RosettaCommons/UTexasAptamer huggingface dataset:
Aptamer: DD18
Target: Neutrophil elastase (NE)
Type of nucleic acid: ssDNA
Sequence: 5'CACGATGGTTAGGCGGGCCTTGAGGCTAATAATGTTGTTA3'
Sequence length: 40
GC content: 0.475
Affinity: Not reported 
Pool type: 5'-GGGAGGACGATGCGG-N40-CAGACGACGAGCGGA-3'
Pool random region: 40
Binding buffer/conditions: HBSS/0.01% hSA/25mM HEPES, pH 7.5, for neutrophil SELEX, the same buffer plus 100 mM NaCl for high-salt SELEX)
Buffer type: Other Buffers
pH: 7.5
Molecular weight of target: Not reported
Post-SELEX modifications: Truncation:the three 5‘-terminal nucleotides were removed from all truncates, leaving intact the full 12 bp splint-fixed region double helix. No more nucleotides were removed from the 5‘ end, and progressively shorter inhibitors were synthesized by omission of 3‘ terminal nucleotides. All sequences were initially synthesized with the 3‘ fixed region removed, yielding inhibitors of length 51 or 52.
Application as quoted in the referenced paper: Therapeutic: "The development of NE inhibitors as therapeutic agents has been pursued by a variety of strategies, including the identification and production of endogenous inhibitors and the synthesis and screening of smaller organic molecules"
Additional information: Sequence selected from high-salt SELEX
Reference (1997, Biochemistry ): Charlton, J., Kirschenheuter, G. P., & Smith, D. (1997). Highly potent irreversible inhibitors of neutrophil elastase generated by selection from a randomized DNA-valine phosphonate library. Biochemistry, 36(10), 3018–3026. https://doi.org/10.1021/bi962669h
Aptamer: ED1
Target: Neutrophil elastase (NE)
Type of nucleic acid: ssDNA
Sequence: 5'CAGCGTCATTTAGGATTCGTCAGGTTCTACCCGTAGTGTG3'
Sequence length: 40
GC content: 0.5
Affinity: Not reported 
Pool type: 5'-GGGAGGACGATGCGG-N40-CAGACGACGAGCGGA-3'
Pool random region: 40
Binding buffer/conditions: HBSS/0.01% hSA/25mM HEPES, pH 7.5, for neutrophil SELEX, the same buffer plus 100 mM NaCl for high-salt SELEX)
Buffer type: Other Buffers
pH: 7.5
Molecular weight of target: Not reported
Post-SELEX modifications: Truncation:the three 5‘-terminal nucleotides were removed from all truncates, leaving intact the full 12 bp splint-fixed region double helix. No more nucleotides were removed from the 5‘ end, and progressively shorter inhibitors were synthesized by omission of 3‘ terminal nucleotides. All sequences were initially synthesized with the 3‘ fixed region removed, yielding inhibitors of length 51 or 52.
Application as quoted in the referenced paper: Therapeutic: "The development of NE inhibitors as therapeutic agents has been pursued by a variety of strategies, including the identification and production of endogenous inhibitors and the synthesis and screening of smaller organic molecules"
Additional information: Sequence selected from neutrophil SELEX
Reference (1997, Biochemistry ): Charlton, J., Kirschenheuter, G. P., & Smith, D. (1997). Highly potent irreversible inhibitors of neutrophil elastase generated by selection from a randomized DNA-valine phosphonate library. Biochemistry, 36(10), 3018–3026. https://doi.org/10.1021/bi962669h
Aptamer: ED45
Target: Neutrophil elastase (NE)
Type of nucleic acid: ssDNA
Sequence: 5'CCTGCGTAACAACGCGGAGGAAACTTCCCTCCTATCTCT3'
Sequence length: 39
GC content: 0.5384615384615384
Affinity: Not reported 
Pool type: 5'-GGGAGGACGATGCGG-N40-CAGACGACGAGCGGA-3'
Pool random region: 40
Binding buffer/conditions: HBSS/0.01% hSA/25mM HEPES, pH 7.5, for neutrophil SELEX, the same buffer plus 100 mM NaCl for high-salt SELEX)
Buffer type: Other Buffers
pH: 7.5
Molecular weight of target: Not reported
Post-SELEX modifications: Truncation:the three 5‘-terminal nucleotides were removed from all truncates, leaving intact the full 12 bp splint-fixed region double helix. No more nucleotides were removed from the 5‘ end, and progressively shorter inhibitors were synthesized by omission of 3‘ terminal nucleotides. All sequences were initially synthesized with the 3‘ fixed region removed, yielding inhibitors of length 51 or 52.
