Protein Production & Assays References

Protein Purification
Strep-Tactin® Sepharose® Resin (Cat. 2-1201-002), (Cat. 2-1201-010), & (Cat. 2-1201-025)
1. Jinkun Xu, et al. (2022). Conformational Changes of a Phosphatidylcholine Flippase in Lipid Membranes. Cell Reports, 38(11), 110518. doi: 10.1016/j.celrep.2022.110518
2. Xiaonan Liu, et al. (2021). SARS-CoV-2–Host Proteome Interactions for Antiviral Drug Discovery. Molecular Systems Biology, 17(11), e10396. doi: 10.15252/msb.202110396
3. Kuo Zhang, et al. (2021). Structural Insights into Viral RNA Capping and Plasma Membrane Targeting by Chikungunya Virus Nonstructural Protein 1. Cell Host & Microbe, 29(5), 757-764. doi: 10.1016/j.chom.2021.02.018
4. Bing Rao, et al. (2021). The Cryo-EM Structure of an ERAD Protein Channel Formed by Tetrameric Human Derlin-1. Science Advances, 7(10). doi: 10.1126/sciadv.abe8591
5. Chunyan Wang, et al. (2020). A Human Monoclonal Antibody Blocking SARS-CoV-2 Infection. Nature Communications, 11, 2251. doi: 10.1038/s41467-020-16256-y
6. Yasunori Watanabe, et al. (2020). Site-Specific Glycan Analysis of the SARS-CoV-2 Spike. Science, 369(6501), 330-333. doi: 10.1126/science.abb9983
7. Jung Hwan Hwang, et al. (2019). Gadd45β Promotes Regeneration After Injury Through TGFβ-Dependent Restitution in Experimental Colitis. Experimental & Molecular Medicine, 51, 1–14. doi: 10.1038/s12276-019-0335-y
8. Jana Krieger, et al. (2018). Cationic Domains in Particle-Forming and Assembly-Deficient HBV Core Antigens Capture Mammalian RNA that stimulates Th1-Biased Antibody Responses by DNA Vaccination. Scientific Reports, 8, 14660. doi: 10.1038/s41598-018-32971-5
9. Francisco Romero Pastrana, et al. (2017). A Lactococcus lactis Expression Vector Set with Multiple Affinity Tags to Facilitate Isolation and Direct Labeling of Heterologous Secreted Proteins. Applied Microbiology and Biotechnology, 101, 8139–8149. doi: 10.1007/s00253-017-8524-x
10. Franziska Tausch, et al. (2017). Evidence for Complex Formation of the Bacillus cereus Haemolysin BL Components in Solution. Toxins, 9(9), 288. doi: 10.3390/toxins9090288
11. Markus Mörk-Mörkenstein, et al. (2017). Non-Canonical Activation of Histidine Kinase KdpD by Phosphotransferase Protein PtsN through Interaction with the Transmitter Domain. Molecular Microbiology, 106(1), 54-73. doi: 10.1111/mmi.13751
12. Oliver Pänke, et al. (2000). F-ATPase: Specific Observation of the Rotating C Subunit Oligomer of EFoEF1. FEBS Letters, 472(1), 34-38. doi: 10.1016/S0014-5793(00)01436-8
Strep-Tactin®XT 4Flow® Resin (Cat. 2-5010-002), (Cat. 2-5010-010), & (Cat. 2-5010-025)
1. Ema Johnston, et al. (2023). The Structural Components of the Azotobacter Vinelandii Iron-Only Nitrogenase, AnfDKG, Form a Protein Complex within the Plant Mitochondrial Matrix. doi: 10.21203/rs.3.rs-2567372/v1
2. Marina Serna, et al. (2022). CryoEM of RUVBL1–RUVBL2–ZNHIT2, a Complex that Interacts with Pre-mRNA-Processing-Splicing Factor 8. Nucleic Acids Research, 50(2), 1128–1146. doi: 10.1093/nar/gkab1267
3. Dave W. Anderson, et al. (2021). The Adaptive Landscape of a Metallo-Enzyme is Shaped by Environment-Dependent Epistasis. Nature Communications, 12, 3867. doi: 10.1038/s41467-021-23943-x
4. Antoni G. Wrobel, et al. (2020). SARS-CoV-2 and Bat RaTG13 Spike Glycoprotein Structures Inform on Virus Evolution and Furin-Cleavage Effects. Nature Structural & Molecular Biology, 27, 763–767. doi: 10.1038/s41594-020-0468-7
5. Juliette Hordeaux. (2019). The GPI-Linked Protein LY6A Drives AAV-PHP.B Transport across the Blood-Brain Barrier. Molecular Therapy, 27(5), 912-921. doi: 10.1016/j.ymthe.2019.02.013
6. Li Wang, et al. (2018). Expression and Purification of a Rapidly Degraded Protein, TMEM8B-a, in Mammalian Cell Line. Protein Expression and Purification, 151, 38-45. doi: 10.1016/j.pep.2018.06.002
7. Christopher J. Holler, et al. (2017). Intracellular Proteolysis of Progranulin Generates Stable, Lysosomal Granulins that Are Haploinsufficient in Patients with Frontotemporal Dementia Caused by GRN Mutations. eNeuro, 4(4). doi: 10.1523/ENEURO.0100-17.2017
8. Alexei Yeliseev, et al. (2017). Application of Strep-Tactin XT for Affinity Purification of Twin-Strep-Tagged CB2, a G Protein-Coupled Cannabinoid Receptor. Protein Expression and Purification, 131, 109-118. doi: 10.1016/j.pep.2016.11.006
9. Sebastian Dintner, et al. (2014). A Sensory Complex Consisting of an ATP-binding Cassette Transporter and a Two-component Regulatory System Controls Bacitracin Resistance in Bacillus subtilis. Journal of Biological Chemistry, 289(40), 27899-27910. doi: 10.1074/jbc.M114.596221
Strep-Tactin® Superflow® High Capacity Resin (Cat. 2-1208-002), (Cat. 2-1208-010), & (Cat. 2-1208-025)
