RosettaCommons/UTexasAptamer huggingface dataset:
Aptamer: Apt2
Target: Prion protein rPrP23-231 (rPrPc) fused to glutathione S-transferase (GST), Recombinant Syrian golden hamster
Type of nucleic acid: ssRNA
Sequence: 5'GGAGCUCAGCCUUCACUGCAGCAAUGCGUUGUGUGGGAAUUUGAGGGACGAUGGGGAAGUGGGGACGAAUGACUCAUUGCCGCGGUAGGGUUGGCACCACGGUCGGAUCC3'
Sequence length: 110
GC content: 0.5909090909090909
Affinity: Not reported 
Pool type: 5'-GGAGCTCAGCCTT-CACTGC-N74-GGCACCACGGTCGGATCC-3'
Pool random region: 74
Binding buffer/conditions: 8 mM Na2HPO4–0.87 mM KH2PO4–136 mM NaCl–112.6 mM KCl–2 mM dithiothreitol–2 mM MgCl2
Divalent salt: MgCl
Buffer type: PBS/phosphate buffers
Molecular weight of target: 33 kDa
Application as quoted in the referenced paper: Research: " Specificity of the aptamer-PrP interaction was further confirmed by binding assays with antisense aptamer RNA or a mutant aptamer in which the guanosine residues in the G tetrad scaffold were replaced by uridine residues. The aptamers did not recognize PrP27-30 in brain homogenates from scrapie-infected mice. RNA aptamers may provide a first milestone in the development of a diagnostic assay for the detection of transmissible spongiform 
encephalopathies."
Additional information: The aptamers did not recognize the fusion partner GST or the fusion protein GST::rPrP90-231 (rPrP27-30), which lacks 67 amino acids from the PrP N terminus; pool was reported by (Famulok et al. 1994)
Reference (1997, J Virol ): Weiss, S., Proske, D., Neumann, M., Groschup, M. H., Kretzschmar, H. A., Famulok, M., & Winnacker, E. L. (1997). RNA aptamers specifically interact with the prion protein PrP. Journal of virology, 71(11), 8790–8797. https://doi.org/10.1128/JVI.71.11.8790-8797.1997
Aptamer: Apt3
Target: Prion protein rPrP23-231 (rPrPc) fused to glutathione S-transferase (GST), Recombinant Syrian golden hamster
Type of nucleic acid: ssRNA
Sequence: 5'GGAGCUCAGCCUUCACUGCUACCUUAGAGUAGGAGCGGGACGAGGGGUUGUUGGGACGUGGGUAUGAUCCAUACAUUAGGAAGCUGGUGAGCUGGCACCACGGUCGGAUCC3'
Sequence length: 111
GC content: 0.5765765765765766
Affinity: Not reported 
Pool type: 5'-GGAGCTCAGCCTT-CACTGC-N74-GGCACCACGGTCGGATCC-3'
Pool random region: 74
Binding buffer/conditions: 8 mM Na2HPO4–0.87 mM KH2PO4–136 mM NaCl–112.6 mM KCl–2 mM dithiothreitol–2 mM MgCl2
Divalent salt: MgCl
Buffer type: PBS/phosphate buffers
Molecular weight of target: 33 kDa
Application as quoted in the referenced paper: Research: " Specificity of the aptamer-PrP interaction was further confirmed by binding assays with antisense aptamer RNA or a mutant aptamer in which the guanosine residues in the G tetrad scaffold were replaced by uridine residues. The aptamers did not recognize PrP27-30 in brain homogenates from scrapie-infected mice. RNA aptamers may provide a first milestone in the development of a diagnostic assay for the detection of transmissible spongiform 
encephalopathies."