Application as quoted in the referenced paper: Therapeutic: "The development of NE inhibitors as therapeutic agents has been pursued by a variety of strategies, including the identification and production of endogenous inhibitors and the synthesis and screening of smaller organic molecules"
Additional information: Sequence selected from neutrophil SELEX
Reference (1997, Biochemistry ): Charlton, J., Kirschenheuter, G. P., & Smith, D. (1997). Highly potent irreversible inhibitors of neutrophil elastase generated by selection from a randomized DNA-valine phosphonate library. Biochemistry, 36(10), 3018–3026. https://doi.org/10.1021/bi962669h
Aptamer: DD7
Target: Neutrophil elastase (NE)
Type of nucleic acid: ssDNA
Sequence: 5'GACTGCGTATCAACGCGGTGAAACCTAACCTCATCTTGAT3'
Sequence length: 40
GC content: 0.475
Affinity: Not reported 
Pool type: 5'-GGGAGGACGATGCGG-N40-CAGACGACGAGCGGA-3'
Pool random region: 40
Binding buffer/conditions: HBSS/0.01% hSA/25mM HEPES, pH 7.5, for neutrophil SELEX, the same buffer plus 100 mM NaCl for high-salt SELEX)
Buffer type: Other Buffers
pH: 7.5
Molecular weight of target: Not reported
Post-SELEX modifications: Truncation:the three 5‘-terminal nucleotides were removed from all truncates, leaving intact the full 12 bp splint-fixed region double helix. No more nucleotides were removed from the 5‘ end, and progressively shorter inhibitors were synthesized by omission of 3‘ terminal nucleotides. All sequences were initially synthesized with the 3‘ fixed region removed, yielding inhibitors of length 51 or 52.
Application as quoted in the referenced paper: Therapeutic: "The development of NE inhibitors as therapeutic agents has been pursued by a variety of strategies, including the identification and production of endogenous inhibitors and the synthesis and screening of smaller organic molecules"
Additional information: Sequence selected from high-salt SELEX
Reference (1997, Biochemistry ): Charlton, J., Kirschenheuter, G. P., & Smith, D. (1997). Highly potent irreversible inhibitors of neutrophil elastase generated by selection from a randomized DNA-valine phosphonate library. Biochemistry, 36(10), 3018–3026. https://doi.org/10.1021/bi962669h
Aptamer: ED38
Target: Neutrophil elastase (NE)
Type of nucleic acid: ssDNA
Sequence: 5'CACGGTAGTGCTACCAGATGGTTATGTTACTTCAATTCTG3'
Sequence length: 40
GC content: 0.425
Affinity: Not reported 
Pool type: 5'-GGGAGGACGATGCGG-N40-CAGACGACGAGCGGA-3'
Pool random region: 40
Binding buffer/conditions: HBSS/0.01% hSA/25mM HEPES, pH 7.5, for neutrophil SELEX, the same buffer plus 100 mM NaCl for high-salt SELEX)
Buffer type: Other Buffers
pH: 7.5
Molecular weight of target: Not reported
Post-SELEX modifications: Truncation:the three 5‘-terminal nucleotides were removed from all truncates, leaving intact the full 12 bp splint-fixed region double helix. No more nucleotides were removed from the 5‘ end, and progressively shorter inhibitors were synthesized by omission of 3‘ terminal nucleotides. All sequences were initially synthesized with the 3‘ fixed region removed, yielding inhibitors of length 51 or 52.
Application as quoted in the referenced paper: Therapeutic: "The development of NE inhibitors as therapeutic agents has been pursued by a variety of strategies, including the identification and production of endogenous inhibitors and the synthesis and screening of smaller organic molecules"
Additional information: Sequence selected from neutrophil SELEX
Reference (1997, Biochemistry ): Charlton, J., Kirschenheuter, G. P., & Smith, D. (1997). Highly potent irreversible inhibitors of neutrophil elastase generated by selection from a randomized DNA-valine phosphonate library. Biochemistry, 36(10), 3018–3026. https://doi.org/10.1021/bi962669h
Aptamer: DD25
Target: Neutrophil elastase (NE)
Type of nucleic acid: ssDNA
Sequence: 5'CATGACAGAATGTCTGCAGAGCTAATCTTGGTCACTGAT3'
Sequence length: 39
GC content: 0.4358974358974359
Affinity: Not reported 
Pool type: 5'-GGGAGGACGATGCGG-N40-CAGACGACGAGCGGA-3'
Pool random region: 40
Binding buffer/conditions: HBSS/0.01% hSA/25mM HEPES, pH 7.5, for neutrophil SELEX, the same buffer plus 100 mM NaCl for high-salt SELEX)
Buffer type: Other Buffers
pH: 7.5
Molecular weight of target: Not reported
Post-SELEX modifications: Truncation:the three 5‘-terminal nucleotides were removed from all truncates, leaving intact the full 12 bp splint-fixed region double helix. No more nucleotides were removed from the 5‘ end, and progressively shorter inhibitors were synthesized by omission of 3‘ terminal nucleotides. All sequences were initially synthesized with the 3‘ fixed region removed, yielding inhibitors of length 51 or 52.
