Vectors are available for SNAP-tag and CLIP-tag fusion protein expression and labeling in mammalian and bacterial systems. Vectors are available for SNAP-tag and CLIP-tag fusion protein expression and labeling in mammalian and bacterial systems. The mammalian SNAPf and CLIPf vectors express faster-reacting variants of the SNAP-tag and CLIP-tag than previously available vectors. Improved polylinker sequences both upstream and downstream from the tag allow expression of the tag on either end of the protein of interest, under control of the CMV promoter. SNAPf and CLIPf expression vectors contain a neomycin resistance (NeoR) gene for selection of stable transfectants, together with an IRES element for efficient expression of both the fusion protein and NeoR. Codon usage has been optimized for mammalian expression. The pSNAP-tag®(T7)-2 vector (NEB #N9181) is an E.coli expression plasmid encoding the SNAP-tag protein. The codon usage of the SNAP26b gene is optimized for expression in E.coli. Expression is under the control of the IPTG-inducible T7 promoter.
- Cloning of CLIP-tag Fusions in pCLIPf (N9215)
- Expression of CLIP-tag Fusions (N9215)
- Cloning of SNAP-tag Fusions in pSNAPf (N9183)
- Cloning of SNAP-tag Fusions in pSNAP-tag(T7)-2 (N9181)
- Expression of SNAP-tag Fusions (N9181)
- Expression of SNAPf Fusions (N9183)
- Optimizing Restriction Endonuclease Reactions
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
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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.