RosettaCommons/UTexasAptamer huggingface dataset:
Aptamer: F38
Target: RNA-dependent RNA polymerase (3Dpol)
Type of nucleic acid: ssRNA
Sequence: 5'GGGAAGGGAUCCACAUCUACAAAUUCCUUCAUAAUAAACCCGUCCACGCCCUUCGAAGCAGUUCAGACGUCACUU3'
Sequence length: 75
GC content: 0.48
Affinity: Kd: 460 nM
Pool type: 5′-GATAATACGACTCACTATAGGGAATGGATCCACACATCTACGA-N30-TTCGAAGCAGTTCAGACGTCACTT-3′
Pool random region: 30
Binding buffer/conditions: 50 mM Tris-HCl at pH 7.5, 100 mM NaCl, 1 mM dithiothreitol [DTT], 1 mM EDTA
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: " Foot-and-mouth disease virus causes a highly contagious disease of agricultural livestock and is of enormous economic importance. Replication of the RNA genome of the virus, via negative strand intermediates, involves an RNA-dependent RNA polymerase (3Dpol). RNA aptamers specific to this enzyme have been selected and characterized. Some of these molecules inhibit enzymatic activity in vitro."
Additional information: Pool type and sequences don't match, 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 (2006, RNA ): Ellingham, M., Bunka, D. H., Rowlands, D. J., & Stonehouse, N. J. (2006). Selection and characterization of RNA aptamers to the RNA-dependent RNA polymerase from foot-and-mouth disease virus. RNA (New York, N.Y.), 12(11), 1970–1979. https://doi.org/10.1261/rna.161006
Aptamer: F47tr
Target: RNA-dependent RNA polymerase (3Dpol)
Type of nucleic acid: ssRNA
Sequence: 5'GGGUUAACAGAAAACCUCAGUUGCUGGGUUGU3'
Sequence length: 32
GC content: 0.46875
Affinity: Kd: 325
Pool type: 5′-GATAATACGACTCACTATAGGGAATGGATCCACACATCTACGA-N30-TTCGAAGCAGTTCAGACGTCACTT-3′
Pool random region: 30
Binding buffer/conditions: 50 mM Tris-HCl at pH 7.5, 100 mM NaCl, 1 mM dithiothreitol [DTT], 1 mM EDTA
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: " Foot-and-mouth disease virus causes a highly contagious disease of agricultural livestock and is of enormous economic importance. Replication of the RNA genome of the virus, via negative strand intermediates, involves an RNA-dependent RNA polymerase (3Dpol). RNA aptamers specific to this enzyme have been selected and characterized. Some of these molecules inhibit enzymatic activity in vitro."
Reference (2006, RNA ): Ellingham, M., Bunka, D. H., Rowlands, D. J., & Stonehouse, N. J. (2006). Selection and characterization of RNA aptamers to the RNA-dependent RNA polymerase from foot-and-mouth disease virus. RNA (New York, N.Y.), 12(11), 1970–1979. https://doi.org/10.1261/rna.161006
Aptamer: Ab3
Target: Abrin toxin
Type of nucleic acid: ssDNA
Sequence: 5'CAGCTCAGAAGCTTGATCCTGTGCGAAAAGGATGCGGGCAGCGGACTCAAGGCCATCTGACTCGAAGTCGTGCATCTGCA3'
Sequence length: 80
GC content: 0.5625
Affinity: Kd: 50 ± 15 nM
Pool type: 5′-CAGCTCAGAAGCTTGATCCTGTG-N35-GACTCGAAGTCGTGCATCTGCA-3′
Pool random region: 35
Binding buffer/conditions: SHMCK (20 mM HEPES, pH 7.35, 120 mM NaCl, 5 mM KCl, 1 mM CaCl2, 1 mM MgCl2
Divalent salt: MgCl/CaCl
Buffer type: Other Buffers
pH: 7.35
Molecular weight of target: 63 kDa
Post-SELEX modifications: Not applicable
Application as quoted in the referenced paper: Diagnostic: " In this assay, three truncated aptamers against abrin toxin were chosen and evaluated, in which aptamer TA6 has been shown as the best signaling performance. The signaling aptamers with luminescence switching complexes were further proved to be a series of powerful reagents for aptamer-based target detection, even in a quite complicated biological matrix, such as diluted serum, and without further signal amplifications."
