Membrane proteins are challenging to study given their hydrophobic nature, generally low native abundance and intrinsic instability(1,2). Regardless, half of all protein drug targets are membrane proteins. For imaging, most fluorescent proteins (i.e. GFP) cannot specifically visualize cell surface subpopulations. However, CLIP-tag, SNAP-tag and cell surface-specific ACP/MCP-tag systems can specifically label subpopulations of target protein expressed on the cell surface using non-cell permeable substrates (3). This approach permits discrimination of different populations of a cell surface protein: those properly translocated to the plasma membrane from those retained in the secretory pathway or already internalized (e.g. upon ligand binding).
- Lacapère J-J, Pebay-Peyroula E, Neumann J-M, Etchebest C. (2007) Trends Biochem Sci. 32, 259–270. PMID: 17481903
- von Heijne G. (2007) J Intern Med. 261, 543–557. PMID: 17547710
- Keppler, A., Pick, H., Arrivoli, C. et al. (2004) Proc. Natl. Acad. Sci. USA, 101, 9955. PMID: 15226507
CLIP-tag™ is a trademark of New England Biolabs, Inc.
SNAP-tag® is a registered trademark of New England Biolabs, Inc.
FAQs for CLIP Surface
Protocols for CLIP Surface
- Cellular Labeling (E9230)
- Cellular Labeling (S9217)
- Cellular Labeling (S9219)
- Cellular Labeling (S9232)
- Cellular Labeling (S9233)
- Cellular Labeling (S9234)
- Cloning of CLIP-tag Fusions in pCLIPf (N9215)
- Expression of CLIP-tag Fusions (N9215)
- Labeling of Proteins in vitro (S9220)
- Labeling of Proteins in vitro (S9233)
- Labeling of Proteins in vitro (S9234)
- Labeling of Proteins in vitro (S9217)
- Labeling of Proteins in vitro (S9219)
- Labeling of Proteins in vitro (S9232)
- Labeling of Proteins in Solution (E9230)
- Use of CLIP-Cell Block with CLIP-Cell Substrates (E9230)
- Use with CLIP-tag substrates (S9220)
- 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
Cellular Imaging & Analysis Brochure
The Cellular Imaging and Analysis brochure provides information on the labeling technologies offered by NEB for studying the function and localization of proteins in cells.
SNAP-tag® Technologies: Novel Tools to Study Protein Function
- Comparison of SNAP-tag®/CLIP-tag™ Technologies to GFP
- Labeling with SNAP-tag® Technology Troubleshooting Guide
Other Tools & Resources
- Simultaneous dual protein labeling on the surface of live cells
- Protein localization and translocation
- Pulse-chase experiments
- Receptor internalization studies
- Selective cell surface labeling
- 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
Protein Labeling with SNAP-tag and CLIP-tag
SNAP-tag®, CLIP-tag™ and ACP/MCP-tag Substrate Selection Chart
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@example.com.
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.