RosettaCommons/UTexasAptamer huggingface dataset:
Aptamer: G26
Target: Farnesylated peptide modeled after the carboxyl terminus of K ras
Type of nucleic acid: ssRNA
Sequence: 5'GGGAGAAUUCCGACCAGAAGCCUGAGAUGUAUCGUUGCCGGGGAUGGGUGGGUGGUGUGAAGGCGAUCGUCAUCAGUUCGAGCCAUAUGUGCGUCUACAUGGAUCCUCA3'
Sequence length: 109
GC content: 0.5504587155963303
Affinity: Kd: 0.93 ± 0.05 uM
Pool type: 5'-GGGAGAAUUCCGACCAGAAGCCU-N60-CAUAUGUGCGUCUACAUGGAUCCUCA-3'
Pool random region: 60
Binding buffer/conditions: 140 mM NaCl, 5 mM KCL, 1 mM CaCl:, and 20 mM Tris acetate at pH 7.4.
Divalent salt: CaCl
Buffer type: Tris Buffers
pH: 7.4
Molecular weight of target: Not reported
Application as quoted in the referenced paper: Research: " Binding to the nonfarnesylated peptide was at least 10-fold weaker, showing that the aptamers can recognize the hydrophobic farnesyl moiety. High affinity aptamers could be useful in specifically interfering with oncogenic ras function in particular, and G proteins in general."
Reference (1997, Bioorg Med Chem ): Gilbert, B. A., Sha, M., Wathen, S. T., & Rando, R. R. (1997). RNA aptamers that specifically bind to a K Ras-derived farnesylated peptide. Bioorganic & medicinal chemistry, 5(6), 1115–1122. https://doi.org/10.1016/s0968-0896(97)00047-3
Aptamer: G6–16
Target: NS3 Protein of Hepatitis C Virus (HCV)
Type of nucleic acid: ssRNA
Sequence: 5'GGGAGAAUUCCGACCAGAAGGCUUGCUGUUGUUUCCCUGUUGUUUUGUCUCUCAACUUUAUUGUGGUAAAGAUCACUGGGUUGAUAAGGGCUAACUCUAAUUUGACUACAUGGUCGGACCAAUCAGUUCUUAUGGGAGAUGCAUAUGUGCGUCUACAUGGAUCCUCA3'
Sequence length: 167
GC content: 0.437125748502994
Affinity: Kd: 120 ± 18 nM
Pool type: 5'-GGGAGAATTCCGACCAGAAGCTT-N120-CATATGTGCGTCTACATGGATCCTCA-3'
Pool random region: 120
Binding buffer/conditions: 50 mM Tris – HCl (pH 7.7), 30 mM NaCl, 5 mM CaCl2 , 10 mM dithiothreitol (DTT)]
Divalent salt: CaCl
Buffer type: Tris Buffers
pH: 7.7
Molecular weight of target: Not reported
Application as quoted in the referenced paper: Therapeutic " and Drug Development: We also analyzed aptamers G6 – 16 and G6 – 19 for their action with a longer protein substrate (amino acid region 2203 – 2506) and found that these aptamers efficiently inhibited the proteolytic activity of NS3. In addition, both G6 – 16 and G6 – 19 aptamers were found to inhibit the helicase activity of NS3. Since these aptamers possesses dual inhibitory function for NS3, they could prove to be useful as anti-HCV drug leads"
Additional information: The aptamer G6 – 16 inhibited the proteotic activity in a mixed (competitive and noncompetitive). The aptamer was truncated.