Additional information: The aptamers did not recognize the fusion partner GST or the fusion protein GST::rPrP90-231 (rPrP27-30), which lacks 67 amino acids from the PrP N terminus; pool was reported by (Famulok et al. 1994)
Reference (1997, J Virol ): Weiss, S., Proske, D., Neumann, M., Groschup, M. H., Kretzschmar, H. A., Famulok, M., & Winnacker, E. L. (1997). RNA aptamers specifically interact with the prion protein PrP. Journal of virology, 71(11), 8790–8797. https://doi.org/10.1128/JVI.71.11.8790-8797.1997
Aptamer: 70cam6
Target: Chloramphenicol (Cam)
Type of nucleic acid: ssRNA
Sequence: 5'GGGAAAAGCGAAUCAUACACAAGAAUGAAAAGGGCUGGCGAGACAUAUCCGCUGGGCAAUCAGAUUCGGAGCCGCACCACCCUCGAAGUAGACAGGGCAUAAGGUAUUUAAUUCCAUA3'
Sequence length: 118
GC content: 0.4830508474576271
Affinity: Kd: 2.1 ±  0.3 µM
Pool type: 5'-GGGAAAAGCGAAUCAUACACAAGA-N70-GGGCAUAAGGUAUUUAAUUCCAUA-3'
Pool random region: 70
Binding buffer/conditions: 20 mM MgCI2, 400 mM NaCI, 100 mM his-Tris pH 6.4.
Divalent salt: MgCl
Buffer type: Tris Buffers
pH: 6.4
Molecular weight of target: Not reported 
Application as quoted in the referenced paper: Research: " Expand our understanding of molecular recognition by RNA and to facilitate ribosomal modeling. Specifically, the antibiotic chloramphenicol (Cam) naturally binds bacterial ribosomes in the ‘peptidyl transferase loop' of 23s ribosomal RNA to inhibit peptide bond formation."
Reference (1997, Chem Biol ): Burke, D. H., Hoffman, D. C., Brown, A., Hansen, M., Pardi, A., & Gold, L. (1997). RNA aptamers to the peptidyl transferase inhibitor chloramphenicol. Chemistry & biology, 4(11), 833–843. https://doi.org/10.1016/s1074-5521(97)90116-2
Aptamer: 70cam9
Target: Chloramphenicol (Cam)
Type of nucleic acid: ssRNA
Sequence: 5'GGGAAAAGCGAAUCAUACACAAGAAGAGCUUGACGGUCCCGAGAGUCGAGCCCAAGCUGACACUGGACCUUUGCGGACCACGUGUUGAUCGUCGGGGCAUAAGGUAUUUAAUUCCAUA3'
Sequence length: 118
GC content: 0.5084745762711864
Affinity: Kd: 8 ±  4 µM
Pool type: 5'-GGGAAAAGCGAAUCAUACACAAGA-N70-GGGCAUAAGGUAUUUAAUUCCAUA-3'
Pool random region: 70
Binding buffer/conditions: 20 mM MgCI2, 400 mM NaCI, 100 mM his-Tris pH 6.4.
Divalent salt: MgCl
Buffer type: Tris Buffers
pH: 6.4
Molecular weight of target: Not reported 
Application as quoted in the referenced paper: Research: " Expand our understanding of molecular recognition by RNA and to facilitate ribosomal modeling. Specifically, the antibiotic chloramphenicol (Cam) naturally binds bacterial ribosomes in the ‘peptidyl transferase loop' of 23s ribosomal RNA to inhibit peptide bond formation."
Reference (1997, Chem Biol ): Burke, D. H., Hoffman, D. C., Brown, A., Hansen, M., Pardi, A., & Gold, L. (1997). RNA aptamers to the peptidyl transferase inhibitor chloramphenicol. Chemistry & biology, 4(11), 833–843. https://doi.org/10.1016/s1074-5521(97)90116-2
Aptamer: 70cam53
Target: Chloramphenicol (Cam)
Type of nucleic acid: ssRNA
Sequence: 5'GGGAAAAGCGAAUCAUACACAAGAGGCACCAAAGCUGAAGUAGCGGGAUAACUCAAAUUACUUUAGGUGUAUGAAGGUGAAACUAGCAAUGAAGGGCAUAAGGUAUUUAAUUCCAUA3'
Sequence length: 117
GC content: 0.3931623931623931
Affinity: Kd: 7 ±  2 µM
Pool type: 5'-GGGAAAAGCGAAUCAUACACAAGA-N70-GGGCAUAAGGUAUUUAAUUCCAUA-3'
Pool random region: 70
Binding buffer/conditions: 20 mM MgCI2, 400 mM NaCI, 100 mM his-Tris pH 6.4.
Divalent salt: MgCl
Buffer type: Tris Buffers
pH: 6.4
Molecular weight of target: Not reported 
Application as quoted in the referenced paper: Research: " Expand our understanding of molecular recognition by RNA and to facilitate ribosomal modeling. Specifically, the antibiotic chloramphenicol (Cam) naturally binds bacterial ribosomes in the ‘peptidyl transferase loop' of 23s ribosomal RNA to inhibit peptide bond formation."
