RosettaCommons/UTexasAptamer huggingface dataset:
Aptamer: Apt-106
Target: Autonomously replicating sequence‐binding factor 1 (ABF1) protein
Type of nucleic acid: ssDNA
Sequence: 5′GACCCGTAGGGCAGTGAATTCAGACATGTGATGATATATCGTGTCTCGTGATAGCAAGCTTGGACGTGTGTGCG3'
Sequence length: 74
GC content: 0.5
Affinity: Kd: 2.4 ± 0.4 nM
Pool type: 5′‐GACCCGTAGGGCAGTGAATTCAG‐N30‐GCAAGCTTGGACGTGTGTGCG-3'
Pool random region: 30
Binding buffer/conditions: 25 mM HEPES, pH 7.5, 25 μM ZnCl2, 2 mM β‐mercaptoethanol, 5% glycerol, 75 mM NaCl, 0.1 mg/ml poly(dI‐dC) and 0.1 mg/ml BSA
Buffer type: Other Buffers
pH: 7.5
Molecular weight of target: Not reported
Post-SELEX modifications: Not applicable
Application as quoted in the referenced paper: Detection: " DNA sequences that are bound by ABF1 with nearly two-magnitude higher affinity as compared to the hitherto accepted ABF1 consensus sequence. The autonomously replicating sequence-binding factor 1 (ABF1) from Sacchramoyces cerevisiae is known as a multifunctional DNA binding protein that is involved in transcriptional regulation, DNA-replication, and in restructuring of chromatin via nucleosome remodelling."
Reference (2005, FEBS Lett ): Beinoraviciūte-Kellner, R., Lipps, G., & Krauss, G. (2005). In vitro selection of DNA binding sites for ABF1 protein from Saccharomyces cerevisiae. FEBS letters, 579(20), 4535–4540. https://doi.org/10.1016/j.febslet.2005.07.009
Aptamer: Apt-74
Target: Autonomously replicating sequence‐binding factor 1 (ABF1) protein
Type of nucleic acid: ssDNA
Sequence: 5′GACCCGTAGGGCAGTGAATTCAGCGTGTCGTATTGAGTGATATGATGCACATAGCAAGCTTGGACGTGTGTGCG3'
Sequence length: 74
GC content: 0.5135135135135135
Affinity: Kd: 4.1 ± 0.6 nM
Pool type: 5′‐GACCCGTAGGGCAGTGAATTCAG‐N30‐GCAAGCTTGGACGTGTGTGCG-3'
Pool random region: 30
Binding buffer/conditions: 25 mM HEPES, pH 7.5, 25 μM ZnCl2, 2 mM β‐mercaptoethanol, 5% glycerol, 75 mM NaCl, 0.1 mg/ml poly(dI‐dC) and 0.1 mg/ml BSA
Buffer type: Other Buffers
pH: 7.5
Molecular weight of target: Not reported
Post-SELEX modifications: Not applicable
Application as quoted in the referenced paper: Detection: " DNA sequences that are bound by ABF1 with nearly two-magnitude higher affinity as compared to the hitherto accepted ABF1 consensus sequence. The autonomously replicating sequence-binding factor 1 (ABF1) from Sacchramoyces cerevisiae is known as a multifunctional DNA binding protein that is involved in transcriptional regulation, DNA-replication, and in restructuring of chromatin via nucleosome remodelling."
Reference (2005, FEBS Lett ): Beinoraviciūte-Kellner, R., Lipps, G., & Krauss, G. (2005). In vitro selection of DNA binding sites for ABF1 protein from Saccharomyces cerevisiae. FEBS letters, 579(20), 4535–4540. https://doi.org/10.1016/j.febslet.2005.07.009
Aptamer: Apt-58
Target: Autonomously replicating sequence‐binding factor 1 (ABF1) protein
Type of nucleic acid: ssDNA
Sequence: 5′GACCCGTAGGGCAGTGAATTCAGTTACCGTGATGTATGATATGCATCCACCGTGGCAAGCTTGGACGTGTGTGCG3'
Sequence length: 75
GC content: 0.5333333333333333
Affinity: Kd: 10.8 ± 1.5 nM
Pool type: 5′‐GACCCGTAGGGCAGTGAATTCAG‐N30‐GCAAGCTTGGACGTGTGTGCG-3'
Pool random region: 30
Binding buffer/conditions: 25 mM HEPES, pH 7.5, 25 μM ZnCl2, 2 mM β‐mercaptoethanol, 5% glycerol, 75 mM NaCl, 0.1 mg/ml poly(dI‐dC) and 0.1 mg/ml BSA
Buffer type: Other Buffers
pH: 7.5
Molecular weight of target: Not reported
Post-SELEX modifications: Not applicable
Application as quoted in the referenced paper: Detection: " DNA sequences that are bound by ABF1 with nearly two-magnitude higher affinity as compared to the hitherto accepted ABF1 consensus sequence. The autonomously replicating sequence-binding factor 1 (ABF1) from Sacchramoyces cerevisiae is known as a multifunctional DNA binding protein that is involved in transcriptional regulation, DNA-replication, and in restructuring of chromatin via nucleosome remodelling."