Reference (1997, Virology ): Kumar, P. K., Machida, K., Urvil, P. T., Kakiuchi, N., Vishnuvardhan, D., Shimotohno, K., Taira, K., & Nishikawa, S. (1997). Isolation of RNA aptamers specific to the NS3 protein of hepatitis C virus from a pool of completely random RNA. Virology, 237(2), 270–282. https://doi.org/10.1006/viro.1997.8773
Aptamer: G6–19
Target: NS3 Protein of Hepatitis C Virus (HCV)
Type of nucleic acid: ssRNA
Sequence: 5'GGGAGAAUUCCGACCAGAAGCUUAUACUGAAUUAAUCGCUACCGUGUCAUUGUACUUGGUAGUGUUGAUGGUUUGGGUCGCAUUUGGCUUGGCUUAUGGUUUUUUCACCCUACCUCUCAUUGACGCACUAGGCUCUCAUAUGUGCGUCUACAUGGAUCCUCA3'
Sequence length: 162
GC content: 0.4567901234567901
Affinity: Not reported 
Pool type: 5'-GGGAGAATTCCGACCAGAAGCTT-N120-CATATGTGCGTCTACATGGATCCTCA-3'
Pool random region: 120
Binding buffer/conditions: 50 mM Tris – HCl (pH 7.7), 30 mM NaCl, 5 mM CaCl2 , 10 mM dithiothreitol (DTT)]
Divalent salt: CaCl
Buffer type: Tris Buffers
pH: 7.7
Molecular weight of target: Not reported
Application as quoted in the referenced paper: Therapeutic and Drug Development: We also analyzed aptamers G6 – 16 and G6 – 19 for their action with a longer protein substrate (amino acid region 2203 – 2506) and found that these aptamers efficiently inhibited the proteolytic activity of NS3. In addition, both G6 – 16 and G6 – 19 aptamers were found to inhibit the helicase activity of NS3. Since these aptamers possesses dual inhibitory function for NS3, they could prove to be useful as anti-HCV drug leads"
Reference (1997, Virology ): Kumar, P. K., Machida, K., Urvil, P. T., Kakiuchi, N., Vishnuvardhan, D., Shimotohno, K., Taira, K., & Nishikawa, S. (1997). Isolation of RNA aptamers specific to the NS3 protein of hepatitis C virus from a pool of completely random RNA. Virology, 237(2), 270–282. https://doi.org/10.1006/viro.1997.8773
Aptamer: 945
Target: Special elongation factor SelB of Escherichia coli
Type of nucleic acid: ssRNA
Sequence: 5′GUCAGGAUGACUGCUGCGCUCGUGUCGUCACUGACCAUCUGUCGCAGGUCUGCGCACAUCGGUCGUUCACGGCCCAUCGGUUGCAGGUCUGCACCAAUCGGUCGGUAAUGGCGCAAUGAGCAUUACGGAUUCAAGC3′
Sequence length: 136
GC content: 0.5808823529411765
Affinity: binding ratio: 2.0
Pool type: 5′-GTCAGGATGACTGCTGCGCTCGTGTC-N3-CACGGCCCATCGGTTGCAGGTCTGCACCAATCGGTCGGTAATGGCGCAATGAGCATTACGGATTCAAGC-3′
Pool random region: 3
Binding buffer/conditions: 50 mM potassium phosphate, pH 7.0/5.0 mM Mg(OAc)2/0.1 mM EDTA/1.0 mM DTT/0.5 mM GTP/0.02% Tween 20/50 μg 5S rRNA
Buffer type: PBS/phosphate buffers
pH: 7
Molecular weight of target: 17 kDa 
Application as quoted in the referenced paper: Research: " Our in vitro selection study provides for the first time, to the best of our knowledge, SelB-binding variants of the SelB-responsive wild-type fdhF mRNA hairpin, which allow for the dissection of SelB binding from the overall biological function of this mRNA secondary structure."
Additional information: The 39 nucleotide hairpin fragment of the fdhF mRNA was mutagenized at a level of 30% per base position and exhibited a complexity of 5 × 1014 sequences.