Application as quoted in the referenced paper: Therapeutic: "The development of NE inhibitors as therapeutic agents has been pursued by a variety of strategies, including the identification and production of endogenous inhibitors and the synthesis and screening of smaller organic molecules"
Additional information: Sequence selected from high-salt SELEX
Reference (1997, Biochemistry ): Charlton, J., Kirschenheuter, G. P., & Smith, D. (1997). Highly potent irreversible inhibitors of neutrophil elastase generated by selection from a randomized DNA-valine phosphonate library. Biochemistry, 36(10), 3018–3026. https://doi.org/10.1021/bi962669h
Aptamer: Aptamer 5
Target: Nonpancreatic secretory phospholipase A2 (hnps-PLA2), Human
Type of nucleic acid: 2'-amino-RNA
Sequence: 5‘GGGAAAAGCGAAUCAUACACAAGACGGCCGGCGCCAUAGCCGAGAUCCGAGGUGUUGAACGAUGACAACUCGGUGCUCCGCCAGAGACCAACCGAGAA3‘
Sequence length: 98
GC content: 0.5714285714285714
Affinity: Kd: 0.5 ± 0.3, Ki: 0.2 nM 
Pool type: 5′-GGGAAAAGCGAATCATACACAAG-N50-GCTCCGCCAGAGACCAACCGAGAA-3′
Pool random region: 50
Binding buffer/conditions: 25 mM Tris, pH 7.4, 150 mM NaCl, 5 mM CaCl2
Divalent salt: CaCl
Buffer type: Tris Buffers
pH: 7.4
Molecular weight of target: 13.9 Kda
Post-SELEX modifications: The sequences of synthetic ssdnas were derived from aptamer 5 (table 1).
Application as quoted in the referenced paper: Research: " Dramatically elevated levels of circulating hnps-PLA2 are associated with numerous disease states, such as acute pancreatitis, adult respiratory distress syndrome (ARDS), bacterial peritonitis, and septic shock; Two factors that have hindered efforts to define the role of hnps-PLA2 are the existence of multiple enzymes with phospholipase A2 activity and the lack of specific, high-affinity antagonists. Such antagonists are deemed essential for deciphering the biological role(s) of hnps-PLA2."
Additional information: RNA library contains 2'-NH2-pyrimidines and 2'-OH-purines
Reference (1998, J Med Chem ): Bridonneau, P., Chang, Y. F., O'Connell, D., Gill, S. C., Snyder, D. W., Johnson, L., Goodson, T., Jr, Herron, D. K., & Parma, D. H. (1998). High-affinity aptamers selectively inhibit human nonpancreatic secretory phospholipase A2 (hnps-PLA2). Journal of medicinal chemistry, 41(6), 778–786. https://doi.org/10.1021/jm970579k
Aptamer: Aptamer 15
Target: Nonpancreatic secretory phospholipase A2 (hnps-PLA2), Human
Type of nucleic acid: 2'-amino-RNA
Sequence: 5'GGGAAAAGAGACGGCCGGCGCCAUAGCCGAGAUCCGAGGUGUUGCCGAGAA3'
Sequence length: 51
GC content: 0.6274509803921569
Affinity: Kd: 1.7 ± 0.2 nM, IC50: 4 nM, Ki: 0.14 nM 
Pool type: 5′-GGGAAAAGCGAATCATACACAAG-N50-GCTCCGCCAGAGACCAACCGAGAA-3′
Pool random region: 50
Binding buffer/conditions: 25 mM Tris, pH 7.4, 150 mM NaCl, 5 mM CaCl2
Divalent salt: CaCl
Buffer type: Tris Buffers
pH: 7.4
Molecular weight of target: 13.9 Kda
Post-SELEX modifications: The sequences of synthetic ssdnas were derived from aptamer 5 (table 1). In turn, the sequence of aptamer 15 is determined by the synthetic template. The sequence has been trucated
Application as quoted in the referenced paper: Research: " Dramatically elevated levels of circulating hnps-PLA2 are associated with numerous disease states, such as acute pancreatitis, adult respiratory distress syndrome (ARDS), bacterial peritonitis, and septic shock; Two factors that have hindered efforts to define the role of hnps-PLA2 are the existence of multiple enzymes with phospholipase A2 activity and the lack of specific, high-affinity antagonists. Such antagonists are deemed essential for deciphering the biological role(s) of hnps-PLA2."