Reference (2005, FEBS Lett ): Beinoraviciūte-Kellner, R., Lipps, G., & Krauss, G. (2005). In vitro selection of DNA binding sites for ABF1 protein from Saccharomyces cerevisiae. FEBS letters, 579(20), 4535–4540. https://doi.org/10.1016/j.febslet.2005.07.009
Aptamer: C17
Target: Herpes simplex virus-1 (HSV-1) US11
Type of nucleic acid: ssRNA
Sequence: 5'GGGAAUGGAUCCACAUCUACGAAUUCGCAAUCCUGUAUUGAACUUCUCACUAAAACUUCACUGCAGACUUGACGAAGCUU3'
Sequence length: 80
GC content: 0.425
Affinity: Kd: 70 nM
Pool type: 5'-GGGAAUGGAUCCACAUCUACGAA-N32-UUCACUGCAGACUUGACGAAGCUU-3'
Pool random region: 32
Binding buffer/conditions: 50 mM Tris, pH 7.5, 200 mM NaCl, 5 mM MgCl2 and 1 mM DTT
Divalent salt: MgCl
Buffer type: Tris Buffers
pH: 7.5
Molecular weight of target: 23 kDa
Post-SELEX modifications: Not applicable
Application as quoted in the referenced paper: Detection: " RNA-binding protein, herpes simplex virus-1 (HSV-1) US11, is a relatively small (∼23 kDa), highly basic phosphoprotein that is expressed late in infection but is present at early times post-infection as it enters the cell as a component of the virion. There have, however, been some reports regarding potential functions of the protein such as a role in axonal transport of the virion and the regulation of gene expression"
Reference (2005, Nucleic Acids Res ): Bryant, K. F., Cox, J. C., Wang, H., Hogle, J. M., Ellington, A. D., & Coen, D. M. (2005). Binding of herpes simplex virus-1 US11 to specific RNA sequences. Nucleic acids research, 33(19), 6090–6100. https://doi.org/10.1093/nar/gki919
Aptamer: Aptamer 1
Target: Mammalian eukaryotic translation initiation factor 4F (eIF4E)
Type of nucleic acid: ssRNA
Sequence: 5'GGGAGACAAGAAUAAACGCUCAAUGUUCAACCAGAGUGAAACCACUAACGGGUCAGAGCCCCUUCGACAGGAGGCUCACAACAGGC3'
Sequence length: 86
GC content: 0.5232558139534884
Affinity: Kd: 11.2 nM
Pool type: 5'-GGGAGACAAGAATAAACGCTCAA-N40-TTCGACAGGAGGCTCACAACAGGC-3'
Pool random region: 40
Binding buffer/conditions: 20 mM Tris-HCl at pH 7.6, 80 mM potassium acetate, 2.5 mM magnesium acetate, 1 mM dithiothreitol, 5% glycerol
Buffer type: Tris Buffers
pH: 7.6
Molecular weight of target: Not reported
Post-SELEX modifications: Not applicable
Application as quoted in the referenced paper: Therapeutic: " The eukaryotic translation initiation factor 4F (eIF4F) consists of three polypeptides (eIF4A, eIF4G, and eIF4E) and is responsible for recruiting ribosomes to mRNA. eIF4E recognizes the mRNA 5′-cap structure (m7GpppN) and plays a pivotal role in control of translation initiation, which is the rate-limiting step in translation. Overexpression of eIF4E has a dramatic effect on cell growth and leads to oncogenic transformation. Therefore, an inhibitory agent to eIF4E, if any, might serve as a novel therapeutic against malignancies that are caused by aberrant translational control."