Reference (1997, Proc Natl Acad Sci U S A ): Klug, S. J., Hüttenhofer, A., Kromayer, M., & Famulok, M. (1997). In vitro and in vivo characterization of novel mRNA motifs that bind special elongation factor SelB. Proceedings of the National Academy of Sciences of the United States of America, 94(13), 6676–6681. https://doi.org/10.1073/pnas.94.13.6676
Aptamer: l-aptamer/l-VP
Target: Peptide hormone vasopressin (vertebrate hormone arginine vasopressin (VP), a 9-residue cyclic l peptide)
Type of nucleic acid: ssDNA
Sequence: 5'TCACGTGCATGATAGACGGCGAAGCCGTCGAGTTGCTGTGTGCCGATGCACGTGA3'
Sequence length: 55
GC content: 0.5818181818181818
Affinity: Kd = 1.17 μM
Pool type: 5′-TCTAACGTCAATGATAGA-N60-TTAACTTATTCGACCAAA3'
Pool random region: 60
Binding buffer/conditions: 20 mM sodium 2-[bis(2-hydroxyethyl)amino]ethane sulfonate, pH 7.3/140 mM NaCl/5 mM KCl/5 mM MgCl2/1 mM CaCl2/0.02% Triton X-100
Divalent salt: MgCl/CaCl
Buffer type: Other Buffers
pH: 7.3
Molecular weight of target: Not reported
Post-SELEX modifications: Not applicable
Application as quoted in the referenced paper: Research and Therapeutic: "The principle has application to a problem in biotechnology, namely, that the peptide or nucleic acid ligands generated by phage display or in vitro selection are susceptible to enzymatic degradation; for example, a DNA oligonucleotide injected i.v. is degraded with a half-life of ≈5 min (4–7). The principle of chiral inversion can be coupled to the powerful reiterable selection methods to generate ligands that are insusceptible to degradative enzymes. A stable ligand of VP could be useful as a diagnostic reagent or as a therapeutic antagonist in diseases associated with excessive levels of VP in blood or cerebrospinal fluid."
Additional information: This paper has identified a mirror-image single-stranded DNA that binds the peptide hormone vasopressin Pre-SELEX modification: one preparation of l-aptamer contained a 5′ tail of two d-thymidine residues; this modification had no detectable effect on binding activity. The starting pool for the second selection had 68 nt from sequence B doped at 30% and flanked by AGGCTAGGAAGATCAATT and TTAACTTATTCGACCAAA.
Reference (1997, Proc Natl Acad Sci U S A ): Williams, K. P., Liu, X. H., Schumacher, T. N., Lin, H. Y., Ausiello, D. A., Kim, P. S., & Bartel, D. P. (1997). Bioactive and nuclease-resistant L-DNA ligand of vasopressin. Proceedings of the National Academy of Sciences of the United States of America, 94(21), 11285–11290. https://doi.org/10.1073/pnas.94.21.11285
Aptamer: d-aptamer/d-VP
Target: Peptide hormone vasopressin (vertebrate hormone arginine vasopressin (VP), a 9-residue cyclic l peptide)
Type of nucleic acid: ssDNA
Sequence: 5'TCACGTGCATGATAGACGGCGAAGCCGTCGAGTTGCTGTGTGCCGATGCACGTGA3'
Sequence length: 55
GC content: 0.5818181818181818
Affinity: Kd = 0.85 μM 
Pool type: 5′-TCTAACGTCAATGATAGA-N60-TTAACTTATTCGACCAAA3'
Pool random region: 60
Binding buffer/conditions: 20 mM sodium 2-[bis(2-hydroxyethyl)amino]ethane sulfonate, pH 7.3/140 mM NaCl/5 mM KCl/5 mM MgCl2/1 mM CaCl2/0.02% Triton X-100
Divalent salt: MgCl/CaCl
Buffer type: Other Buffers
pH: 7.3
Molecular weight of target: Not reported
Post-SELEX modifications: Not applicable
Application as quoted in the referenced paper: Research and Therapeutic: "The principle has application to a problem in biotechnology, namely, that the peptide or nucleic acid ligands generated by phage display or in vitro selection are susceptible to enzymatic degradation; for example, a DNA oligonucleotide injected i.v. is degraded with a half-life of ≈5 min (4–7). The principle of chiral inversion can be coupled to the powerful reiterable selection methods to generate ligands that are insusceptible to degradative enzymes. A stable ligand of VP could be useful as a diagnostic reagent or as a therapeutic antagonist in diseases associated with excessive levels of VP in blood or cerebrospinal fluid."
Additional information: This paper has identified a mirror-image single-stranded DNA that binds the peptide hormone vasopressin Pre-SELEX modification: one preparation of l-aptamer contained a 5′ tail of two d-thymidine residues; this modification had no detectable effect on binding activity. The starting pool for the second selection had 68 nt from sequence B doped at 30% and flanked by AGGCTAGGAAGATCAATT and TTAACTTATTCGACCAAA.