Reference (1997, Chem Biol ): Burke, D. H., Hoffman, D. C., Brown, A., Hansen, M., Pardi, A., & Gold, L. (1997). RNA aptamers to the peptidyl transferase inhibitor chloramphenicol. Chemistry & biology, 4(11), 833–843. https://doi.org/10.1016/s1074-5521(97)90116-2
Aptamer: 80Cm50*
Target: Chloramphenicol (Cam)
Type of nucleic acid: ssRNA
Sequence: 5'GGGCAUAAGGUAUUUAAUUCCAUACGGCAGACGAGCCUUGACGAGCCAAUCUACACUUGGCGAUGACCGAUGGGCCCCAGCUACUUCUGGCAGUUUCGAUUCGUUUGAUUCGGAUGCUCGGUAGCUCAACUCG3'
Sequence length: 133
GC content: 0.518796992481203
Affinity: Kd: 25 ±  3 µM
Pool type: 5'-GGGCAUAAGGUAUUUAAUUCCAUA-N80-UUGAUUCGGAUGCUCGGUAGCUCAACUCG-3'
Pool random region: 80
Binding buffer/conditions: 20 mM MgCI2, 400 mM NaCI, 100 mM his-Tris pH 6.4.
Divalent salt: MgCl
Buffer type: Tris Buffers
pH: 6.4
Molecular weight of target: Not reported 
Application as quoted in the referenced paper: Research: " Expand our understanding of molecular recognition by RNA and to facilitate ribosomal modeling. Specifically, the antibiotic chloramphenicol (Cam) naturally binds bacterial ribosomes in the ‘peptidyl transferase loop' of 23s ribosomal RNA to inhibit peptide bond formation."
Reference (1997, Chem Biol ): Burke, D. H., Hoffman, D. C., Brown, A., Hansen, M., Pardi, A., & Gold, L. (1997). RNA aptamers to the peptidyl transferase inhibitor chloramphenicol. Chemistry & biology, 4(11), 833–843. https://doi.org/10.1016/s1074-5521(97)90116-2
Aptamer: BBS #8
Target: B52 protein
Type of nucleic acid: ssRNA
Sequence: 5'GGGAGAAUUCAACUGCCAUCUAGGCUGGUCAACCAGGCGACCGCCACCCGCGCGCGCAAUACCUAGUACUACAAGCUUCUGGACUCGGU3'
Sequence length: 89
GC content: 0.5842696629213483
Affinity: Kd: 20nM
Pool type: DNA Pool Version: 5'-ACCGAGTCCAGAAGCTTGTAGTACT-N40-GCCTAGATGGCAGTTGAATTCTCCCTATAGTGAGTCGTATTAC-3' & RNA Pool Version: 5'-GGGAGAAUUCAACUGCCAUCUAGGC-N40-AGUACUACAAGCUUCUGGACUCGGU-3'
Pool random region: 40
Binding buffer/conditions: 50 mM Tris-Cl [pH 7.6], 200 mM potassium acetate, 5 mM MgCl2, 2.5 mM dithiothreitol
Divalent salt: MgCl
Buffer type: Tris Buffers
pH: 7.6
Molecular weight of target: Not reported
Application as quoted in the referenced paper: Detection: " This has encouraged us to make use of BBS RNA as a genetic tool for dissecting B52 function in vivo, by creating Drosophila fly lines designed to overproduce BBS RNAs (40). We envision that the controlled and modulated expression of these RNA aptamers in living flies will serve as a specific, reversible, fast-acting B52 inhibitor that should provide insight into the function of B52 in vivo"
Additional information: The Drosophila SR protein B52 was cloned from an embryonic cDNA expression library by using a monoclonal antibody against a Drosophila protein associated with transcriptionally active loci on polytene chromosomes. The 59 constant sequence included a promoter for T7 RNA polymerase
Reference (1997, Mol Cell Biol ): Shi, H., Hoffman, B. E., & Lis, J. T. (1997). A specific RNA hairpin loop structure binds the RNA recognition motifs of the Drosophila SR protein B52. Molecular and cellular biology, 17(5), 2649–2657. https://doi.org/10.1128/MCB.17.5.2649
Aptamer: BBS #11
Target: B52 protein
Type of nucleic acid: ssRNA
Sequence: 5'GGGAGAAUUCAACUGCCAUCUAGGCUGCUCACGAGUCCAUGACCAGUACGAUCAACCAGGCGACAGUACUACAAGCUUCUGGACUCGGU3'
Sequence length: 89
GC content: 0.5280898876404494
Affinity: Not reported
Pool type: DNA Pool Version: 5'-ACCGAGTCCAGAAGCTTGTAGTACT-N40-GCCTAGATGGCAGTTGAATTCTCCCTATAGTGAGTCGTATTAC-3' & RNA Pool Version: 5'-GGGAGAAUUCAACUGCCAUCUAGGC-N40-AGUACUACAAGCUUCUGGACUCGGU-3'
Pool random region: 40
Binding buffer/conditions: 50 mM Tris-Cl [pH 7.6], 200 mM potassium acetate, 5 mM MgCl2, 2.5 mM dithiothreitol
Divalent salt: MgCl
Buffer type: Tris Buffers
pH: 7.6
Molecular weight of target: Not reported