Reference (2005, RNA ): Mochizuki, K., Oguro, A., Ohtsu, T., Sonenberg, N., & Nakamura, Y. (2005). High affinity RNA for mammalian initiation factor 4E interferes with mRNA-cap binding and inhibits translation. RNA (New York, N.Y.), 11(1), 77–89. https://doi.org/10.1261/rna.7108205
Aptamer: Aptamer 2
Target: Mammalian eukaryotic translation initiation factor 4F (eIF4E)
Type of nucleic acid: ssRNA
Sequence: 5'GGGAGACAAGAAUAAACGCUCAAGCCAGAGCAACAACCUUCCGAGCCGCGGGAUAAAACCGAGUUCGACAGGAGGCUCACAACAGGC3'
Sequence length: 87
GC content: 0.5517241379310345
Affinity: Not reported
Pool type: 5'-GGGAGACAAGAATAAACGCTCAA-N40-TTCGACAGGAGGCTCACAACAGGC-3'
Pool random region: 40
Binding buffer/conditions: 20 mM Tris-HCl at pH 7.6, 80 mM potassium acetate, 2.5 mM magnesium acetate, 1 mM dithiothreitol, 5% glycerol
Buffer type: Tris Buffers
pH: 7.6
Molecular weight of target: Not reported
Post-SELEX modifications: Not applicable
Application as quoted in the referenced paper: Therapeutic: " The eukaryotic translation initiation factor 4F (eIF4F) consists of three polypeptides (eIF4A, eIF4G, and eIF4E) and is responsible for recruiting ribosomes to mRNA. eIF4E recognizes the mRNA 5′-cap structure (m7GpppN) and plays a pivotal role in control of translation initiation, which is the rate-limiting step in translation. Overexpression of eIF4E has a dramatic effect on cell growth and leads to oncogenic transformation. Therefore, an inhibitory agent to eIF4E, if any, might serve as a novel therapeutic against malignancies that are caused by aberrant translational control."
Reference (2005, RNA ): Mochizuki, K., Oguro, A., Ohtsu, T., Sonenberg, N., & Nakamura, Y. (2005). High affinity RNA for mammalian initiation factor 4E interferes with mRNA-cap binding and inhibits translation. RNA (New York, N.Y.), 11(1), 77–89. https://doi.org/10.1261/rna.7108205
Aptamer: S-PS8.4
Target: Type IVB pili of Salmonella enterica (S. enterica) serovar Typhi (pre-PilS)
Type of nucleic acid: ssRNA
Sequence: 5′GCGGAAUUCUAAUACGACUCACUAUAGGGAACAGUCCGAGCCUCACUGUUAUCCGAUAGCAGCGCGGGAUGAGGGUCAAUGCGUCAUA3'
Sequence length: 88
GC content: 0.5113636363636364
Affinity: Kd: 8.56 nM
Pool type: 5′-GCGGAAUUCUAAUACGACUCACUAUAGGGAACAGUCCGAGCC-N30-GGGUCAAUGCGUCAUA-3
Pool random region: 30
Binding buffer/conditions: Binding Buffer For Assay: 25 mM Tris-HCl, 50 mM KCl, 200 mM NaCl, 0.2 mM EDTA, 5% [vol/vol] glycerol, 0.5 mM DTT, pH 7.5
Buffer type: Tris Buffers
pH: 7.5
Molecular weight of target: Not reported
Post-SELEX modifications: Not applicable
Application as quoted in the referenced paper: Therapeutic: " Analysis of bacterial type IVB pilus-host cell interactions, may yield information for the development of putative new drugs against S. enterica serovar Typhi bacterial infections, useful both in prevention of infection and in therapeutic treatment."