Reference (1997, Proc Natl Acad Sci U S A ): Williams, K. P., Liu, X. H., Schumacher, T. N., Lin, H. Y., Ausiello, D. A., Kim, P. S., & Bartel, D. P. (1997). Bioactive and nuclease-resistant L-DNA ligand of vasopressin. Proceedings of the National Academy of Sciences of the United States of America, 94(21), 11285–11290. https://doi.org/10.1073/pnas.94.21.11285
Aptamer: 2'F-1
Target: Interferon-γ (IFN-γ)
Type of nucleic acid: 2'-fluoro-RNA
Sequence: 5'GGGAGGACGAUGCGGACACCGUUAAUCUGAGGCCCUGUCCUAUUCCUUCACGCCUCAGACGACUCGCCCGA3'
Sequence length: 71
GC content: 0.6056338028169014
Affinity: Kd: biphasic 6.8 nM and 320 nM
Pool type: 5'-GGGAGGACGAUGCGG-N40-CAGACGACUCGCCCGA-3'
Pool random region: 40
Binding buffer/conditions: mPBS (138 mM NaCL, 2.7 mM KCl, 8.1 mM Na2HP4, and 1.1 mM KH2PO4, pH 7.4) Modified to contin a 1mM Mg+2 ion and 0.01% human serum albumin
Buffer type: PBS/phosphate buffers
pH: 7.4
Molecular weight of target: 34 kDa
Application as quoted in the referenced paper: Therapeutic and Diagnostic: "IFN-γ plays a major role in promoting inflammatory responses by stimulating macrophages, enhancing adhesion of vascular endothelial cells, and facilitating lymphocyte extravasation either alone or in synergy with other cytokines, in particular TNF-a; Oligonucleotide ligands to IFN-γ that bind with high affinity and specificity would be useful for therapeutic as well as diagnostic purposes"
Additional information: all pyrimidines modified to 2'-F-CMP and 2'-F-UMP
Reference (1997, J Immunol ): Kubik, M. F., Bell, C., Fitzwater, T., Watson, S. R., & Tasset, D. M. (1997). Isolation and characterization of 2'-fluoro-, 2'-amino-, and 2'-fluoro-/amino-modified RNA ligands to human IFN-gamma that inhibit receptor binding. Journal of immunology (Baltimore, Md. : 1950), 159(1), 259–267.
Aptamer: 2'F-27
Target: Interferon-γ (IFN-γ)
Type of nucleic acid: 2'-fluoro-RNA
Sequence: 5'GGGAGGACGAUGCGGAACACCCCCGGUCUGACGCUUGUUCCGAAUUCCUCCACCGUCAGACGACUCGCCCGA3'
Sequence length: 72
GC content: 0.6388888888888888
Affinity: Kd: biphasic 8.8 nM and 384 nM
Pool type: 5'-GGGAGGACGAUGCGG-N40-CAGACGACUCGCCCGA-3'
Pool random region: 40
Binding buffer/conditions: mPBS (138 mM NaCL, 2.7 mM KCl, 8.1 mM Na2HP4, and 1.1 mM KH2PO4, pH 7.4) Modified to contin a 1mM Mg+2 ion and 0.01% human serum albumin
Buffer type: PBS/phosphate buffers
pH: 7.4
Molecular weight of target: 34 kDa
Application as quoted in the referenced paper: Therapeutic and Diagnostic: "IFN-γ plays a major role in promoting inflammatory responses by stimulating macrophages, enhancing adhesion of vascular endothelial cells, and facilitating lymphocyte extravasation either alone or in synergy with other cytokines, in particular TNF-a; Oligonucleotide ligands to IFN-γ that bind with high affinity and specificity would be useful for therapeutic as well as diagnostic purposes"
Additional information: all pyrimidines modified to 2'-F-CMP and 2'-F-UMP
Reference (1997, J Immunol ): Kubik, M. F., Bell, C., Fitzwater, T., Watson, S. R., & Tasset, D. M. (1997). Isolation and characterization of 2'-fluoro-, 2'-amino-, and 2'-fluoro-/amino-modified RNA ligands to human IFN-gamma that inhibit receptor binding. Journal of immunology (Baltimore, Md. : 1950), 159(1), 259–267.