1. Kerstin Wernike, et al. (2021). Differentiation of Antibodies against Selected Simbu Serogroup Viruses by a Glycoprotein Gc-Based Triplex ELISA. Veterinary Sciences, 8(1), 12. doi: 10.3390/vetsci8010012
2. Gleyder Roman-Sosa, et al. (2016). Analysis of the Humoral Immune Response Against the Envelope Glycoprotein Gc of Schmallenberg Virus Reveals a Domain Located At the Amino Terminus Targeted by mAbs with Neutralizing Activity. Journal of General Virology, 97(3). doi: 10.1099/jgv.0.000377
Strep-Tactin® Superflow® Resin (Cat. 2-1206-025)
1. Siebren Faber, et al. (2023). PDE6D Mediates Trafficking of Prenylated Proteins NIM1K and UBL3 to Primary Cilia. Cells, 12(2), 312. doi: 10.3390/cells12020312
2. Chang Liu, et al. (2022). The Antibody Response to SARS-CoV-2 Beta Underscores the Antigenic Distance to Other Variants. Cell Host & Microbe, 30(1), 53-68.E12. doi: 10.1016/j.chom.2021.11.013
MagStrep "type3" XT Beads (Cat. 2-4090-002) & (Cat. 2-4090-010)
1. Bing Rao, et al. (2021). The Cryo-EM Structure of an ERAD Protein Channel Formed by Tetrameric Human Derlin-1. Science Advances, 7(10). doi: 10.1126/sciadv.abe8591
2. David E. Gordon, et al. (2020). A SARS-CoV-2 Protein Interaction Map Reveals Targets for Drug Repurposing. Nature, 583, 459–468. doi: 10.1038/s41586-020-2286-9
3. Jörg Scholl, et al. (2020). Phosphoenolpyruvate Carboxylase from the Cyanobacterium Synechocystis sp. PCC 6803 is Under Global Metabolic Control by PII Signaling. Molecular Microbiology, 114(2), 292-307. doi: 10.1111/mmi.14512
4. Manuel Maidorn, et al. (2018). Nanobodies Reveal an Extra-Synaptic Population of SNAP-25 and Syntaxin 1A in Hippocampal Neurons. mAbs, 11(2), 305-321. doi: 10.1080/19420862.2018.1551675
5. Kow Essuman, et al. (2018). TIR Domain Proteins Are an Ancient Family of NAD+-Consuming Enzymes. Current Biology, 28(3), 421-430.E4. doi: 10.1016/j.cub.2017.12.024
6. Mario González, et al. (2017). The Botrytis cinerea Elicitor Protein BcIEB1 Interacts with the Tobacco PR5-Family Protein Osmotin and Protects the Fungus Against Its Antifungal Activity. New Phytologist, 215(1), 397-410. doi: 10.1111/nph.14588
7. Alexei Yeliseev, et al. (2017). Application of Strep-Tactin XT for Affinity Purification of Twin-Strep-Tagged CB2, a G Protein-Coupled Cannabinoid Receptor. Protein Expression and Purification, 131, 109-118. doi: 10.1016/j.pep.2016.11.006
MagStrep "type3" Strep-Tactin® Beads (Cat. 2-1613-002)
1. Xiaonan Liu, et al. (2018). An AP-MS- and BioID-Compatible MAC-Tag Enables Comprehensive Mapping of Protein Interactions and Subcellular Localizations. Nature Communications, 9, 1188. doi: 10.1038/s41467-018-03523-2
Strep-Tactin® Sepharose® Column (Cat. 2-1202-001)
1. Laura Prioretti, et al. (2023). Carbon Fixation in the Chemolithoautotrophic Bacterium Aquifex aeolicus Involves Two Low-Potential Ferredoxins as Partners of the PFOR and OGOR Enzymes. Life, 13(3), 627. doi: 10.3390/life13030627
2. Yun Nan Hou, et al. (2022). A Conformation-Specific Nanobody Targeting the Nicotinamide Mononucleotide-Activated State of SARM1. Nature Communications, 13, 7898. doi: 10.1038/s41467-022-35581-y
3. Lukas Muschallik, et al. (2020). Synthesis of α-hydroxy Ketones and Vicinal (R,R)-Diols by Bacillus clausii DSM 8716T Butanediol Dehydrogenase. RSC Advances, 10, 12206-12216. doi: 10.1039/D0RA02066D
4. Christina S. Heil, et al. (2018). Site-Specific Labeling of Multidomain Proteins by Amber Codon Suppression. Scientific Reports, 8, 14864. doi: 10.1038/s41598-018-33115-5
5. Christophe J. Lalaurie, et al. (2018). The de novo Design of a Biocompatible and Functional Integral Membrane Protein Using Minimal Sequence Complexity. Scientific Reports, 8, 14564. doi: 10.1038/s41598-018-31964-8
6. Nicole Schäfer, et al. (2016). Complement Regulator FHR-3 Is Elevated either Locally or Systemically in a Selection of Autoimmune Diseases. Frontiers in Immunology, 7, doi: 10.3389/fimmu.2016.00542
7. Cyril Barinka, et al. (2016). Selection and Characterization of Anticalins Targeting Human Prostate-Specific Membrane Antigen (PSMA). Protein Engineering, Design and Selection, 29(3), 105–115. doi: 10.1093/protein/gzv065
8. Sebastian Dintner, et al. (2014). A Sensory Complex Consisting of an ATP-binding Cassette Transporter and a Two-component Regulatory System Controls Bacitracin Resistance in Bacillus subtilis. Journal of Biological Chemistry, 289(40), 27899-27910. doi: 10.1074/jbc.M114.596221
Strep-Tactin® Superflow® High Capacity Column (Cat. 2-1209-550), (Cat. 2-1209-001), & (Cat. 2-1209-051)
1. Jörg Scholl, et al. (2020). Phosphoenolpyruvate Carboxylase from the Cyanobacterium Synechocystis sp. PCC 6803 is Under Global Metabolic Control by PII Signaling. Molecular Microbiology, 114(2), 292-307. doi: 10.1111/mmi.14512
2. Fabian Mohr, et al. (2018). Efficient Immunoaffinity Chromatography of Lymphocytes Directly from Whole Blood. Scientific Reports, 8: 16731. doi: 10.1038/s41598-018-34589-z