Reference (2005, Antimicrob Agents Chemother ): Pan, Q., Zhang, X. L., Wu, H. Y., He, P. W., Wang, F., Zhang, M. S., Hu, J. M., Xia, B., & Wu, J. (2005). Aptamers that preferentially bind type IVB pili and inhibit human monocytic-cell invasion by Salmonella enterica serovar typhi. Antimicrobial agents and chemotherapy, 49(10), 4052–4060. https://doi.org/10.1128/AAC.49.10.4052-4060.2005
Aptamer: R12-2
Target: RNase H domain of human immunodeficiency virus-1 reverse transcriptase (HIV-1 RT)
Type of nucleic acid: dsDNA
Sequence: 5'ATGCTTCCACGAGCCTTTCGGGGTTGGTGTACGGTGGCAGGCTGCGAGGCGGTAGTCTATTC3'
Sequence length: 62
GC content: 0.5967741935483871
Affinity: Kd: 70 nM
Pool type: 5'-ATGCTTCCACGAGCCTTTC-N22-CTGCGAGGCGGTAGTCTATTC-3'
Pool random region: 22
Binding buffer/conditions: 50 mM Tris-HCl, 1.25 mM MgCl2, 25-400 mM KCl and 10 mM DTT
Divalent salt: MgCl
Buffer type: Tris Buffers
Molecular weight of target: Not reported
Post-SELEX modifications: Not applicable
Application as quoted in the referenced paper: Therapeutic: " Aptamer S-PS8.4, selected here for affinity for type IVB pili, has strong potential both as an antagonist against S. enterica serovar Typhi invasion of human monocytic cells and as a tool to analyze the interactions of bacterial type IVB pili with host cells and examine important aspects of bacterial pathogenesis."
Reference (2005, Biochemistry ): Somasunderam, A., Ferguson, M. R., Rojo, D. R., Thiviyanathan, V., Li, X., O'Brien, W. A., & Gorenstein, D. G. (2005). Combinatorial selection, inhibition, and antiviral activity of DNA thioaptamers targeting the RNase H domain of HIV-1 reverse transcriptase. Biochemistry, 44(30), 10388–10395. https://doi.org/10.1021/bi0507074
Aptamer: clone A (wild type)
Target: Hemagglutinin influenza virus (HA influenza virus)
Type of nucleic acid: ssRNA
Sequence: 5'GGGAGAAUUCCGACCAGAAGGGUUAGCAGUCGGCAUGCGGUACAGACAGACCUUUCCUCUCUCCUUCCUCUUCU3'
Sequence length: 74
GC content: 0.5405405405405406
Affinity: Kd: 188 ± 36 pM
Pool type: 5'-AGGGGAGAAUUCCGACCAGAAG-N30-CCTTTCCTCTCTCCTTCCTCTTCT-2
37.5% Dopped pool:  5'-GGGAGAAUUCCGACCAGAAGGGUUAGCAGUCGGCAUGCGGUACAGACAGACCUUUCCUCUCUCCUUCCUCUUCU-3'
Pool random region: 30
Binding buffer/conditions: 0.01 M Hepes (pH 7.4), 0.15 M NaCl, 3 mM EDTA, and 0.005% Tween 20
Buffer type: Other Buffers
pH: 7.4
Molecular weight of target: Not reported
Post-SELEX modifications: Not applicable
Application as quoted in the referenced paper: Detection: " Enrichment of efficient RNA aptamers using SPR. We previously isolated an aptamer that binds to the hemagglutinin (HA) of human infuenza A/Panama/2007/1999 (H3N2) virus with high aYnity and speciWcity (unpublished data). To identify further the important region within the aptamer, and to definte the RNA consensus sequence for HA binding, we partially randomized the selected aptamer sequence and efficiently selected aptamers using Biacorebased in vitro selections. These studies not only revealed the high-aYnity RNA aptamer but also identified the consensus sequence for binding to the HA of an A strain influenza virus."