Application as quoted in the referenced paper: Detection: " This has encouraged us to make use of BBS RNA as a genetic tool for dissecting B52 function in vivo, by creating Drosophila fly lines designed to overproduce BBS RNAs (40). We envision that the controlled and modulated expression of these RNA aptamers in living flies will serve as a specific, reversible, fast-acting B52 inhibitor that should provide insight into the function of B52 in vivo"
Additional information: *The Drosophila SR protein B52 was cloned from an embryonic cDNA expression library by using a monoclonal antibody against a Drosophila protein associated with transcriptionally active loci on polytene chromosomes. *The 59 constant sequence included a promoter for T7 RNA polymerase *Reproted random region is 39
Reference (1997, Mol Cell Biol ): Shi, H., Hoffman, B. E., & Lis, J. T. (1997). A specific RNA hairpin loop structure binds the RNA recognition motifs of the Drosophila SR protein B52. Molecular and cellular biology, 17(5), 2649–2657. https://doi.org/10.1128/MCB.17.5.2649
Aptamer: BBS #23
Target: B52 protein
Type of nucleic acid: ssRNA
Sequence: 5'GGGAGAAUUCAACUGCCAUCUAGGCCCAACUGCUAAGAAGCAUCCUGUACGAUCAACCCGGCGACAGUACUACAAGCUUCUGGACUCGGU3'
Sequence length: 90
GC content: 0.5222222222222223
Affinity: Not reported
Pool type: DNA Pool Version: 5'-ACCGAGTCCAGAAGCTTGTAGTACT-N40-GCCTAGATGGCAGTTGAATTCTCCCTATAGTGAGTCGTATTAC-3' & RNA Pool Version: 5'-GGGAGAAUUCAACUGCCAUCUAGGC-N40-AGUACUACAAGCUUCUGGACUCGGU-3'
Pool random region: 40
Binding buffer/conditions: 50 mM Tris-Cl [pH 7.6], 200 mM potassium acetate, 5 mM MgCl2, 2.5 mM dithiothreitol
Divalent salt: MgCl
Buffer type: Tris Buffers
pH: 7.6
Molecular weight of target: Not reported
Application as quoted in the referenced paper: Detection: " This has encouraged us to make use of BBS RNA as a genetic tool for dissecting B52 function in vivo, by creating Drosophila fly lines designed to overproduce BBS RNAs (40). We envision that the controlled and modulated expression of these RNA aptamers in living flies will serve as a specific, reversible, fast-acting B52 inhibitor that should provide insight into the function of B52 in vivo"
Additional information: The Drosophila SR protein B52 was cloned from an embryonic cDNA expression library by using a monoclonal antibody against a Drosophila protein associated with transcriptionally active loci on polytene chromosomes. The 59 constant sequence included a promoter for T7 RNA polymerase
Reference (1997, Mol Cell Biol ): Shi, H., Hoffman, B. E., & Lis, J. T. (1997). A specific RNA hairpin loop structure binds the RNA recognition motifs of the Drosophila SR protein B52. Molecular and cellular biology, 17(5), 2649–2657. https://doi.org/10.1128/MCB.17.5.2649
Aptamer: Trnc.A-30
Target: DNA polymerase (Taq pol), Thermus acquaticus
Type of nucleic acid: ssDNA
Sequence: 5'AAGACCAGACAATGTACAGTATTGGCCTGA3'
Sequence length: 30
GC content: 0.4333333333333333
Affinity: Kd: 0.6 ± 0.1 nM, IC50: 110 nM
Pool type: 5'-TTCTCGGTTGGTCTCTGGCGGAGC-N30-TCTTGTGTATGATTCGCTTTTCCC-3'
Pool random region: 30
Binding buffer/conditions: Not reported
Buffer type: Not Reported
Molecular weight of target: 94 kDa
Post-SELEX modifications: The aptamer sequence was truncated
Application as quoted in the referenced paper: Research- " These aptamers have been shown to effciently inhibit the polymerase activity of Taq pol and are useful in enhancing the amplifcation effciency of low copy number targets by the polymerase chain reaction (PCR). The efficiency of inhibition of Trunc-A-30 is less than that of the full length sequence (TQ30). Trunc.A-30 also inhibits the Stoffel fragment (61 kDa) more efficiently than Taq pol.This aptame does not inhibited Tth pol."