3. Annegret Becker, et al. (2018). Functionalization of Gold-Nanoparticles by the Clostridium perfringens Enterotoxin C-Terminus for Tumor Cell Ablation Using the Gold Nanoparticle-Mediated Laser Perforation Technique. Scientific Reports, 8, 14963. doi: 10.1038/s41598-018-33392-0
4. Fabian Mohr, et al. (2017). Minimally Manipulated Murine Regulatory T Cells Purified by Reversible Fab Multimers are Potent Suppressors for Adoptive T-Cell Therapy. European Journal of Immunology, 47(12), 2153-2162. doi: 10.1002/eji.201747137
5. Ghérici Hassaine, et al. (2013). Large Scale Expression and Purification of the Mouse 5-HT3 Receptor. Biochimica et Biophysica Acta (BBA) - Biomembranes, 1828(11), 2544-2552. doi: 10.1016/j.bbamem.2013.05.028
6. Christian Stemberger, et al. (2012). Novel Serial Positive Enrichment Technology Enables Clinical Multiparameter Cell Sorting. PLoS ONE, 7(4): e35798. doi: 10.1371/journal.pone.0035798
Strep-Tactin®XT 4Flow® Column (Cat. 2-5011-005), (Cat. 2-5012-001), (Cat. 2-5013-001), & (Cat. 2-5014-001)
1. Ema Johnston, et al. (2023). The Structural Components of the Azotobacter Vinelandii Iron-Only Nitrogenase, AnfDKG, Form a Protein Complex within the Plant Mitochondrial Matrix. doi: 10.21203/rs.3.rs-2567372/v1
2. Andrea Delle Vedove, et al. (2022). CAPRIN1P512L Causes Aberrant Protein Aggregation and Associates with Early-Onset Ataxia. Cellular and Molecular Life Sciences, 79, 526. doi: 10.1007/s00018-022-04544-3
3. Marina Serna, et al. (2022). CryoEM of RUVBL1–RUVBL2–ZNHIT2, a Complex that Interacts with Pre-mRNA-Processing-Splicing Factor 8. Nucleic Acids Research, 50(2), 1128–1146. doi: 10.1093/nar/gkab1267
4. Peter Braun, et al. (2021). Enzyme-Linked Phage Receptor Binding Protein Assays (ELPRA) Enable Identification of Bacillus anthracis Colonies. Viruses, 13(8), 1462. doi: 10.3390/v13081462
5. Yoonji Kim, et al. (2019). Selection and Characterization of Monoclonal Antibodies Targeting Middle East Respiratory Syndrome Coronavirus through a Human Synthetic Fab Phage Display Library Panning. Antibodies, 8(3), 42. doi: 10.3390/antib8030042
6. Claudia Ortega, et al. (2018). Multi-Compartment and Multi-Host Vector Suite for Recombinant Protein Expression and Purification. Frontiers in Microbiology, 9. doi: 10.3389/fmicb.2018.01384
Strep-Tactin®XT 4Flow® High Capacity Cartridge (Cat. 2-5027-001) & (Cat. 2-5028-001)
1. Emma C. Thomson, et al. (2021). Circulating SARS-CoV-2 Spike N439K Variants Maintain Fitness while Evading Antibody-Mediated Immunity. Cell, 184(5), 1171-1187.E20. doi: 10.1016/j.cell.2021.01.037
2. Sandeep Satapathy, et al. (2020). Rapid High-Yield Expression and Purification of Fully Post-Translationally Modified Recombinant Clusterin and Mutants. Scientific Reports, 10, 14243. doi: 10.1038/s41598-020-70990-3
Strep-Tactin®XT 4Flow® Starter Kit (Cat. 2-5998-000)
1. Tessy A. H. Hick, et al. (2022). Secreted Trimeric Chikungunya Virus Spikes from Insect Cells: Production, Purification, and Glycosylation Status. Processes, 10(1), 162. doi: 10.3390/pr10010162
Desthiobiotin (Cat. 2-1000-002) & (Cat. 2-1000-005)
1. Jinkun Xu, et al. (2022). Conformational Changes of a Phosphatidylcholine Flippase in Lipid Membranes. Cell Reports, 38(11), 110518. doi: 10.1016/j.celrep.2022.110518
2. Karsten Warwas, et al. (2021). Co-Stimulatory Bispecific Antibodies Induce Enhanced T Cell Activation and Tumor Cell Killing in Breast Cancer Models. Frontiers in Immunology, 12. doi: 10.3389/fimmu.2021.719116
3. J. Maximilian Fels, et al. (2021). Protective Neutralizing Antibodies from Human Survivors of Crimean-Congo Hemorrhagic Fever. Cell, 184(13), 3486-3501.E21. doi: 10.1016/j.cell.2021.05.001
4. Jana Krieger, et al. (2018). Cationic Domains in Particle-Forming and Assembly-Deficient HBV Core Antigens Capture Mammalian RNA that stimulates Th1-Biased Antibody Responses by DNA Vaccination. Scientific Reports, 8, 14660. doi: 10.1038/s41598-018-32971-5
5. Cyril Barinka, et al. (2016). Selection and Characterization of Anticalins Targeting Human Prostate-Specific Membrane Antigen (PSMA). Protein Engineering, Design and Selection, 29(3), 105–115. doi: 10.1093/protein/gzv065
6. Oliver Pänke, et al. (2000). F-ATPase: Specific Observation of the Rotating C Subunit Oligomer of EFoEF1. FEBS Letters, 472(1), 34-38. doi: 10.1016/S0014-5793(00)01436-8
Biotin (Cat. 2-1016-002) & (Cat. 2-1016-005)
1. Kuo Zhang, et al. (2021). Structural Insights into Viral RNA Capping and Plasma Membrane Targeting by Chikungunya Virus Nonstructural Protein 1. Cell Host & Microbe, 29(5), 757-764. doi: 10.1016/j.chom.2021.02.018
2. Fabian Schlott, et al. (2018). Characterization and Clinical Enrichment of HLA-C*07:02-Restricted Cytomegalovirus-Specific CD8+ T Cells. Plos One. doi: 10.1371/journal.pone.0193554