Reference (2005, Anal Biochem ): Misono, T. S., & Kumar, P. K. (2005). Selection of RNA aptamers against human influenza virus hemagglutinin using surface plasmon resonance. Analytical biochemistry, 342(2), 312–317. https://doi.org/10.1016/j.ab.2005.04.013
Aptamer: clone B
Target: Hemagglutinin influenza virus (HA influenza virus)
Type of nucleic acid: ssRNA
Sequence: 5'GGGAGAAUUCCGACCAGAAGGGUUAGCGGUCGUCUUAAGUAGUUUUUGGUCCUUUCCUCUCUCCUUCCUCUUCU3'
Sequence length: 74
GC content: 0.4864864864864865
Affinity: Kd: 115 ± 23 pM
Pool type: 5'-AGGGGAGAAUUCCGACCAGAAG-N30-CCTTTCCTCTCTCCTTCCTCTTCT-2
37.5% Dopped pool:  5'-GGGAGAAUUCCGACCAGAAGGGUUAGCAGUCGGCAUGCGGUACAGACAGACCUUUCCUCUCUCCUUCCUCUUCU-3'
Pool random region: 30
Binding buffer/conditions: 0.01 M Hepes (pH 7.4), 0.15 M NaCl, 3 mM EDTA, and 0.005% Tween 20
Buffer type: Other Buffers
pH: 7.4
Molecular weight of target: Not reported
Post-SELEX modifications: Not applicable
Application as quoted in the referenced paper: Detection: " Enrichment of efficient RNA aptamers using SPR. We previously isolated an aptamer that binds to the hemagglutinin (HA) of human infuenza A/Panama/2007/1999 (H3N2) virus with high aYnity and speciWcity (unpublished data). To identify further the important region within the aptamer, and to definte the RNA consensus sequence for HA binding, we partially randomized the selected aptamer sequence and efficiently selected aptamers using Biacorebased in vitro selections. These studies not only revealed the high-aYnity RNA aptamer but also identified the consensus sequence for binding to the HA of an A strain influenza virus."
Reference (2005, Anal Biochem ): Misono, T. S., & Kumar, P. K. (2005). Selection of RNA aptamers against human influenza virus hemagglutinin using surface plasmon resonance. Analytical biochemistry, 342(2), 312–317. https://doi.org/10.1016/j.ab.2005.04.013
Aptamer: ARC224
Target: Vascular endothelial growth factor (VEGF)
Type of nucleic acid: 2'-O-Me-RNA
Sequence: 5′CAUCGAUGCUAGUCGUAACGAUCCCGAUAUGCAGUUUGAGAAGUCGCGCAUUCGCGAGAACGUUCUCUCUCCCUAUAGUGAGUCGUAUUA3′
Sequence length: 90
GC content: 0.4777777777777778
Affinity: Kd: 3.9 nM
Pool type: 5′-CAUCGAUGCUAGUCGUAACGAUCC-N30-CGAGAACGUUCUCUCUCCCUAUAGUGAGUCGUAUUA-3′
Pool random region: 30
Binding buffer/conditions: PBS with 0.1 mg/ml tRNA and 1 mg/ml BSA in a silanized plate
Buffer type: PBS/phosphate buffers
pH: 7.4
Molecular weight of target: Not reported
Post-SELEX modifications: Not applicable
Application as quoted in the referenced paper: Therapeutic: " The utility of VEGF as a therapeutic target has additionally focused upon other angiogenesis disorders such as retinopathy and macular degeneration, for which an anti-VEGF aptamer (Macugen) was recently approved by the FDA. Aptamers that function as VEGF inhibitors offer many advantages as therapeutics, including the fact that they are generated by chemical synthesis and spontaneously refold after denaturation."
Additional information: Entirely comprised of 2′-OMe nucleotides (mrmy)
Reference (2005, Chem Biol ): Burmeister, P. E., Lewis, S. D., Silva, R. F., Preiss, J. R., Horwitz, L. R., Pendergrast, P. S., McCauley, T. G., Kurz, J. C., Epstein, D. M., Wilson, C., & Keefe, A. D. (2005). Direct in vitro selection of a 2'-O-methyl aptamer to VEGF. Chemistry & biology, 12(1), 25–33. https://doi.org/10.1016/j.chembiol.2004.10.017
Aptamer: ARC245
Target: Vascular endothelial growth factor (VEGF)
Type of nucleic acid: 2'-O-Me-RNA
Sequence: 5′CAUCGAUGCUAGUCGUAACGAUCCAUGCAGUUUGAGAAGUCGCGCAUCGAGAACGUUCUCUCUCCCUAUAGUGAGUCGUAUUA3′
Sequence length: 83
GC content: 0.4698795180722891
Affinity: Kd: 2.1 nM
Pool type: 5′-CAUCGAUGCUAGUCGUAACGAUCC-N30-CGAGAACGUUCUCUCUCCCUAUAGUGAGUCGUAUUA-3′
Pool random region: 30
Binding buffer/conditions: 40 μl PBS with 0.1 mg/ml tRNA and 1 mg/ml BSA in a silanized plate
Buffer type: PBS/phosphate buffers
pH: 7.4
Molecular weight of target: Not reported
Post-SELEX modifications: Minimized version of arc224
Application as quoted in the referenced paper: Therapeutic: " The utility of VEGF as a therapeutic target has additionally focused upon other angiogenesis disorders such as retinopathy and macular degeneration, for which an anti-VEGF aptamer (Macugen) was recently approved by the FDA. Aptamers that function as VEGF inhibitors offer many advantages as therapeutics, including the fact that they are generated by chemical synthesis and spontaneously refold after denaturation."
