Simultaneous Labeling of Two Proteins in Live Cells
- SNAPf based pulse labeling for analysis of protein turnover in living cells
SNAP-tag® Technologies: Tools to Study Protein Function
Read about the NEB’s set of protein tools for the specific labeling (SNAP-, CLIP-, ACP- and MCP-tags) of fusion proteins.
- Cellular Imaging & Analysis Brochure
- Comparison of SNAP-tag®/CLIP-tag™ Technologies to GFP
- Labeling with SNAP-tag® Technology Troubleshooting Guide
- P, Katajisto., Dohla, J., Chaffer, CL., Pentinmikko, N., Marjanovic, N., Igbal, S., Zoncu, R., Chen, W., Weinberg, RA., Sabatini, DM. 2015. Stem cells. Asymmetric apportioning of aged mitochondria between daughter cells is required for stemness Science. 348(6232), PubMedID: 25837514, DOI: 10.1126/science.1260384.
- Julien Mouysset, Samuel Gilberto, Michelle G Meier, Fabienne Lampert, Mukta Belwal, Patrick Meraldi, Matthias Peter 2015. CRL4RBBP7 is required for efficient CENP-A deposition at centromeres J Cell Sci. 128(9), PubMedID: 25795299, DOI: 10.1242/jcs.162305.
- Margaret L Rodgers, Joshua Paulson, Aaron A Hoskins 2015. Rapid isolation and single-molecule analysis of ribonucleoproteins from cell lysate by SNAP-SiMPull RNA. 21(5), PubMedID: 25805862, DOI: 10.1261/rna.047845.114
- Meron Mengistu, Krishanu Ray, George K Lewis, Anthony L DeVico 2015. Antigenic properties of the human immunodeficiency virus envelope glycoprotein gp120 on virions bound to target cells PLoS Pathog. 11(3), PubMedID: 25807494, DOI: 10.1371/journal.ppat.1004772.
- Gabriele Fuchs, Alexey N Petrov, Caleb D Marceau, Lauren M Popov, Jin Chen, Sen E O'Leary, Richard Wang, Jan E Carette, Peter Sarnow, Joseph D Puglisi 2015. Kinetic pathway of 40S ribosomal subunit recruitment to hepatitis C virus internal ribosome entry site Proc Natl Acad Sci U S A. 112(2), PubMedID: 25516984, DOI: 10.1073/pnas.1421328111.
- Juri Nio Bach, Marc Bramkamp 2015. Dissecting the molecular properties of prokaryotic flotillins PLoS One. 10(1), PubMedID: 25635948, DOI: 10.1371/journal.pone.0116750.
- Domoszlai T, Martincuks A, Fahrenkamp D, Schmitz-Van de Leur H, Küster A, Müller-Newen G 2014. Consequences of the disease-related L78R mutation for dimerization and activity of STAT3 J Cell Sci. 127(Pt 9), PubMedID: 24569879, DOI: 10.1242/jcs.137422
- Simultaneous dual protein labeling inside live cells
- Protein localization and translocation
- Pulse-chase experiments
- Receptor internalization studies
- Selective cell surface labeling
- Protein pull-down assays
- Protein detection in SDS-PAGE
- Flow cytometry
- High throughput binding assays in microtiter plates
- Biosensor interaction experiments
- FRET-based binding assays
- Single molecule labeling
- Super-resolution microscopy
While NEB develops and validates its products for various applications, the use of this product may require the buyer to obtain additional third party intellectual property rights for certain applications.
For more information about commercial rights, please contact NEB's Global Business Development team at [email protected].
This product is intended for research purposes only. This product is not intended to be used for therapeutic or diagnostic purposes in humans or animals.
Watch as Chris Provost, of New England Biolabs, performs fluorescent imaging of live COS-7 cells expressing SNAP-tag® fusion proteins.
View an interactive tutorial explaining the mechanism of our SNAP-tag® technologies and reagents available for researchers wishing to study the function and localization of proteins in live or fixed cells.