3. Sander Kelderman, et al. (2016). Antigen-Specific TIL Therapy for Melanoma: A Flexible Platform for Personalized Cancer Immunotherapy. European Journal of Immunology, 46(6), 1351-1360. doi: 10.1002/eji.201646436
BioLock (Cat. 2-0205-050) & (Cat. 2-0205-250)
1. Kwiwan Jeong, et al. (2022). Rapid Discovery and Classification of Inhibitors of Coronavirus Infection by Pseudovirus Screen and Amplified Luminescence Proximity Homogeneous Assay. Antiviral Research, 209:105473. doi: 10.1016/j.antiviral.2022.105473
2. Can Baysal, et al. (2022). Functional Expression of the Nitrogenase Fe Protein in Transgenic Rice. Communications Biology, 5:1006. doi: 10.1038/s42003-022-03921-9
3. J. Maximilian Fels, et al. (2021). Protective Neutralizing Antibodies from Human Survivors of Crimean-Congo Hemorrhagic Fever. Cell, 184(13), 3486-3501.E21. doi: 10.1016/j.cell.2021.05.001
4. Kuo Zhang, et al. (2021). Structural Insights into Viral RNA Capping and Plasma Membrane Targeting by Chikungunya Virus Nonstructural Protein 1. Cell Host & Microbe, 29(5), 757-764. doi: 10.1016/j.chom.2021.02.018
5. Emma C. Thomson, et al. (2021). Circulating SARS-CoV-2 Spike N439K Variants Maintain Fitness while Evading Antibody-Mediated Immunity. Cell, 184(5), 1171-1187.E20. doi: 10.1016/j.cell.2021.01.037
6. Kerstin Wernike, et al. (2021). Differentiation of Antibodies against Selected Simbu Serogroup Viruses by a Glycoprotein Gc-Based Triplex ELISA. Veterinary Sciences, 8(1), 12. doi: 10.3390/vetsci8010012
7. Antoni G. Wrobel, et al. (2020). SARS-CoV-2 and Bat RaTG13 Spike Glycoprotein Structures Inform on Virus Evolution and Furin-Cleavage Effects. Nature Structural & Molecular Biology, 27, 763–767. doi: 10.1038/s41594-020-0468-7
8. Juliette Hordeaux. (2019). The GPI-Linked Protein LY6A Drives AAV-PHP.B Transport across the Blood-Brain Barrier. Molecular Therapy, 27(5), 912-921. doi: 10.1016/j.ymthe.2019.02.013
9. Neeti Ananthaswamy, et al. (2019). A Sequestered Fusion Peptide in the Structure of an HIV-1 Transmitted Founder Envelope Trimer. Nature Communications, 10:873. doi: 10.1038/s41467-019-08825-7
10. Claudia Ortega, et al. (2018). Multi-Compartment and Multi-Host Vector Suite for Recombinant Protein Expression and Purification. Frontiers in Microbiology, 9. doi: 10.3389/fmicb.2018.01384
11. Watee Seesuay, et al. (2018). Human Transbodies that Interfere with the Functions of Ebola Virus VP35 Protein in Genome Replication and Transcription and Innate Immune Antagonism. Emerging Microbes & Infections, 7(1), 1-15. doi: 10.1038/s41426-018-0031-3
12. Wadad Al Salmi, et al. (2015). A New Approach to Produce HIV-1 Envelope Trimers. Journal of Biological Chemistry, 290(32), 19780-19795. doi: 10.1074/jbc.M115.656611
Buffer E (10x) (Cat. 2-1000-025)
1. Siebren Faber, et al. (2023). PDE6D Mediates Trafficking of Prenylated Proteins NIM1K and UBL3 to Primary Cilia. Cells, 12(2), 312. doi: 10.3390/cells12020312
2. Manuel Maidorn, et al. (2018). Nanobodies Reveal an Extra-Synaptic Population of SNAP-25 and Syntaxin 1A in Hippocampal Neurons. mAbs, 11(2), 305-321. doi: 10.1080/19420862.2018.1551675
3. Annegret Becker, et al. (2018). Functionalization of Gold-Nanoparticles by the Clostridium perfringens Enterotoxin C-Terminus for Tumor Cell Ablation Using the Gold Nanoparticle-Mediated Laser Perforation Technique. Scientific Reports, 8, 14963. doi: 10.1038/s41598-018-33392-0
4. Xiaonan Liu, et al. (2018). An AP-MS- and BioID-Compatible MAC-Tag Enables Comprehensive Mapping of Protein Interactions and Subcellular Localizations. Nature Communications, 9, 1188. doi: 10.1038/s41467-018-03523-2
Buffer BXT (10x) (Cat. 2-1042-025)
1. Antoni G. Wrobel, et al. (2020). SARS-CoV-2 and Bat RaTG13 Spike Glycoprotein Structures Inform on Virus Evolution and Furin-Cleavage Effects. Nature Structural & Molecular Biology, 27, 763–767. doi: 10.1038/s41594-020-0468-7
2. David E. Gordon, et al. (2020). A SARS-CoV-2 Protein Interaction Map Reveals Targets for Drug Repurposing. Nature, 583, 459–468. doi: 10.1038/s41586-020-2286-9
3. Jörg Scholl, et al. (2020). Phosphoenolpyruvate Carboxylase from the Cyanobacterium Synechocystis sp. PCC 6803 is Under Global Metabolic Control by PII Signaling. Molecular Microbiology, 114(2), 292-307. doi: 10.1111/mmi.14512
4. Yoonji Kim, et al. (2019). Selection and Characterization of Monoclonal Antibodies Targeting Middle East Respiratory Syndrome Coronavirus through a Human Synthetic Fab Phage Display Library Panning. Antibodies, 8(3), 42. doi: 10.3390/antib8030042
Buffer W (10x) (Cat. 2-1003-100)
1. Yoonji Kim, et al. (2019). Selection and Characterization of Monoclonal Antibodies Targeting Middle East Respiratory Syndrome Coronavirus through a Human Synthetic Fab Phage Display Library Panning. Antibodies, 8(3), 42. doi: 10.3390/antib8030042