Reference (2006, Biosens Bioelectron ): Tang, J., Yu, T., Guo, L., Xie, J., Shao, N., & He, Z. (2007). In vitro selection of DNA aptamer against abrin toxin and aptamer-based abrin direct detection. Biosensors & bioelectronics, 22(11), 2456–2463. https://doi.org/10.1016/j.bios.2006.09.015
Aptamer: Ab6
Target: Abrin toxin
Type of nucleic acid: ssDNA
Sequence: 5'CAGCTCAGAAGCTTGATCCTGTGAGGAATGCTCATGCATAGCAAGGGCTAAACACGGCGACTCGAAGTCGTGCATCTGCA3'
Sequence length: 80
GC content: 0.525
Affinity: Kd: 28 ± 9 nM
Pool type: 5′-CAGCTCAGAAGCTTGATCCTGTG-N35-GACTCGAAGTCGTGCATCTGCA-3′
Pool random region: 35
Binding buffer/conditions: SHMCK (20 mM HEPES, pH 7.35, 120 mM NaCl, 5 mM KCl, 1 mM CaCl2, 1 mM MgCl3
Divalent salt: MgCl/CaCl
Buffer type: Other Buffers
pH: 7.35
Molecular weight of target: 64 kDa
Post-SELEX modifications: Not applicable
Application as quoted in the referenced paper: Diagnostic: " In this assay, three truncated aptamers against abrin toxin were chosen and evaluated, in which aptamer TA6 has been shown as the best signaling performance. The signaling aptamers with luminescence switching complexes were further proved to be a series of powerful reagents for aptamer-based target detection, even in a quite complicated biological matrix, such as diluted serum, and without further signal amplifications."
Reference (2006, Biosens Bioelectron ): Tang, J., Yu, T., Guo, L., Xie, J., Shao, N., & He, Z. (2007). In vitro selection of DNA aptamer against abrin toxin and aptamer-based abrin direct detection. Biosensors & bioelectronics, 22(11), 2456–2463. https://doi.org/10.1016/j.bios.2006.09.015
Aptamer: Aptamer 32
Target: DNA polymerase beta (polβ)
Type of nucleic acid: ssRNA
Sequence: 5′GGGAAUGGAUCCACAUCUACGAAUUCGGUUGGGUUGUCGUAGAUAGAGCGCUUCAAUUCACUGCAGACUUGACGAAGCUU3′
Sequence length: 80
GC content: 0.475
Affinity: Kd: 290 ± 80 nM
Pool type: 5′-GGGAAUGGAUCCACAUCUACGAAUUC-N30-UUCACUGCAGACUUGACGAAGCUU-3′
Pool random region: 30
Binding buffer/conditions: 20 mM Tris–HCl, pH 7.7, 120 mM NaCl, 5 mM KCl, 1 mM MgCl2, 1 mM CaCl2
Divalent salt: MgCl/CaCl
Buffer type: Tris Buffers
pH: 7.7
Molecular weight of target: Not reported
Post-SELEX modifications: Not applicable
Application as quoted in the referenced paper: Therapeutic: " DNA polymerase beta (polbeta), a member of the X family of DNA polymerases, is the major polymerase in the base excision repair pathway. Using in vitro selection, we obtained RNA aptamers for polbeta. These semi-selective RNA aptamers that inhibit error-prone repair polymerases could prove useful for understanding the role of repair in the initiation and progression of cancer as well as in the development of resistance to chemotherapeutic DNA damaging agents."