Aptamer: 2'F-28
Target: Interferon-γ (IFN-γ)
Type of nucleic acid: 2'-fluoro-RNA
Sequence: 5'GGGAGGACGAUGCGGAGGGUUGGGAGGGGUCCUUCUUUUCGUCUGCGUGGACCGUCAGACGACUCGCCCGA3'
Sequence length: 71
GC content: 0.647887323943662
Affinity: Kd: 35 nM
Pool type: 5'-GGGAGGACGAUGCGG-N40-CAGACGACUCGCCCGA-3'
Pool random region: 40
Binding buffer/conditions: mPBS (138 mM NaCL, 2.7 mM KCl, 8.1 mM Na2HP4, and 1.1 mM KH2PO4, pH 7.4) Modified to contin a 1mM Mg+2 ion and 0.01% human serum albumin
Buffer type: PBS/phosphate buffers
pH: 7.4
Molecular weight of target: 34 kDa
Application as quoted in the referenced paper: Therapeutic and Diagnostic: "IFN-γ plays a major role in promoting inflammatory responses by stimulating macrophages, enhancing adhesion of vascular endothelial cells, and facilitating lymphocyte extravasation either alone or in synergy with other cytokines, in particular TNF-a; Oligonucleotide ligands to IFN-γ that bind with high affinity and specificity would be useful for therapeutic as well as diagnostic purposes"
Additional information: all pyrimidines modified to 2'-F-CMP and 2'-F-UMP
Reference (1997, J Immunol ): Kubik, M. F., Bell, C., Fitzwater, T., Watson, S. R., & Tasset, D. M. (1997). Isolation and characterization of 2'-fluoro-, 2'-amino-, and 2'-fluoro-/amino-modified RNA ligands to human IFN-gamma that inhibit receptor binding. Journal of immunology (Baltimore, Md. : 1950), 159(1), 259–267.
Aptamer: 2'NH2-17
Target: Interferon-γ (IFN-γ)
Type of nucleic acid: 2'-amino-RNA
Sequence: 5'GGGAGGACGAUGCGGUGGUAGCGCGAUAUAGCGCUGGUAGGGUUGCCGGUGAUCAGACGACUCGCCCGA3'
Sequence length: 69
GC content: 0.6376811594202898
Affinity: Kd: biphasic 1.8 nM and 750 nM
Pool type: 5'-GGGAGGACGAUGCGG-N40-CAGACGACUCGCCCGA-3'
Pool random region: 40
Binding buffer/conditions: mPBS (138 mM NaCL, 2.7 mM KCl, 8.1 mM Na2HP4, and 1.1 mM KH2PO4, pH 7.4) Modified to contin a 1mM Mg+2 ion and 0.01% human serum albumin
Buffer type: PBS/phosphate buffers
pH: 7.4
Molecular weight of target: 34 kDa
Post-SELEX modifications: Truncated IFN-y ligands.
Application as quoted in the referenced paper: Therapeutic  and Diagnostic: "IFN-γ plays a major role in promoting inflammatory responses by stimulating macrophages, enhancing adhesion of vascular endothelial cells, and facilitating lymphocyte extravasation either alone or in synergy with other cytokines, in particular TNF-a; Oligonucleotide ligands to IFN-γ that bind with high affinity and specificity would be useful for therapeutic as well as diagnostic purposes"
Additional information: all pyrimidines modified to 2'-NH2-CMP and 2'-NH-UMP
Reference (1997, J Immunol ): Kubik, M. F., Bell, C., Fitzwater, T., Watson, S. R., & Tasset, D. M. (1997). Isolation and characterization of 2'-fluoro-, 2'-amino-, and 2'-fluoro-/amino-modified RNA ligands to human IFN-gamma that inhibit receptor binding. Journal of immunology (Baltimore, Md. : 1950), 159(1), 259–267.