2. Xiaonan Liu, et al. (2018). An AP-MS- and BioID-Compatible MAC-Tag Enables Comprehensive Mapping of Protein Interactions and Subcellular Localizations. Nature Communications, 9, 1188. doi: 10.1038/s41467-018-03523-2
Strep-tag®II Peptide (Cat. 2-1018-002)
1. Gleyder Roman-Sosa, et al. (2016). Analysis of the Humoral Immune Response Against the Envelope Glycoprotein Gc of Schmallenberg Virus Reveals a Domain Located At the Amino Terminus Targeted by mAbs with Neutralizing Activity. Journal of General Virology, 97(3). doi: 10.1099/jgv.0.000377
GFP-Strep-tag®II Control Protein (Cat. 2-1006-005)
1. Marius Terfrüchte, et al. (2017). Applying Unconventional Secretion in Ustilago maydis for the Export of Functional Nanobodies. International Journal of Molecular Sciences, 18(5), 937; doi: 10.3390/ijms18050937
Protein Detection
StrepMAB-Classic (Cat. 2-1507-001)
1. Chang Liu, et al. (2022). The Antibody Response to SARS-CoV-2 Beta Underscores the Antigenic Distance to Other Variants. Cell Host & Microbe, 30(1), 53-68.E12. doi: 10.1016/j.chom.2021.11.013
2. Can Baysal, et al. (2022). Functional Expression of the Nitrogenase Fe Protein in Transgenic Rice. Communications Biology, 5:1006. doi: 10.1038/s42003-022-03921-9
3. Chu Wang, et al. (2021). Flagellin Lysine Methyltransferase FliB Catalyzes a [4Fe-4S] Mediated Methyl Transfer Reaction. PLoS Pathogens, 17(11), e1010052. doi: 10.1371/journal.ppat.1010052
4. Peter Braun, et al. (2021). Enzyme-Linked Phage Receptor Binding Protein Assays (ELPRA) Enable Identification of Bacillus anthracis Colonies. Viruses, 13(8), 1462. doi: 10.3390/v13081462
5. Yanchun Peng, et al. (2020). Broad and Strong Memory CD4+ and CD8+ T Cells Induced by SARS-CoV-2 in UK Convalescent Individuals Following COVID-19. Nature Immunology, 21, 1336–1345. doi: 10.1038/s41590-020-0782-6
6. Sandeep Satapathy, et al. (2020). Rapid High-Yield Expression and Purification of Fully Post-Translationally Modified Recombinant Clusterin and Mutants. Scientific Reports, 10, 14243. doi: 10.1038/s41598-020-70990-3
7. Eleanor M. Denham, et al. (2019). A Generic Cell Surface Ligand System for Studying Cell–Cell Recognition. PLoS Biology, 17(12): e3000549. doi: 10.1371/journal.pbio.3000549
8. Christina S. Heil, et al. (2018). Site-Specific Labelling of Multidomain Proteins by Amber Codon Suppression. Scientific Reports, 8, 14864. doi: 10.1038/s41598-018-33115-5
9. Franziska Tausch, et al. (2017). Evidence for Complex Formation of the Bacillus cereus Haemolysin BL Components in Solution. Toxins, 9(9), 288. doi: 10.3390/toxins9090288
10. Gleyder Roman-Sosa, et al. (2016). Analysis of the Humoral Immune Response Against the Envelope Glycoprotein Gc of Schmallenberg Virus Reveals a Domain Located At the Amino Terminus Targeted by mAbs with Neutralizing Activity. Journal of General Virology, 97(3). doi: 10.1099/jgv.0.000377
StrepMAB-Classic HRP Conjugate (Cat. 2-1509-001)
1. Ema Johnston, et al. (2023). The Structural Components of the Azotobacter Vinelandii Iron-Only Nitrogenase, AnfDKG, Form a Protein Complex within the Plant Mitochondrial Matrix. doi: 10.21203/rs.3.rs-2567372/v1
2. Marina Serna, et al. (2022). CryoEM of RUVBL1–RUVBL2–ZNHIT2, a Complex that Interacts with Pre-mRNA-Processing-Splicing Factor 8. Nucleic Acids Research, 50(2), 1128–1146. doi: 10.1093/nar/gkab1267
3. Peter Braun, et al. (2021). Enzyme-Linked Phage Receptor Binding Protein Assays (ELPRA) Enable Identification of Bacillus anthracis Colonies. Viruses, 13(8), 1462. doi: 10.3390/v13081462
4. Kerstin Wernike, et al. (2021). Differentiation of Antibodies against Selected Simbu Serogroup Viruses by a Glycoprotein Gc-Based Triplex ELISA. Veterinary Sciences, 8(1), 12. doi: 10.3390/vetsci8010012
5. Chunyan Wang, et al. (2020). A Human Monoclonal Antibody Blocking SARS-CoV-2 Infection. Nature Communications, 11, 2251. doi: 10.1038/s41467-020-16256-y
6. Yoonji Kim, et al. (2019). Selection and Characterization of Monoclonal Antibodies Targeting Middle East Respiratory Syndrome Coronavirus through a Human Synthetic Fab Phage Display Library Panning. Antibodies, 8(3), 42. doi: 10.3390/antib8030042
7. Nicole Schäfer, et al. (2016). Complement Regulator FHR-3 Is Elevated either Locally or Systemically in a Selection of Autoimmune Diseases. Frontiers in Immunology, 7, doi: 10.3389/fimmu.2016.00542
8. Wadad Al Salmi, et al. (2015). A New Approach to Produce HIV-1 Envelope Trimers. Journal of Biological Chemistry, 290(32), 19780-19795. doi: 10.1074/jbc.M115.656611
Strep-Tactin® HRP Conjugate (Cat. 2-1502-001)
1. Kwiwan Jeong, et al. (2022). Rapid Discovery and Classification of Inhibitors of Coronavirus Infection by Pseudovirus Screen and Amplified Luminescence Proximity Homogeneous Assay. Antiviral Research, 209:105473. doi: 10.1016/j.antiviral.2022.105473