Reference (1997, J Mol Biol ): Lin, Y., & Jayasena, S. D. (1997). Inhibition of multiple thermostable DNA polymerases by a heterodimeric aptamer. Journal of molecular biology, 271(1), 100–111. https://doi.org/10.1006/jmbi.1997.1165
Aptamer: Trnc.A-30
Target: Stoffel fragment
Type of nucleic acid: ssDNA
Sequence: 5'AAGACCAGACAATGTACAGTATTGGCCTGA3'
Sequence length: 30
GC content: 0.4333333333333333
Affinity: Kd: 7.7 nM
Pool type: 5'-TTCTCGGTTGGTCTCTGGCGGAGC-N30-TCTTGTGTATGATTCGCTTTTCCC-3'
Pool random region: 30
Binding buffer/conditions: Not reported
Buffer type: Not Reported
Molecular weight of target: 61 kDa
Post-SELEX modifications: The aptamer sequence was truncated
Application as quoted in the referenced paper: Research- " These aptamers have been shown to effciently inhibit the polymerase activity of Taq pol and are useful in enhancing the amplifcation effciency of low copy number targets by the polymerase chain reaction (PCR). The efficiency of inhibition of Trunc-A-30 is less than that of the full length sequence (TQ30). Trunc.A-30 also inhibits the Stoffel fragment (61 kDa) more efficiently than Taq pol.This aptamer does not inhibited Tth pol."
Reference (1997, J Mol Biol ): Lin, Y., & Jayasena, S. D. (1997). Inhibition of multiple thermostable DNA polymerases by a heterodimeric aptamer. Journal of molecular biology, 271(1), 100–111. https://doi.org/10.1006/jmbi.1997.1165
Aptamer: Trnc.2-30
Target: DNA polymerase (Taq pol), Thermus acquaticus
Type of nucleic acid: ssDNA
Sequence: 5'GCCGGCCAATGTACAGTATTGGCCGGC3'
Sequence length: 27
GC content: 0.6296296296296297
Affinity: Kd: 3.1 ± 0.3 nM, IC50: 152 nM
Pool type: 5'-TTCTCGGTTGGTCTCTGGCGGAGC-N30-TCTTGTGTATGATTCGCTTTTCCC-3'
Pool random region: 30
Binding buffer/conditions: Not reported
Buffer type: Not Reported
Molecular weight of target: 94 kDa
Post-SELEX modifications: The aptamer sequence was truncated
Application as quoted in the referenced paper: Research- " These aptamers have been shown to effciently inhibit the polymerase activity of Taq pol and are useful in enhancing the amplifcation effciency of low copy number targets by the polymerase chain reaction (PCR). Trnc.2-30 inhibited both Taq pol and the Stoffel fragment; the latter more effectively. However, it failed to inhibit Tth pol."
Reference (1997, J Mol Biol ): Lin, Y., & Jayasena, S. D. (1997). Inhibition of multiple thermostable DNA polymerases by a heterodimeric aptamer. Journal of molecular biology, 271(1), 100–111. https://doi.org/10.1006/jmbi.1997.1165
Aptamer: Trnc.2-30
Target: Stoffel fragment
Type of nucleic acid: ssDNA
Sequence: 5'GCCGGCCAATGTACAGTATTGGCCGGC3'
Sequence length: 27
GC content: 0.6296296296296297
Affinity: Kd: 5.9 nM, IC50: 152 nM
Pool type: 5'-TTCTCGGTTGGTCTCTGGCGGAGC-N30-TCTTGTGTATGATTCGCTTTTCCC-3'
Pool random region: 30
Binding buffer/conditions: Not reported
Buffer type: Not Reported
Molecular weight of target: 61 kDa
Post-SELEX modifications: The aptamer sequence was truncated
Application as quoted in the referenced paper: Research- " These aptamers have been shown to effciently inhibit the polymerase activity of Taq pol and are useful in enhancing the amplifcation effciency of low copy number targets by the polymerase chain reaction (PCR). Trnc.2-30 inhibited both Taq pol and the Stoffel fragment; the latter more effectively. However, it failed to inhibit Tth pol."