Additional information: RNA library contains 2'-NH2-pyrimidines and 2'-OH-purines
Reference (1998, J Med Chem ): Bridonneau, P., Chang, Y. F., O'Connell, D., Gill, S. C., Snyder, D. W., Johnson, L., Goodson, T., Jr, Herron, D. K., & Parma, D. H. (1998). High-affinity aptamers selectively inhibit human nonpancreatic secretory phospholipase A2 (hnps-PLA2). Journal of medicinal chemistry, 41(6), 778–786. https://doi.org/10.1021/jm970579k
Aptamer: XBA RNA
Target: Xanthine (2,6-dioxypurine)
Type of nucleic acid: ssRNA
Sequence: 5'GGCACGUGUAUUACCCUAGUGGUCGACGUGCC3'
Sequence length: 32
GC content: 0.59375
Affinity: Kd: 3.3 µM
Pool type: 5'-GGTGAGAATTCCGACCAGGATCC-N60-GTCGACGTAGAAGCTTGGGCGG-3'
Pool random region: 60
Binding buffer/conditions: 20 mM Tris–HCl, pH 7.5, 0.3 M NaCl and 5 mM MgCl2
Divalent salt: MgCl
Buffer type: Tris Buffers
pH: 7.5
Molecular weight of target: Not reported
Post-SELEX modifications: Turnction: We designed the 32mer RNA (designated as XBA) shown inFigure 3B, which has the common secondary structure, including the consensus sequence, of the 60mer aptamers
Application as quoted in the referenced paper: Research: " To further explore this ability of RNA to recognize purine bases and/or the purine base moiety of nucleosides. The special elongation factor SelB of Escherichia coli promotes selenocysteine incorporation into formate dehydrogenases. By in vitro selection, novel RNA sequences ("aptamers"), which can interact tightly and specifically with SelB, were isolated from an RNA library. The library was comprised of mutagenized variants of the wild-type fdhF mRNA hairpin.This finding implies functions of the fdhF hairpin that go beyond the mere tethering of selenocysteyl-tRNASec to the UGA codon."
Additional information: A single-stranded DNA (105 nt), consisting of a random sequence of 60 nt and two flanking primer-binding regions (23 and 22 nt) for PCR and reverse transcription, was chemically synthesized with a Cyclone plus DNA/RNA synthesizer (Millipore). The PCR primers, with the sequences of 5′-AGTAATACGACTCACTA_x0002_TAGGTGAGAATTCCGACCAGGATCC-3′, (the T7 promoter sequence is underlined) and 5′-CCGCCCAAGCTTCTACGTC_x0002_GAC-3′, were also synthesized

We designed the 32mer RNA (designated as XBA) shown inFigure 3B, which has the common secondary structure, including the consensus sequence, of the 60mer aptamers

DNA library/pool was used as a template to generate the RNA pool used in the selection. A T7 promoter sequence might be necessary to use this DNA library/pool as a template to generate the RNA pool in the selection.