2. Annika Roth, et al. (2020). LL-37 fights SARS-CoV-2: The Vitamin D-Inducible Peptide LL-37 Inhibits Binding of SARS-CoV-2 Spike Protein to its Cellular Receptor Angiotensin Converting Enzyme 2 In Vitro. bioRxiv. doi: 10.1101/2020.12.02.408153
3. Karolin Montag, et al. (2020). Phylogenetic Analysis of Plant Multi-Domain SEC14-Like Phosphatidylinositol Transfer Proteins and Structure–Function Properties of PATELLIN2. Plant Molecular Biology, 104, 665–678. doi: 10.1007/s11103-020-01067-y
4. Annegret Becker, et al. (2018). Functionalization of Gold-Nanoparticles by the Clostridium perfringens Enterotoxin C-Terminus for Tumor Cell Ablation Using the Gold Nanoparticle-Mediated Laser Perforation Technique. Scientific Reports, 8, 14963. doi: 10.1038/s41598-018-33392-0
5. Watee Seesuay, et al. (2018). Human Transbodies that Interfere with the Functions of Ebola Virus VP35 Protein in Genome Replication and Transcription and Innate Immune Antagonism. Emerging Microbes & Infections, 7(1), 1-15. doi: 10.1038/s41426-018-0031-3
Strep-Tactin® AP Conjugate (Cat. 2-1503-001)
1. Watee Seesuay, et al. (2018). Human Transbodies that Interfere with the Functions of Ebola Virus VP35 Protein in Genome Replication and Transcription and Innate Immune Antagonism. Emerging Microbes & Infections, 7(1), 1-15. doi: 10.1038/s41426-018-0031-3
2. Cyril Barinka, et al. (2016). Selection and Characterization of Anticalins Targeting Human Prostate-Specific Membrane Antigen (PSMA). Protein Engineering, Design and Selection, 29(3), 105–115. doi: 10.1093/protein/gzv06
Strep-Tactin®XT DY-488 Conjugate (Cat. 2-1562-050)
1. Emanuele Andreano, et al. (2021). Extremely Potent Human Monoclonal Antibodies from COVID-19 Convalescent Patients. Cell, 184, 1821–1835. doi: 10.1016/j.cell.2021.02.035
Strep-Tactin®XT DY-649 Conjugate (Cat. 2-1568-050)
1. Andrés Guillén-Samander, et al. (2022). A Partnership Between the Lipid Scramblase XK and the Lipid Transfer Protein VPS13A at the Plasma Membrane. PNAS, 119(35), e2205425119, doi: 10.1073/pnas.2205425119
2. Yaara Finkel, et al. (2021). SARS-CoV-2 Uses a Multipronged Strategy to Impede Host Protein Synthesis. Nature, 594, 240–245. doi: 10.1038/s41586-021-03610-3
StrepMAB-Classic DY-549 Conjugate (Cat. 2-1566-050)
1. Chang Liu, et al. (2022). The Antibody Response to SARS-CoV-2 Beta Underscores the Antigenic Distance to Other Variants. Cell Host & Microbe, 30(1), 53-68.E12. doi: 10.1016/j.chom.2021.11.013
StrepMAB-Classic DY-649 Conjugate (Cat. 2-1569-050)
1. Andrés Guillén-Samander, et al. (2022). A Partnership Between the Lipid Scramblase XK and the Lipid Transfer Protein VPS13A at the Plasma Membrane. PNAS, 119(35), e2205425119, doi: 10.1073/pnas.2205425119
StrepMAB-Immo DY-488 Conjugate (Cat. 2-1564-050)
1. Watee Seesuay, et al. (2018). Human Transbodies that Interfere with the Functions of Ebola Virus VP35 Protein in Genome Replication and Transcription and Innate Immune Antagonism. Emerging Microbes & Infections, 7(1), 1-15. doi: 10.1038/s41426-018-0031-3
Strep-tag®II Peptide (Cat. 2-1018-002)
1. Gleyder Roman-Sosa, et al. (2016). Analysis of the Humoral Immune Response Against the Envelope Glycoprotein Gc of Schmallenberg Virus Reveals a Domain Located At the Amino Terminus Targeted by mAbs with Neutralizing Activity. Journal of General Virology, 97(3). doi: 10.1099/jgv.0.000377
GFP-Strep-tag®II Control Protein (Cat. 2-1006-005)
1. Marius Terfrüchte, et al. (2017). Applying Unconventional Secretion in Ustilago maydis for the Export of Functional Nanobodies. International Journal of Molecular Sciences, 18(5), 937; doi: 10.3390/ijms18050937
Twin-Strep-tag® Capture Kit - Classic (Cat. 2-4370-000), Maxi (Cat. 2-4370-010)
1. Emma C. Thomson, et al. (2021). Circulating SARS-CoV-2 Spike N439K Variants Maintain Fitness while Evading Antibody-Mediated Immunity. Cell, 184(5), 1171-1187.E20. doi: 10.1016/j.cell.2021.01.037
More Examples
1. Bo Hou, et al. (2018). The TatA Component of the Twin-Arginine Translocation System Locally Weakens the Cytoplasmic Membrane of Escherichia coli Upon Protein Substrate Binding. Journal of Biological Chemistry, 293(20), 7592-7605. doi: 10.1074/jbc.RA118.002205
Cloning & Expression
MEXi-293E Cells (Cat. 2-6001-001)
1. Kritika Khanna, et al. (2022). Exploring Antiviral and Anti-Inflammatory Effects of Thiol Drugs in COVID-19. Journal of Physiology-Lung Cellular and Molecular Physiology, 323(3), L372-L389. doi: 10.1152/ajplung.00136.2022
2. Sandeep Satapathy, et al. (2020). Rapid High-Yield Expression and Purification of Fully Post-Translationally Modified Recombinant Clusterin and Mutants. Scientific Reports, 10, 14243. doi: 10.1038/s41598-020-70990-3
MEXi-Culture Medium (Cat. 2-6010-010)
1. Kritika Khanna, et al. (2022). Exploring Antiviral and Anti-Inflammatory Effects of Thiol Drugs in COVID-19. Journal of Physiology-Lung Cellular and Molecular Physiology, 323(3), L372-L389. doi: 10.1152/ajplung.00136.2022