Additional information: aptamer inhibits polβ activity
Reference (2006, Nucleic Acids Res ): Gening, L. V., Klincheva, S. A., Reshetnjak, A., Grollman, A. P., & Miller, H. (2006). RNA aptamers selected against DNA polymerase beta inhibit the polymerase activities of DNA polymerases beta and kappa. Nucleic acids research, 34(9), 2579–2586. https://doi.org/10.1093/nar/gkl326
Aptamer: Aptamer 32
Target: DNA polymerase kappa (polκ)
Type of nucleic acid: ssRNA
Sequence: 5′GGGAAUGGAUCCACAUCUACGAAUUCGGUUGGGUUGUCGUAGAUAGAGCGCUUCAAUUCACUGCAGACUUGACGAAGCUU3′
Sequence length: 80
GC content: 0.475
Affinity: Kd: 410 ± 50 nM
Pool type: 5′-GGGAAUGGAUCCACAUCUACGAAUUC-N30-UUCACUGCAGACUUGACGAAGCUU-3′
Pool random region: 30
Binding buffer/conditions: 20 mM Tris–HCl, pH 7.7, 120 mM NaCl, 5 mM KCl, 1 mM MgCl2, 1 mM CaCl2
Divalent salt: MgCl/CaCl
Buffer type: Tris Buffers
pH: 7.7
Molecular weight of target: Not reported
Post-SELEX modifications: Not applicable
Application as quoted in the referenced paper: Therapeutic: " DNA polymerase beta (polbeta), a member of the X family of DNA polymerases, is the major polymerase in the base excision repair pathway. Using in vitro selection, we obtained RNA aptamers for polbeta. These semi-selective RNA aptamers that inhibit error-prone repair polymerases could prove useful for understanding the role of repair in the initiation and progression of cancer as well as in the development of resistance to chemotherapeutic DNA damaging agents."
Additional information: aptamer inhibits polκ activity
Reference (2006, Nucleic Acids Res ): Gening, L. V., Klincheva, S. A., Reshetnjak, A., Grollman, A. P., & Miller, H. (2006). RNA aptamers selected against DNA polymerase beta inhibit the polymerase activities of DNA polymerases beta and kappa. Nucleic acids research, 34(9), 2579–2586. https://doi.org/10.1093/nar/gkl326
Aptamer: Aptamer 25
Target: DNA polymerase beta (polβ)
Type of nucleic acid: ssRNA
Sequence: 5′GGGAAUGGAUCCACAUCUACGAAUUCGGUUGGGUUGUCGUAGAUAUAGCUUAGCCAUUCACUGCAGACUUGACGAAGCUU3′
Sequence length: 80
GC content: 0.4625
Affinity: Kd: 430 ± 130 nM
Pool type: 5′-GGGAAUGGAUCCACAUCUACGAAUUC-N30-UUCACUGCAGACUUGACGAAGCUU-3′
Pool random region: 30
Binding buffer/conditions: 20 mM Tris–HCl, pH 7.7, 120 mM NaCl, 5 mM KCl, 1 mM MgCl2, 1 mM CaCl2
Divalent salt: MgCl/CaCl
Buffer type: Tris Buffers
pH: 7.7
Molecular weight of target: Not reported
Post-SELEX modifications: Not applicable
Application as quoted in the referenced paper: Therapeutic: " DNA polymerase beta (polbeta), a member of the X family of DNA polymerases, is the major polymerase in the base excision repair pathway. Using in vitro selection, we obtained RNA aptamers for polbeta. These semi-selective RNA aptamers that inhibit error-prone repair polymerases could prove useful for understanding the role of repair in the initiation and progression of cancer as well as in the development of resistance to chemotherapeutic DNA damaging agents."
Additional information: aptamer inhibits polβ activity
Reference (2006, Nucleic Acids Res ): Gening, L. V., Klincheva, S. A., Reshetnjak, A., Grollman, A. P., & Miller, H. (2006). RNA aptamers selected against DNA polymerase beta inhibit the polymerase activities of DNA polymerases beta and kappa. Nucleic acids research, 34(9), 2579–2586. https://doi.org/10.1093/nar/gkl326
Aptamer: Aptamer 25
Target: DNA polymerase kappa (polκ)
Type of nucleic acid: ssRNA
Sequence: 5′GGGAAUGGAUCCACAUCUACGAAUUCGGUUGGGUUGUCGUAGAUAUAGCUUAGCCAUUCACUGCAGACUUGACGAAGCUU3′
Sequence length: 80
GC content: 0.4625
Affinity: Kd: 500 ± 100 nM
Pool type: 5′-GGGAAUGGAUCCACAUCUACGAAUUC-N30-UUCACUGCAGACUUGACGAAGCUU-3′
Pool random region: 30
Binding buffer/conditions: 20 mM Tris–HCl, pH 7.7, 120 mM NaCl, 5 mM KCl, 1 mM MgCl2, 1 mM CaCl2
Divalent salt: MgCl/CaCl
Buffer type: Tris Buffers
pH: 7.7
Molecular weight of target: Not reported
Post-SELEX modifications: Not applicable
Application as quoted in the referenced paper: Therapeutic: " DNA polymerase beta (polbeta), a member of the X family of DNA polymerases, is the major polymerase in the base excision repair pathway. Using in vitro selection, we obtained RNA aptamers for polbeta. These semi-selective RNA aptamers that inhibit error-prone repair polymerases could prove useful for understanding the role of repair in the initiation and progression of cancer as well as in the development of resistance to chemotherapeutic DNA damaging agents."
