Cellular Analysis
Studies of protein properties, expression, transport, degradation and their interactions with other cellular systems are integral to biomedical research, drug discovery and developmental biology. Eukaryotic proteins function in signaling pathways, metabolism, structure, adhesion, cell movement, active and passive transport, DNA repair, viral disease mechanisms, the immune system, fertilization, differentiation, epigenetics, cancer and the cell division cycle.
For efficient analysis of cellular protein interactions and expression, target genes are often engineered into reporter systems, and then expressed in cells as recombinant fusion proteins. Reporter gene characteristics are chosen to enable downstream in vitroor in vivo method applications. This commonly used and widely successful strategy can facilitate applications such as flow cytometry, cell sorting, in vitro or in vivo imaging, proteomic microarray, cell-based microarray, SDS-PAGE gel electrophoresis, Western blot, quantitative affinity purification followed by mass spectrometry (q-AP-MS), pulse-chase and receptor internalization assays. In particular, improved reporter systems in conjunction with optical imaging technical advances are pushing the frontiers of fluorescence imaging applications.
New England Biolabs offers an innovative technology for studying the function and localization of proteins in living and fixed cells. Covalent protein labeling offers simplicity and versatility to the imaging of mammalian proteins in live cells, as well as the ability to capture proteins in vitro. A single genetic construct generates a fusion protein which, when covalently attached to a variety of fluorophores, biotin or beads, provides a powerful tool for studying protein dynamics. In the first system, the protein is labeled by a self-labeling fusion protein; SNAP-tag® or CLIP-tag™.
SNAP-tag® is a registered trademark of New England Biolabs, Inc.
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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.
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Gaussia and Cypridina Luciferases - Ultrasensitive secreted reporters and their use in dual assays
- Cellular Imaging & Analysis Brochure
- Spectral Properties of SNAP-tag and CLIP-tag Fluorescent Substrates
- Comparison of SNAP-tag®/CLIP-tag™ Technologies to GFP
- Labeling with SNAP-tag® Technology Troubleshooting Guide
- In Vitro Reconstitution of Thermococcus Species 9°N Okazaki Fragment Maturation (2015)
- One Ring To Bind Them All: Is HemeBiosynthesis A Factor In Wolbachia-Filarial Nematode Endosymbiosis? (2015)
- Genome-wide profiling of nuclease protected domains reveals physical properties of chromatin (2019)
- Improving Transcriptome Profiling for Single Cell and Low Input RNA (2019)
Feature Articles
Brochures
Selection Tools
Troubleshooting Guides
Posters
- Reuter, W.H., Masuch, T., Ke, N., Lenon, M., Radzinski, M., Van Loi, V., Ren, G., Riggs, P., Antelmann, H., Reichmann, D., Leichert, L.I., Berkmen, M (2019) Utilizing redox-sensitive GFP fusions to detect in vivo redox changes in a genetically engineered prokaryote Redox Biol; 26, 101280. PubMedID: 31450103, DOI: 10.1016/j.redox.2019.101280
- Maffei, M., Morelli, C., Graham, E., Patriarca, S., Donzelli, L., Doleschall, B., de Castro, Reis, F., Nocchi, L., Chadick, C.H., Reymond, L., Correa, I.R., Jr., Johnsson, K., Hackett, J.A., Heppenstall, P.A (2019) A ligand based system for receptor specific delivery of proteins Sci Rep; 9(1), 19214.. PubMedID: 31844114, DOI: 10.1038/s41598-019-55797-1
- Carpinone, E.M., Li, Z., Mills, M.K., Foltz, C., Brannon, E.R., Carlow, C.K.S., Starai, V.J. (2018) Identification of putative effectors of the Type IV secretion system from the Wolbachia endosymbiont of Brugia malayi PLoS One; 13 (9), e0204736. PubMedID: 30261054, DOI: 10.1371/journal.pone.0204736
- Ke, N., Landgraf, D., Paulsson, J. and Berkmen, M. (2016) Visualization of Periplasmic and Cytoplasmic Proteins with a Self-Labeling Protein Tag. J Bacteriol; Jan 19;198(7), 1035-43. PubMedID: 26787765
- 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), 1899-910. PubMedID: 24569879, DOI: 10.1242/jcs.137422
- Johnson K. (2008) SNAP-tag Technologies: Novel tools to study protein function NEB Expressions ; 3.3 , 1-3 .
Products and content are covered by one or more patents, trademarks and/or copyrights owned or controlled by New England Biolabs, Inc (NEB). The use of trademark symbols does not necessarily indicate that the name is trademarked in the country where it is being read; it indicates where the content was originally developed. All other trademarks are the property of their respective owners. The use of this product may require the buyer to obtain additional third-party intellectual property rights for certain applications. For more information, please email busdev@neb.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.