MEXi-Transfection Medium (Cat. 2-6011-010)
1. Sandeep Satapathy, et al. (2020). Rapid High-Yield Expression and Purification of Fully Post-Translationally Modified Recombinant Clusterin and Mutants. Scientific Reports, 10, 14243. doi: 10.1038/s41598-020-70990-3
Competent E. coli TOP10 (Cat. 5-1600-020)
1. Johanna Hausjell, et al. (2019). Recombinant Production of a Hard-to-Express Membrane-Bound Cytochrome P450 in Different Yeasts—Comparison of Physiology and Productivity. Yeast, 37(2), 217-226. doi: 10.1002/yea.3441
2. Ellen Becher, et al. (2018). Active Site Alanine Preceding Catalytic Cysteine Determines Unique Substrate Specificity in Bacterial CoA-Acylating Prenal Dehydrogenase. FEBS Letters, 592(7), 1150-1160. doi: 10.1002/1873-3468.13019
pASK-IBA3C Vector (Cat. 2-1322-000)
1. Chu Wang, et al. (2021). Flagellin Lysine Methyltransferase FliB Catalyzes a [4Fe-4S] Mediated Methyl Transfer Reaction. PLoS Pathogens, 17(11), e1010052. doi: 10.1371/journal.ppat.1010052
2. Franziska Tausch, et al. (2017). Evidence for Complex Formation of the Bacillus cereus Haemolysin BL Components in Solution. Toxins, 9(9), 288. doi: 10.3390/toxins9090288
pASK-IBA5C Vector (Cat. 2-1324-000)
1. Jörg Scholl, et al. (2020). Phosphoenolpyruvate Carboxylase from the Cyanobacterium Synechocystis sp. PCC 6803 is Under Global Metabolic Control by PII Signaling. Molecular Microbiology, 114(2), 292-307. doi: 10.1111/mmi.14512
2. Franziska Tausch, et al. (2017). Evidence for Complex Formation of the Bacillus cereus Haemolysin BL Components in Solution. Toxins, 9(9), 288. doi: 10.3390/toxins9090288
3. Sebastian Dintner, et al. (2014). A Sensory Complex Consisting of an ATP-binding Cassette Transporter and a Two-component Regulatory System Controls Bacitracin Resistance in Bacillus subtilis. Journal of Biological Chemistry, 289(40), 27899-27910. doi: 10.1074/jbc.M114.596221
pASG-IBA43 Vector (Cat. 5-4043-001)
1. Ellen Becher, et al. (2018). Active Site Alanine Preceding Catalytic Cysteine Determines Unique Substrate Specificity in Bacterial CoA-Acylating Prenal Dehydrogenase. FEBS Letters, 592(7), 1150-1160. doi: 10.1002/1873-3468.13019
pENTRY-IBA51 Vector (Cat. 5-4091-001)
1. Christian Stemberger, et al. (2012). Novel Serial Positive Enrichment Technology Enables Clinical Multiparameter Cell Sorting. PLoS ONE, 7(4): e35798. doi: 10.1371/journal.pone.0035798
Protein Immobilization
Strep-Tactin®XT Coated Microplate (Cat. 2-1501-001)
1. Neeti Ananthaswamy, et al. (2019). A Sequestered Fusion Peptide in the Structure of an HIV-1 Transmitted Founder Envelope Trimer. Nature Communications, 10:873. doi: 10.1038/s41467-019-08825-7
2. Francisco Romero Pastrana, et al. (2017). A Lactococcus lactis Expression Vector Set with Multiple Affinity Tags to Facilitate Isolation and Direct Labeling of Heterologous Secreted Proteins. Applied Microbiology and Biotechnology, 101, 8139–8149. doi: 10.1007/s00253-017-8524-x
3. Gleyder Roman-Sosa, et al. (2016). Analysis of the Humoral Immune Response Against the Envelope Glycoprotein Gc of Schmallenberg Virus Reveals a Domain Located At the Amino Terminus Targeted by mAbs with Neutralizing Activity. Journal of General Virology, 97(3). doi: 10.1099/jgv.0.000377
4. Wadad Al Salmi, et al. (2015). A New Approach to Produce HIV-1 Envelope Trimers. Journal of Biological Chemistry, 290(32), 19780-19795. doi: 10.1074/jbc.M115.656611
5. Wolfgang J. Ernst, et al. (2001). Expanding Baculovirus Surface Display. European Journal of Biochemistry, 267(13), 4033-4039. doi: 10.1046/j.1432-1327.2000.01439.x
Strep-Tactin®XT Coated Microplate (Cat. 2-4101-001)
1. Nadine Vollack-Hesse, et al. (2021). Recombinant VWF Fragments Improve Bioavailability of Subcutaneous Factor VIII in Hemophilia A Mice. Blood, 137(8), 1072–1081. doi: 10.1182/blood.2020006468
2. Juliette Hordeaux. (2019). The GPI-Linked Protein LY6A Drives AAV-PHP.B Transport across the Blood-Brain Barrier. Molecular Therapy, 27(5), 912-921. doi: 10.1016/j.ymthe.2019.02.013
StrepMAB-Immo (Cat. 2-1517-001)
1. Christopher J. Holler, et al. (2017). Intracellular Proteolysis of Progranulin Generates Stable, Lysosomal Granulins that Are Haploinsufficient in Patients with Frontotemporal Dementia Caused by GRN Mutations. eNeuro, 4(4). doi: 10.1523/ENEURO.0100-17.2017
2. Cyril Barinka, et al. (2016). Selection and Characterization of Anticalins Targeting Human Prostate-Specific Membrane Antigen (PSMA). Protein Engineering, Design and Selection, 29(3), 105–115. doi: 10.1093/protein/gzv065
Twin-Strep-tag® Capture Kit - Classic (Cat. 2-4370-000), Maxi (Cat. 2-4370-010)
1. Emma C. Thomson, et al. (2021). Circulating SARS-CoV-2 Spike N439K Variants Maintain Fitness while Evading Antibody-Mediated Immunity. Cell, 184(5), 1171-1187.E20. doi: 10.1016/j.cell.2021.01.037