Reference (1997, J Mol Biol ): Lin, Y., & Jayasena, S. D. (1997). Inhibition of multiple thermostable DNA polymerases by a heterodimeric aptamer. Journal of molecular biology, 271(1), 100–111. https://doi.org/10.1006/jmbi.1997.1165
Aptamer: Trnc-21
Target: DNA polymerase (Taq pol), Thermus acquaticus
Type of nucleic acid: ssDNA
Sequence: 5'TGGCGGAGCGATCATCTCAGAGCATTCTTAGCGTTTTGTTCTTGTGTATGA3'
Sequence length: 51
GC content: 0.4509803921568627
Affinity: Kd: 9 ±  1pM, IC50: 21nM
Pool type: 5'-TTCTCGGTTGGTCTCTGGCGGAGC-N30-TCTTGTGTATGATTCGCTTTTCCC-3'
Pool random region: 30
Binding buffer/conditions: Not reported
Buffer type: Not Reported
Molecular weight of target: 94 kDa
Post-SELEX modifications: The aptamer sequence was truncated
Application as quoted in the referenced paper: Research- " These aptamers have been shown to effciently inhibit the polymerase activity of Taq pol and are useful in enhancing the amplifcation effciency of low copy number targets by the polymerase chain reaction (PCR). TQ21 aptamer inhibited both Taq and Tth polymerases, but did not inhibit the Stoffel fragment."
Reference (1997, J Mol Biol ): Lin, Y., & Jayasena, S. D. (1997). Inhibition of multiple thermostable DNA polymerases by a heterodimeric aptamer. Journal of molecular biology, 271(1), 100–111. https://doi.org/10.1006/jmbi.1997.1165
Aptamer: Trnc-21
Target: DNA polymerase (Tth pol), Thermus thermophilus (Tth)
Type of nucleic acid: ssDNA
Sequence: 5'TGGCGGAGCGATCATCTCAGAGCATTCTTAGCGTTTTGTTCTTGTGTATGA3'
Sequence length: 51
GC content: 0.4509803921568627
Affinity: Kd: 40 ± 10 pM, IC50: 35 nM
Pool type: 5'-TTCTCGGTTGGTCTCTGGCGGAGC-N30-TCTTGTGTATGATTCGCTTTTCCC-3'
Pool random region: 30
Binding buffer/conditions: Not reported
Buffer type: Not Reported
Molecular weight of target: 94 kDa
Post-SELEX modifications: The aptamer sequence was truncated
Application as quoted in the referenced paper: Research- " These aptamers have been shown to effciently inhibit the polymerase activity of Taq pol and are useful in enhancing the amplifcation effciency of low copy number targets by the polymerase chain reaction (PCR). TQ21 aptamer inhibited both Taq and Tth polymerases, but did not inhibit the Stoffel fragment."
Reference (1997, J Mol Biol ): Lin, Y., & Jayasena, S. D. (1997). Inhibition of multiple thermostable DNA polymerases by a heterodimeric aptamer. Journal of molecular biology, 271(1), 100–111. https://doi.org/10.1006/jmbi.1997.1165
Aptamer: D.21-D.30
Target: DNA polymerase (Taq pol), Thermus acquaticus
Type of nucleic acid: ssDNA
Sequence: 5'TGGCGGAGCGATCATCTCAGAGCATTCTTAGCGTTTTGTTCTTGTGTATGATTTGCCGGCCAATGTACAGTATTGGCCGGC3'
Sequence length: 81
GC content: 0.4938271604938271
Affinity: Kd:10 pM, IC50: 30 nM
Pool type: 5'-TTCTCGGTTGGTCTCTGGCGGAGC-N30-TCTTGTGTATGATTCGCTTTTCCC-3'
Pool random region: 30
Binding buffer/conditions: Not reported
Buffer type: Not Reported
Molecular weight of target: 94 kDa
Application as quoted in the referenced paper: Research- " These aptamers have been shown to effciently inhibit the polymerase activity of Taq pol and are useful in enhancing the amplifcation effciency of low copy number targets by the polymerase chain reaction (PCR). Aptamer that effectively inhibited all three polymerases and were shown to be useful in detecting a low copy number target by PCR amplifcation. However, the additon of D.21 decreased the inhibitory potency of the Stoffel fragment as compared to D.30 alone."