Aptamer: 2'NH2-30
Target: Interferon-γ (IFN-γ)
Type of nucleic acid: 2'-amino-RNA
Sequence: 5'GGGAGGACGAUGCGGCAGGUAAUUACAUGAAGGUGGGUUAGGUACUUUCAGGGUCAGACGACUCGCCCGA3'
Sequence length: 70
GC content: 0.5571428571428572
Affinity: Kd: biphasic 2.7 nM and 103 nM
Pool type: 5'-GGGAGGACGAUGCGG-N40-CAGACGACUCGCCCGA-3'
Pool random region: 40
Binding buffer/conditions: mPBS (138 mM NaCL, 2.7 mM KCl, 8.1 mM Na2HP4, and 1.1 mM KH2PO4, pH 7.4) Modified to contin a 1mM Mg+2 ion and 0.01% human serum albumin
Buffer type: PBS/phosphate buffers
pH: 7.4
Molecular weight of target: 34 kDa
Application as quoted in the referenced paper: Therapeutic " and Diagnostic: IFN-γ plays a major role in promoting inflammatory responses by stimulating macrophages, enhancing adhesion of vascular endothelial cells, and facilitating lymphocyte extravasation either alone or in synergy with other cytokines, in particular TNF-a; Oligonucleotide ligands to IFN-γ that bind with high affinity and specificity would be useful for therapeutic as well as diagnostic purposes"
Additional information: all pyrimidines modified to 2'-NH2-CMP and 2'-NH-UMP
Reference (1997, J Immunol ): Kubik, M. F., Bell, C., Fitzwater, T., Watson, S. R., & Tasset, D. M. (1997). Isolation and characterization of 2'-fluoro-, 2'-amino-, and 2'-fluoro-/amino-modified RNA ligands to human IFN-gamma that inhibit receptor binding. Journal of immunology (Baltimore, Md. : 1950), 159(1), 259–267.
Aptamer: 2'F/NH2-3
Target: Interferon-γ (IFN-γ)
Type of nucleic acid: 2'-fluoro/amino-RNA
Sequence: 5'GGGAGGACGAUGCGGUUCAGAGGGUAGGUAAGUGGGAGGAAAAAUGCCGUAUCGCCUCAGACGACUCGCCCGA3'
Sequence length: 73
GC content: 0.589041095890411
Affinity: Kd: 106 nM
Pool type: 5'-GGGAGGACGAUGCGG-N40-CAGACGACUCGCCCGA-3'
Pool random region: 40
Binding buffer/conditions: mPBS (138 mM NaCL, 2.7 mM KCl, 8.1 mM Na2HP4, and 1.1 mM KH2PO4, pH 7.4) Modified to contin a 1mM Mg+2 ion and 0.01% human serum albumin
Buffer type: PBS/phosphate buffers
pH: 7.4
Molecular weight of target: 34 kDa
Application as quoted in the referenced paper: Therapeutic and Diagnostic: "IFN-γ plays a major role in promoting inflammatory responses by stimulating macrophages, enhancing adhesion of vascular endothelial cells, and facilitating lymphocyte extravasation either alone or in synergy with other cytokines, in particular TNF-a; Oligonucleotide ligands to IFN-γ that bind with high affinity and specificity would be useful for therapeutic as well as diagnostic purposes"
Additional information: all pyrimidines modified to 2'-F-CMP and 2'-F-NH2-UMP
Reference (1997, J Immunol ): Kubik, M. F., Bell, C., Fitzwater, T., Watson, S. R., & Tasset, D. M. (1997). Isolation and characterization of 2'-fluoro-, 2'-amino-, and 2'-fluoro-/amino-modified RNA ligands to human IFN-gamma that inhibit receptor binding. Journal of immunology (Baltimore, Md. : 1950), 159(1), 259–267.