Additional information: Entirely comprised of 2′-OMe nucleotides (mrmy)
Reference (2005, Chem Biol ): Burmeister, P. E., Lewis, S. D., Silva, R. F., Preiss, J. R., Horwitz, L. R., Pendergrast, P. S., McCauley, T. G., Kurz, J. C., Epstein, D. M., Wilson, C., & Keefe, A. D. (2005). Direct in vitro selection of a 2'-O-methyl aptamer to VEGF. Chemistry & biology, 12(1), 25–33. https://doi.org/10.1016/j.chembiol.2004.10.017
Aptamer: CII-1-37
Target: Alpha-thrombin (α-thrombin), Human
Type of nucleic acid: 4'-thio-RNA
Sequence: 5′GGGAGAAGGGAAGUAACAGGUGGGCGCGUGAUUAUGUUUGUACGAAGACUGUGAGAAGAGGUGACGGUACCAG3′
Sequence length: 73
GC content: 0.5205479452054794
Affinity: Kd: 4.7 nM
Pool type: 5′-GGGAGAAGGGAAGTAACAGG-N30-GTGAGAAGAGGTGACGGTACCAG-3′
Pool random region: 30
Binding buffer/conditions: 50 mM Tris–HCl, pH 7.4, 100 mM NaCl, 1 mM MgCl 2 and 1 mM DTT
Divalent salt: MgCl
Buffer type: Tris Buffers
pH: 7.4
Molecular weight of target: Not reported
Post-SELEX modifications: Not applicable
Application as quoted in the referenced paper: Detection: " The synthesis of the triphosphates of 4'-thiouridine and 4'-thiocytidine, 4'-thioUTP (7; thioUTP) and 4'-thioCTP (8; thioCTP), and their utility for SELEX (systematic evolution of ligands by exponential enrichment) is described. The stability of the thioRNA toward RNase A was 50 times greater than that of the corresponding natural RNA. With these successful results in hand, we attempted the selection of thioRNA aptamers to human alpha-thrombin using thioUTP and thioCTP, and found a thioRNA aptamer with high binding affinity (K(d) = 4.7 nM)."
Additional information: Thio-RNA --> 4'-thio UTP & 4'- thio CTP, GTP, ATP 
Reference (2005, Nucleic Acids Res ): Kato, Y., Minakawa, N., Komatsu, Y., Kamiya, H., Ogawa, N., Harashima, H., & Matsuda, A. (2005). New NTP analogs: the synthesis of 4'-thioUTP and 4'-thioCTP and their utility for SELEX. Nucleic acids research, 33(9), 2942–2951. https://doi.org/10.1093/nar/gki578
Aptamer: CI-2-23
Target: Alpha-thrombin (α-thrombin), Human
Type of nucleic acid: 4'-thio-RNA
Sequence: 5′GGGAGAAGGGAAGUAACAGGUUUAGACCAAGGGGCGGGAUGAGGUGAGAAGAGGUGACGGUACCAG3′
Sequence length: 66
GC content: 0.5606060606060606
Affinity: Not reported
Pool type: 5′-GGGAGAAGGGAAGTAACAGG-N30-GTGAGAAGAGGTGACGGTACCAG-3′
Pool random region: 30
Binding buffer/conditions: 50 mM Tris–HCl, pH 7.4, 100 mM NaCl, 1 mM MgCl 2 and 1 mM DTT
Divalent salt: MgCl
Buffer type: Tris Buffers
pH: 7.4
Molecular weight of target: Not reported
Post-SELEX modifications: Not applicable
Application as quoted in the referenced paper: Detection: " The synthesis of the triphosphates of 4'-thiouridine and 4'-thiocytidine, 4'-thioUTP (7; thioUTP) and 4'-thioCTP (8; thioCTP), and their utility for SELEX (systematic evolution of ligands by exponential enrichment) is described. The stability of the thioRNA toward RNase A was 50 times greater than that of the corresponding natural RNA. With these successful results in hand, we attempted the selection of thioRNA aptamers to human alpha-thrombin using thioUTP and thioCTP, and found a thioRNA aptamer with high binding affinity (K(d) = 4.7 nM)."