Additional information: Truncated aptamers derived from two parent (Trnc.2-30 and Trnc-21) ligands from both families were combined to form a heterodimeric aptamer.
Reference (1997, J Mol Biol ): Lin, Y., & Jayasena, S. D. (1997). Inhibition of multiple thermostable DNA polymerases by a heterodimeric aptamer. Journal of molecular biology, 271(1), 100–111. https://doi.org/10.1006/jmbi.1997.1165
Aptamer: D.21-D.30
Target: DNA polymerase (Tth pol), Thermus thermophilus (Tth)
Type of nucleic acid: ssDNA
Sequence: 5'TGGCGGAGCGATCATCTCAGAGCATTCTTAGCGTTTTGTTCTTGTGTATGATTTGCCGGCCAATGTACAGTATTGGCCGGC3'
Sequence length: 81
GC content: 0.4938271604938271
Affinity: IC50: 36nM
Pool type: 5'-TTCTCGGTTGGTCTCTGGCGGAGC-N30-TCTTGTGTATGATTCGCTTTTCCC-3'
Pool random region: 30
Binding buffer/conditions: Not reported
Buffer type: Not Reported
Molecular weight of target: 94 kDa
Application as quoted in the referenced paper: Research- " These aptamers have been shown to effciently inhibit the polymerase activity of Taq pol and are useful in enhancing the amplifcation effciency of low copy number targets by the polymerase chain reaction (PCR). Aptamer that effectively inhibited all three polymerases and were shown to be useful in detecting a low copy number target by PCR amplifcation. However, the additon of D.21 decreased the inhibitory potency of the Stoffel fragment as compared to D.30 alone."
Additional information: Truncated aptamers derived from two parent (Trnc.2-30 and Trnc-21) ligands from both families were combined to form a heterodimeric aptamer.
Reference (1997, J Mol Biol ): Lin, Y., & Jayasena, S. D. (1997). Inhibition of multiple thermostable DNA polymerases by a heterodimeric aptamer. Journal of molecular biology, 271(1), 100–111. https://doi.org/10.1006/jmbi.1997.1165
Aptamer: g18_4.seq
Target: RNA stem-loop target (5'GCACGGTGCTGCTGAGATGCCCGT3')
Type of nucleic acid: ssRNA
Sequence: 5'GGGAGAAUUCCGACCAGAAGCUUCCGAAGCAUUCCGGCGUAGGGGUCUGUGCGCAAAACCAUCGGCCCUGGUGCCUAUGUGCGUCUACAUGGAUCCUCA3'
Sequence length: 99
GC content: 0.5757575757575758
Affinity: Kd: 70 ± 15 nM
Pool type: 5'-GGGAGAAUUCCGACCAGAAGCUU-N50-CCUAUGUGCGUCUACAUGGAUCCUCA-3'
Pool random region: 50
Binding buffer/conditions: 10 mM TrisCl, pH 8.3/25 mM MgCl2/l00 mM NaCl/165 mM KCl
Divalent salt: MgCl
Buffer type: Tris Buffers
pH: 8.3
Molecular weight of target: Not reported
Application as quoted in the referenced paper: Detection: " The winning aptamers described here are analogous to a conventional or monoclonal antibody in their ability to distinguish the presence of a domain in a larger molecule. They could be valuable in studies of the architecture or assembly of larger (e.g., catalytic) RNAs. The methods of combinatorial selection and counterselection described here should allow RNA aptamers capable of specific RNA recognition to be generated with relative ease."
Reference (1997, Bioorg Med Chem ): Cho, B., Taylor, D. C., Nicholas, H. B., Jr, & Schmidt, F. J. (1997). Interacting RNA species identified by combinatorial selection. Bioorganic & medicinal chemistry, 5(6), 1107–1113. https://doi.org/10.1016/s0968-0896(97)00046-1