Restriction Endonucleases
Choose Type:
- Digestion of Agarose-Embedded DNA
- Standard Digest Using RE-Mix®
- Double Digest Protocol using Two RE-Mix® Enzymes
- Optimizing Restriction Endonuclease Reactions
- Double Digest Protocol using One RE-Mix and One Standard Restriction Enzyme
- Protocol for Direct Digestion of gDNA during droplet digital PCR (ddPCR)
- Double Digest Protocol with Standard Restriction Enzymes
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Restriction Endonucleases: Molecular Cloning and Beyond
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Type II Restriction Enzymes: What You Need to Know | NEB
Read about Type II restriction enzymes and the distinguishing properties of the four principle subtypes.
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A Modern Day Gene Genie Sir Richard Roberts on Rebase
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Restriction Enzyme Cleavage: ‘single-site’ enzymes and ‘multi-site’ enzymes
Restriction enzymes are proteins used to fragment and clone DNA, but their biological function is to protect bacteria and archaea against viral infections.
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Whole genome assembly from next generation sequencing data using restriction and nicking enzymes in optical mapping and proximity-based ligation strategies
High throughput sequencing methods have revolutionized genomic analysis by producing millions of sequence reads from an organism’s DNA at an ever decreasing cost.
- NEB Restriction Enzyme Activity Poster
- DNA Sequences and Maps Tool
- REBASE®
- Alphabetized List of Recognition Sequences
- Cleavage Of Supercoiled DNA
- Compatible Cohesive Ends and Generation of New Restriction Sites
- Dam-Dcm and CpG Methylation
- Enzymes with Multiple Recognition Sequences
- Enzymes with Nonpalindromic Sequences
- Frequencies of Restriction Sites
- Interrupted Palindromes
- Isoelectric Points (pI) for Restriction Enzymes
- Isoschizomers
- Recleavable Blunt Ends
- Recleavable Filled-in 5' Overhangs
- Time-Saver™ Qualified Enzymes
- Type IIS Restriction Enzymes
- Why Choose Recombinant Enzymes?
- Restriction Enzyme Troubleshooting Guide
- Activity at 37°C for Restriction Enzymes with Alternate Incubation Temperatures
- Activity of Restriction Enzymes in PCR Buffers
- Alteration of Apparent Recognition Specificities Using Methylases
- Cleavage Close to the End of DNA Fragments
- Dam and Dcm Methylases of E. coli
- Digestion of Agarose-Embedded DNA: Info for Specific Enzymes
- Double Digests
- Effects of CpG Methylation on Restriction Enzyme Cleavage
- Heat Inactivation
- NEBuffer Activity/Performance Chart with Restriction Enzymes
- Optimizing Restriction Endonuclease Reactions
- Restriction Endonucleases - Survival in a Reaction
- Restriction Enzyme Diluent Buffer Compatibility
- Restriction Enzyme Tips
- Restriction Enzymes for Droplet Digital PCR (ddPCR)
- Restriction Enzymes requiring multi-sites for efficient cleavage
- Restriction of Foreign DNA by E. coli K-12
- Site Preferences
- Star Activity
- Traditional Cloning Quick Guide
- Crystal Structure of the 8 bp-Specific Restriction Enzyme SwaI (2015)
Feature Articles
Brochures
Web Tools
Selection Tools
Troubleshooting Guides
Usage Guidelines
Posters
- Kamps-Hughes, N., Quimby, A., Zhu, Z., Johnson, E.A. (2013) Massively parallel characterization of restriction endonucleases Nucleic Acids Res ; 41(11), e119. PubMedID: 23605040, DOI: 10.1093/nar/gkt257
- Roberts, R.J., Vincze, T., Posfai, J., Macelis, D. (2015) REBASE - A database for DNA restriction and modification: enzymes, genes and genomes Nucleic Acids Res; 43, D298-D299. PubMedID: 25378308
- Loenen, W.A., Raleigh, E.A. (2014) The other face of restriction: modification-dependent enzymes. Nucleic Acids Res; 42, 56-69. PubMedID: 23990325
- Roberts, R.J., Vincze, T., Posfai, J., Macelis, D. (2014) REBASE - A database for DNA restriction and modification: enzymes, genes and genomes Nucleic Acids Res;
- Morgan, R.D., Luyten, Y.A., Johnson, S.A., Clough, E.M., Clark, T.A. and Roberts, R.J. (2016) Novel m4C modification in type I restriction-modification systems. Nucleic Acids Res; Nov, 2;44(19):9413-9425. PubMedID: 27580720
- Fu YB, Peterson G. W., Dong Y (2016) Increasing Genome Sampling and Improving SNP Genotyping for Genotyping-by-Sequencing with New Combinations of Restriction Enzymes G3 (Bethesda); 6:4, 845-846. PubMedID: 26818077
- Blow, M.J., Clark, T.A., Daum, C.G., Deutschbauer, A.M., Fomenkov, A., Fries, R., Froula, J., Kang, D.D., Malmstrom, R.R., Morgan, R.D., Posfai, J., Singh, K., Visel, A., Wetmore, K., Zhao, Z., Rubin, E.M., Korlach, J., Pennacchio, L.A. and Roberts, R.J. (2016) The Epigenomic Landscape of Prokaryotes. PLoS Genet; Feb 12;12(2):e1005854, PubMedID: 26870957, DOI: 10.1371/journal.pgen.1005854
- Callahan, S.J., Luyten, Y.A., Gupta, Y.K., Wilson, G.G., Roberts, R.J., Morgan, R.D. and Aggarwal, A.K. (2016) Structure of Type IIL Restriction-Modification Enzyme MmeI in Complex with DNA Has Implications for Engineering New Specificities. PLoS Biol; Apr 15;14(4):e1002442, PubMedID: 27082731
- Shah, S., Sanchez, J., Stewart, A., et al. (2015) Probing the Run-On Oligomer of Activated SgrAI Bound to DNA PLoS One; 10(4), PubMedID: 25880668, DOI: 10.1371/journal.pone.0124783.
- Fomenkov, A., Lunnen, K.D., Zhu, Z., Anton, B.P., Wilson, G.G., Vincze, T. and Roberts, R.J. (2015) Complete genome sequence and methylome analysis of bacillus strain x1 Genome Announc; 3(1), PubMedID: 25700417
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