Additional information: Thio-RNA --> 4'-thio UTP & 4'- thio CTP, GTP, ATP 
Reference (2005, Nucleic Acids Res ): Kato, Y., Minakawa, N., Komatsu, Y., Kamiya, H., Ogawa, N., Harashima, H., & Matsuda, A. (2005). New NTP analogs: the synthesis of 4'-thioUTP and 4'-thioCTP and their utility for SELEX. Nucleic acids research, 33(9), 2942–2951. https://doi.org/10.1093/nar/gki578
Aptamer: III-30
Target: Streptavidin
Type of nucleic acid: ssDNA
Sequence: 5′ATACCAGCTTATTCAATTCGGGGGGTACGTGCCCGTGTTGCTCGGCGGCCCCCTCGCTTATTTTTGTGTGCCCTTTAGATAGTAAGTGCAATCT3′
Sequence length: 94
GC content: 0.5106382978723404
Affinity: Kd: 65.5 ± 8.6 nM
Pool type: 5′-ATACCAGCTTATTCAATT-N60-AGATAGTAAGTGCAATCT-3′
Pool random region: 60
Binding buffer/conditions: 100 mmol L−1 NaCl, 20 mmol L−1 Tris-HCl pH 7.6, 2 mmol L−1 MgCl2, 5 mmol L−1 KCl, 1 mmol L−1 CaCl2, 0.02% Tween 20
Divalent salt: MgCl/CaCl
Buffer type: Tris Buffers
pH: 7.6
Molecular weight of target: Not reported
Post-SELEX modifications: Not applicable
Application as quoted in the referenced paper: Detection: " With FluMag-SELEX we have provided a methodological background for our objective of being able to select DNA aptamers for targets with very different properties and size. These aptamers will be applied as new biosensor receptors. In this work selection of streptavidin-specific aptamers by FluMag-SELEX is described. The streptavidin-specific aptamers will be used to check the surface occupancy of streptavidin-coated magnetic beads with biotinylated molecules after immobilization procedures."
Reference (2005, Anal Bioanal Chem ): Stoltenburg, R., Reinemann, C., & Strehlitz, B. (2005). FluMag-SELEX as an advantageous method for DNA aptamer selection. Analytical and bioanalytical chemistry, 383(1), 83–91. https://doi.org/10.1007/s00216-005-3388-9
Aptamer: IV-33
Target: Streptavidin
Type of nucleic acid: ssDNA
Sequence: 5′ATACCAGCTTATTCAATTACAATGTCGCTCTCCGCCGCAGGAGCATTGTCTGTCTTTATGCTTCTCTTTTTTGTTGCAGATAGTAAGTGCAATCT3′
Sequence length: 95
GC content: 0.4105263157894737
Affinity: Kd: 59.0 ± 7.5
Pool type: 5′-ATACCAGCTTATTCAATT-N60-AGATAGTAAGTGCAATCT-3′
Pool random region: 60
Binding buffer/conditions: 100 mmol L−1 NaCl, 20 mmol L−1 Tris-HCl pH 7.6, 2 mmol L−1 MgCl2, 5 mmol L−1 KCl, 1 mmol L−1 CaCl2, 0.02% Tween 20
Divalent salt: MgCl/CaCl
Buffer type: Tris Buffers
pH: 7.6
Molecular weight of target: Not reported
Post-SELEX modifications: Not applicable
Application as quoted in the referenced paper: Detection: " With FluMag-SELEX we have provided a methodological background for our objective of being able to select DNA aptamers for targets with very different properties and size. These aptamers will be applied as new biosensor receptors. In this work selection of streptavidin-specific aptamers by FluMag-SELEX is described. The streptavidin-specific aptamers will be used to check the surface occupancy of streptavidin-coated magnetic beads with biotinylated molecules after immobilization procedures."
Reference (2005, Anal Bioanal Chem ): Stoltenburg, R., Reinemann, C., & Strehlitz, B. (2005). FluMag-SELEX as an advantageous method for DNA aptamer selection. Analytical and bioanalytical chemistry, 383(1), 83–91. https://doi.org/10.1007/s00216-005-3388-9