More References
1. Thomas G.M. Schmidt, et al. (2021). The Role of Changing Loop Conformations in Streptavidin Versions Engineered for High-affinity Binding of the Strep-tag II Peptide. Journal of Molecular Biology, 433(9), 166893. doi: 10.1016/j.jmb.2021.166893
2. Renhong Yang, et al. (2020). Structural Basis for the Recognition of SARS-CoV-2 by Full-Length Human ACE2. Science, 367(6485), 1444-1448. doi: 10.1126/science.abb2762
3. Zhou Tong, et al. (2020). Efficient Affinity-Tagging of M13 Phage Capsid Protein IX for Immobilization of Protein III-Displayed Oligopeptide Probes on Abiotic Platforms. Applied Microbiology and Biotechnology, 104, 1201–1209. doi: 10.1007/s00253-019-10338-8
4. Charlotte S. Sørensen, et al. (2019). Linker Dependence of Avidity in Multivalent Interactions Between Disordered Proteins. Journal of Molecular Biology, 431(24), 4784-4795. doi: 10.1016/j.jmb.2019.09.001
5. Fabian Giska, et al. (2019). PP2C Phosphatase Pic1 Negatively Regulates the Phosphorylation Status of Pti1b Kinase, A Regulator of Flagellin-Triggered Immunity in Tomato. Biochemical Journal, 476 (11), 1621–1635. doi: 10.1042/BCJ20190299
6. Guillaume Adelmant, et al. (2019). Tandem Affinity Purification and Mass Spectrometry (TAP-MS) for the Analysis of Protein Complexes. Current Protocols in Protein Science, 96.1, e84. doi: 10.1002/cpps.84
7. Jonas Johannes Christ, et al. (2018). Enzymatic Quantification and Length Determination of Polyphosphate Down to a Chain Length of Two. Analytical Biochemistry, 548, 82-90. doi: 10.1016/j.ab.2018.02.018
8. Robert Hardt, et al. (2018). Identification of Progesterone Receptor Membrane Component-1 as an Interaction Partner and Possible Regulator of Fatty Acid 2-Hydroxylase. Biochemical Journal, 475(5), 853–871. doi: 10.1042/BCJ20170963
9. Désirée L. Röhlen, et al. (2017). Development of an Amperometric Biosensor Platform for the Combined Determination of L-Malic, Fumaric, and L-Aspartic Acid. Applied Biochemistry and Biotechnology, 183, 566–581. doi: 10.1007/s12010-017-2578-1
10. Ghérici Hassaïne, et al. (2017). Expression, Biochemistry, and Stabilization with Camel Antibodies of Membrane Proteins: Case Study of the Mouse 5-HT3 Receptor. Membrane Protein Structure and Function Characterization, 1635. doi: 10.1007/978-1-4939-7151-0_8
11. Sarah Matko, et al. (2017). Enumeration of WT1-Specific CD8+ T Cells for Clinical Application Using an MHC Streptamer Based No-Wash Single-Platform Flow-Cytometric Assay. Cytometry Part A, 91(10), 1001-1008. doi: 10.1002/cyto.a.23146
12. Z. Chen, et al. (2017). Interference of a speB 5′ Untranslated Region Partial Deletion with mRNA Degradation in Streptococcus pyogenes. Molecular Oral Microbiology, 32(5), 390-403. doi: 10.1111/omi.12181
13. Vincent J. C. van Winden, et al. (2016). Mycosins Are Required for the Stabilization of the ESX-1 and ESX-5 Type VII Secretion Membrane Complexes. mBio, 7(5). doi: 10.1128/mBio.01471-16
14. Karina Trojan, et al. (2016). IFNy+ And IFNy- Treg Subsets with Stable and Unstable Foxp3 Expression in Kidney Transplant Recipients with Good Long-Term Graft Function. Transplant Immunology, 39, 1-9. doi: 10.1016/j.trim.2016.10.003
15. Thomas Schmidt, et al. (2015). The Strep-tag System for One-Step Affinity Purification of Proteins from Mammalian Cell Culture. Methods in Molecular Biology, 1286. doi: 10.1007/978-1-4939-2447-9_8
16. Saima Zafar, et al. (2014). Anchorless 23–230 PrPC Interactomics for Elucidation of PrPC Protective Role. Molecular Neurobiology, 49, 1385–1399. doi: 10.1007/s12035-013-8616-2
17. Susanne Jäckel, et al. (2014). Generation and Application of Monoclonal Antibodies Against Rift Valley Fever Virus Nucleocapsid Protein NP and Glycoproteins Gn and Gc. Archives of Virology, 159, 535–546. doi: 10.1007/s00705-013-1867-4
18. Patrick Seitz, et al. (2013). DNA-Uptake Machinery of Naturally Competent Vibrio cholerae. PNAS, 110(44), 17987-17992. doi: 10.1073/pnas.1315647110
19. Boerries Brandenburg, et al. (2005). A Novel System for Efficient Gene Transfer into Primary Human Hepatocytes Via Cell-Permeable Hepatitis B Virus–Like Particle. Hepatology, 42(6), 1300-1309. doi: 10.1002/hep.20950
20. Petra Sebastian, et al (2003). Semi Automated Production of a Set of Different Recombinant GST-Streptag Fusion Proteins. Journal of Chromatography B, 786(1–2), 343-355. doi: 10.1016/S1570-0232(02)00915-7
21. Arne Skerra, et al. (2000). Use of the Strep-Tag and Streptavidin for Detection and Purification of Recombinant Proteins. Methods in Enzymology, 326, 271-304. doi: 10.1016/S0076-6879(00)26060-6
22. Arne Skerra. (1994). Use of the Tetracycline Promoter for the Tightly Regulated Production of a Murine Antibody Fragment in Escherichia coli. Gene, 151(1–2), 131-135. doi: 10.1016/0378-1119(94)90643-2