Aptamer: 14F
Target: Keratinocyte growth factor (hKGF), Human
Type of nucleic acid: 2'-fluoro-RNA
Sequence: 5'GGGAGGACGAUGCGGUGGUCUCCCAAUUCUAAACUUUCUCCAUCGUAUCUGGGCAGACGACUCGCCCGA3'
Sequence length: 69
GC content: 0.5652173913043478
Affinity: Kd: biphasic 0.001 nM Ki: 3.3 nM
Pool type: 5'-GGGAGGACGATGCGG-N40-CAGACGACTCGCCCGA-3'
Pool random region: 40
Binding buffer/conditions: Ca++ and Mg++ containing Dulbeco's Phosphate Buffered Saline (DPBS, Life Technologies, Gaithersburg, MD) with 0.01% human serum albumin (Sigma, St. Louis, MO)
Buffer type: PBS/phosphate buffers
pH: 7.4
Molecular weight of target: 26-28 kDa
Application as quoted in the referenced paper: Research: " RNA molecules with fluoro (2'F) or amino (2'NH2) substitution at the 2' position of pyrimidines are nuclease resistant' and can be synthesized by T7 RNA polymerase. Thus, SELEX experiments with libraries carrying such modifications can lead to nuclease-resistant ligands"
Additional information: all pyrimidines have 2' fluro substitutions, 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 (1997, Nat Biotechnol ): Pagratis, N. C., Bell, C., Chang, Y. F., Jennings, S., Fitzwater, T., Jellinek, D., & Dang, C. (1997). Potent 2'-amino-, and 2'-fluoro-2'-deoxyribonucleotide RNA inhibitors of keratinocyte growth factor. Nature biotechnology, 15(1), 68–73. https://doi.org/10.1038/nbt0197-68
Aptamer: 6F
Target: Keratinocyte growth factor (hKGF), Human
Type of nucleic acid: 2'-fluoro-RNA
Sequence: 5'GGGAGGACGAUGCGGGAUCCUUUGUGGGCUCUUGUUGACCCCCUCGUUGUCCCCCCCAGACGACUCGCCCGA3'
Sequence length: 72
GC content: 0.6527777777777778
Affinity: Kd: biphasic 0.05 nM Ki: 1.3 nM
Pool type: 5'-GGGAGGACGATGCGG-N40-CAGACGACTCGCCCGA-3'
Pool random region: 40
Binding buffer/conditions: Ca++ and Mg++ containing Dulbeco's Phosphate Buffered Saline (DPBS, Life Technologies, Gaithersburg, MD) with 0.01% human serum albumin (Sigma, St. Louis, MO)
Buffer type: PBS/phosphate buffers
pH: 7.4
Molecular weight of target: 26-28 kDa
Application as quoted in the referenced paper: Research: " RNA molecules with fluoro (2'F) or amino (2'NH2) substitution at the 2' position of pyrimidines are nuclease resistant' and can be synthesized by T7 RNA polymerase. Thus, SELEX experiments with libraries carrying such modifications can lead to nuclease-resistant ligands"
Additional information: all pyrimidines have 2' fluro substitutions, 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 (1997, Nat Biotechnol ): Pagratis, N. C., Bell, C., Chang, Y. F., Jennings, S., Fitzwater, T., Jellinek, D., & Dang, C. (1997). Potent 2'-amino-, and 2'-fluoro-2'-deoxyribonucleotide RNA inhibitors of keratinocyte growth factor. Nature biotechnology, 15(1), 68–73. https://doi.org/10.1038/nbt0197-68
Aptamer: 15F
Target: Keratinocyte growth factor (hKGF), Human
Type of nucleic acid: 2'-fluoro-RNA
Sequence: 5'GGGAGGACGAUGCGGUCAUGGUGUCUUUCCACAGCUCUUCCCAUGAUCGCCCGGCAGACGACUCGCCCGA3'
Sequence length: 70
GC content: 0.6285714285714286
Affinity: Kd: biphasic 0.07 nM Ki: 6.7 nM
Pool type: 5'-GGGAGGACGATGCGG-N40-CAGACGACTCGCCCGA-3'
Pool random region: 40
Binding buffer/conditions: Ca++ and Mg++ containing Dulbeco's Phosphate Buffered Saline (DPBS, Life Technologies, Gaithersburg, MD) with 0.01% human serum albumin (Sigma, St. Louis, MO)
Buffer type: PBS/phosphate buffers
pH: 7.4
Molecular weight of target: 26-28 kDa
Application as quoted in the referenced paper: Research: " RNA molecules with fluoro (2'F) or amino (2'NH2) substitution at the 2' position of pyrimidines are nuclease resistant' and can be synthesized by T7 RNA polymerase. Thus, SELEX experiments with libraries carrying such modifications can lead to nuclease-resistant ligands"
Additional information: all pyrimidines have 2' fluro substitutions, 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 (1997, Nat Biotechnol ): Pagratis, N. C., Bell, C., Chang, Y. F., Jennings, S., Fitzwater, T., Jellinek, D., & Dang, C. (1997). Potent 2'-amino-, and 2'-fluoro-2'-deoxyribonucleotide RNA inhibitors of keratinocyte growth factor. Nature biotechnology, 15(1), 68–73. https://doi.org/10.1038/nbt0197-68