Reference (1998,Nucleic Acids Res): Kiga, D., Futamura, Y., Sakamoto, K., & Yokoyama, S. (1998). An RNA aptamer to the xanthine/guanine base with a distinctive mode of purine recognition. Nucleic Acids Research, 26(7), 1755–1760. https://doi.org/10.1093/nar/26.7.1755
Aptamer: XBA RNA
Target: Guanine
Type of nucleic acid: ssRNA
Sequence: 5'GGCACGUGUAUUACCCUAGUGGUCGACGUGCC3'
Sequence length: 32
GC content: 0.59375
Affinity: Kd: 1.3 µM
Pool type: 5'-GGTGAGAATTCCGACCAGGATCC-N60-GTCGACGTAGAAGCTTGGGCGG-3'
Pool random region: 60
Binding buffer/conditions: 20 mM Tris–HCl, pH 7.5, 0.3 M NaCl and 5 mM MgCl2
Divalent salt: MgCl
Buffer type: Tris Buffers
pH: 7.5
Molecular weight of target: Not reported
Application as quoted in the referenced paper: Research: " To further explore this ability of RNA to recognize purine bases and/or the purine base moiety of nucleosides. The special elongation factor SelB of Escherichia coli promotes selenocysteine incorporation into formate dehydrogenases. By in vitro selection, novel RNA sequences ("aptamers"), which can interact tightly and specifically with SelB, were isolated from an RNA library. The library was comprised of mutagenized variants of the wild-type fdhF mRNA hairpin.This finding implies functions of the fdhF hairpin that go beyond the mere tethering of selenocysteyl-tRNASec to the UGA codon."
Additional information: A single-stranded DNA (105 nt), consisting of a random sequence of 60 nt and two flanking primer-binding regions (23 and 22 nt) for PCR and reverse transcription, was chemically synthesized with a Cyclone plus DNA/RNA synthesizer (Millipore). The PCR primers, with the sequences of 5′-AGTAATACGACTCACTA_x0002_TAGGTGAGAATTCCGACCAGGATCC-3′, (the T7 promoter sequence is underlined) and 5′-CCGCCCAAGCTTCTACGTC_x0002_GAC-3′, were also synthesized

We designed the 32mer RNA (designated as XBA) shown inFigure 3B, which has the common secondary structure, including the consensus sequence, of the 60mer aptamers

DNA library/pool was used as a template to generate the RNA pool used in the selection. A T7 promoter sequence might be necessary to use this DNA library/pool as a template to generate the RNA pool in the selection.
Reference (1998,Nucleic Acids Res): Kiga, D., Futamura, Y., Sakamoto, K., & Yokoyama, S. (1998). An RNA aptamer to the xanthine/guanine base with a distinctive mode of purine recognition. Nucleic Acids Research, 26(7), 1755–1760. https://doi.org/10.1093/nar/26.7.1755
Aptamer: APC-167
Target: Activated protein C (APC), Human
Type of nucleic acid: ssRNA
Sequence: 5'GGGAGAAUUCCGACCAGAAGCUUGUGAGACCAGCCGAGUGGUGUCUGGCUAUUCACUGGAGCGUGGGUGGAACCCCUGCGCACUCGUUUGGCUGUCCGGGCCUUCGGGCCGGGAUUAUCUCUUUGGGUUUUGUGAUUUGGUCAUAUGUGCGUCUACAUGGAUCCUCA3'
Sequence length: 167
GC content: 0.5568862275449101
Affinity: Ki: 83 ± 17 nM
Pool type: 5'-AGGGAGAATTCCGACCA-N120-CATATGTGCGTCTACATGGATCCTCA-3'
Pool random region: 120
Binding buffer/conditions: 10 mM sodium citrate, 150 mM KCl pH 7.6
Buffer type: Other Buffers
pH: 7.6
Molecular weight of target: 62 kDa
Application as quoted in the referenced paper: Detection and Theraputic: "The thrombin aptamer isolated by an in vitro selection procedure showed a quite interesting structure and a significant physiological function. Human thrombin is the central enzyme of the blood coagulation cascade, while activated protein is also a key enzyme of anticoagulation cascade."
Additional information: DNA library/pool was used as a template to generate the RNA pool used in the selection. A T7 promoter sequence might be necessary to use this DNA library/pool as a template to generate the RNA pool in the selection.
Reference (1998, Eur J Biochem ): Gal, S. W., Amontov, S., Urvil, P. T., Vishnuvardhan, D., Nishikawa, F., Kumar, P. K., & Nishikawa, S. (1998). Selection of a RNA aptamer that binds to human activated protein C and inhibits its protease function. European journal of biochemistry, 252(3), 553–562. https://doi.org/10.1046/j.1432-1327.1998.2520553.x
Aptamer: APC-99
Target: Activated protein C (APC), Human
Type of nucleic acid: ssRNA
Sequence: 5'GUGAGACCAGCCGAGUGGUGUCUGGCUAUUCACUGGAGCGUGGGUGGAACCCCUGCGCACUCGUUUGGCUGUCCGGGCCUUCGGGCCGGGAUUAUCUCU3'
Sequence length: 99
GC content: 0.6262626262626263
Affinity: Ki: 137 ± 14 nM
Pool type: 5'-AGGGAGAATTCCGACCA-N120-CATATGTGCGTCTACATGGATCCTCA-3'
Pool random region: 120
Binding buffer/conditions: 10 mM sodium citrate, 150 mM KCl pH 7.6
Buffer type: Other Buffers
pH: 7.6
Molecular weight of target: 62 kDa
Application as quoted in the referenced paper: Detection and Theraputic: "The thrombin aptamer isolated by an in vitro selection procedure showed a quite interesting structure and a significant physiological function. Human thrombin is the central enzyme of the blood coagulation cascade, while activated protein is also a key enzyme of anticoagulation cascade."
Additional information: truncated version of aptamer APC-167, DNA library/pool was used as a template to generate the RNA pool used in the selection. A T7 promoter sequence might be necessary to use this DNA library/pool as a template to generate the RNA pool in the selection.
Reference (1998, Eur J Biochem ): Gal, S. W., Amontov, S., Urvil, P. T., Vishnuvardhan, D., Nishikawa, F., Kumar, P. K., & Nishikawa, S. (1998). Selection of a RNA aptamer that binds to human activated protein C and inhibits its protease function. European journal of biochemistry, 252(3), 553–562. https://doi.org/10.1046/j.1432-1327.1998.2520553.x
Aptamer: clone 73
Target: Fluorophore sulforhodamine B
Type of nucleic acid: ssDNA
Sequence: 5'CGGGATCCTAATGACCAAGGGTGGGAGGGAGGGGGTCATTAAATCCAGTATCAACACGCCACGATGGGATCACCGCCATGGGCCGTCCCACTGGTGCCAGTCGGATAGTGTTCCTATAGTGAGTCGTATTAGAA3'
Sequence length: 134
GC content: 0.5447761194029851
Affinity: Not Reported 
Pool type: 5'-AACACTATCCGACTGGCACC-N72-CCTTGGTCATTAGGATCCCG-3'
Pool random region: 72
Binding buffer/conditions: 0.1 M KCI, 5 mM MgCI,, 10 mM Na-HEPES, pH 7.4
Buffer type: Other Buffers
pH: 7.4
Molecular weight of target: Not reported
Application as quoted in the referenced paper: Detection: " The incorporation of three-tiered G-quartet stacked on a duplex into other DNAs (e.g. PCR primers) could facilitate their in vitro labeling and detection. Mutagenesis followed by both negative and positive selection might yield specialized aptamers optimized for highly specific recognition of individual fluorophores. The current motif could be incorporated into larger random pools that could serve as the starting point for new selection experiments directed at the isolation of ribozymes that utilize fluorigenie substrates."
Reference (1998, Chem Biol ): Wilson, C., & Szostak, J. W. (1998). Isolation of a fluorophore-specific DNA aptamer with weak redox activity. Chemistry & biology, 5(11), 609–617. https://doi.org/10.1016/s1074-5521(98)90289-7
Aptamer: minimized clone 73
Target: Fluorophore sulforhodamine B
Type of nucleic acid: ssDNA
Sequence: 5'CCGGCCAAGGGTGGGAGGGAGGGGGGCCGG3'
Sequence length: 30
GC content: 0.8333333333333334
Affinity: Not Reported 
Pool type: 5'-AACACTATCCGACTGGCACC-N72-CCTTGGTCATTAGGATCCCG-3'
Pool random region: 72
Binding buffer/conditions: 0.1 M KCI, 5 mM MgCI,, 10 mM Na-HEPES, pH 7.4
Buffer type: Other Buffers
pH: 7.4
Molecular weight of target: Not reported
Post-SELEX modifications: Truncation (Sulforhodamine agarose binding by a minimal aptamer based on clone 73 with  modified helix sequence was assayed under various salt conditions.)
Application as quoted in the referenced paper: Detection: " The incorporation of three-tiered G-quartet stacked on a duplex into other DNAs (e.g. PCR primers) could facilitate their in vitro labeling and detection. Mutagenesis followed by both negative and positive selection might yield specialized aptamers optimized for highly specific recognition of individual fluorophores. The current motif could be incorporated into larger random pools that could serve as the starting point for new selection experiments directed at the isolation of ribozymes that utilize fluorigenie substrates."
Reference (1998, Chem Biol ): Wilson, C., & Szostak, J. W. (1998). Isolation of a fluorophore-specific DNA aptamer with weak redox activity. Chemistry & biology, 5(11), 609–617. https://doi.org/10.1016/s1074-5521(98)90289-7