Additional information: aptamer inhibits polκ activity
Reference (2006, Nucleic Acids Res ): Gening, L. V., Klincheva, S. A., Reshetnjak, A., Grollman, A. P., & Miller, H. (2006). RNA aptamers selected against DNA polymerase beta inhibit the polymerase activities of DNA polymerases beta and kappa. Nucleic acids research, 34(9), 2579–2586. https://doi.org/10.1093/nar/gkl326
Aptamer: Aptamer 53
Target: DNA polymerase beta (polβ)
Type of nucleic acid: ssRNA
Sequence: 5′GGGAAUGGAUCCACAUCUACGAAUUCGGGUGGGUUGUCGUGGAUGACGAUUAUCAGUUCACUGCAGACUUGACGAAGCUU3′
Sequence length: 80
GC content: 0.4875
Affinity: Not reported
Pool type: 5′-GGGAAUGGAUCCACAUCUACGAAUUC-N30-UUCACUGCAGACUUGACGAAGCUU-3′
Pool random region: 30
Binding buffer/conditions: 20 mM Tris–HCl, pH 7.7, 120 mM NaCl, 5 mM KCl, 1 mM MgCl2, 1 mM CaCl2
Divalent salt: MgCl/CaCl
Buffer type: Tris Buffers
pH: 7.7
Molecular weight of target: Not reported
Post-SELEX modifications: Not applicable
Application as quoted in the referenced paper: Therapeutic: " DNA polymerase beta (polbeta), a member of the X family of DNA polymerases, is the major polymerase in the base excision repair pathway. Using in vitro selection, we obtained RNA aptamers for polbeta. These semi-selective RNA aptamers that inhibit error-prone repair polymerases could prove useful for understanding the role of repair in the initiation and progression of cancer as well as in the development of resistance to chemotherapeutic DNA damaging agents."
Additional information: aptamer inhibits polβ activity
Reference (2006, Nucleic Acids Res ): Gening, L. V., Klincheva, S. A., Reshetnjak, A., Grollman, A. P., & Miller, H. (2006). RNA aptamers selected against DNA polymerase beta inhibit the polymerase activities of DNA polymerases beta and kappa. Nucleic acids research, 34(9), 2579–2586. https://doi.org/10.1093/nar/gkl326
Aptamer: Aptamer 45
Target: DNA polymerase beta (polβ)
Type of nucleic acid: ssRNA
Sequence: 5′GGGAAUGGAUCCACAUCUACGAAUUUCGGGGGGGUUGUUCGUGGAAAAUGCUUGCGUUCACUGCAGACUUGACGAAGCUU3′
Sequence length: 80
GC content: 0.5
Affinity: Kd: 490 ± 70 nM
Pool type: 5′-GGGAAUGGAUCCACAUCUACGAAUUU-N30-UUCACUGCAGACUUGACGAAGCUU-3′
Pool random region: 30
Binding buffer/conditions: 20 mM Tris–HCl, pH 7.7, 120 mM NaCl, 5 mM KCl, 1 mM MgCl2, 1 mM CaCl2
Divalent salt: MgCl/CaCl
Buffer type: Tris Buffers
pH: 7.7
Molecular weight of target: Not reported
Post-SELEX modifications: Not applicable
Application as quoted in the referenced paper: Therapeutic: " DNA polymerase beta (polbeta), a member of the X family of DNA polymerases, is the major polymerase in the base excision repair pathway. Using in vitro selection, we obtained RNA aptamers for polbeta. These semi-selective RNA aptamers that inhibit error-prone repair polymerases could prove useful for understanding the role of repair in the initiation and progression of cancer as well as in the development of resistance to chemotherapeutic DNA damaging agents."
Additional information: aptamer inhibits polβ activity
Reference (2006, Nucleic Acids Res ): Gening, L. V., Klincheva, S. A., Reshetnjak, A., Grollman, A. P., & Miller, H. (2006). RNA aptamers selected against DNA polymerase beta inhibit the polymerase activities of DNA polymerases beta and kappa. Nucleic acids research, 34(9), 2579–2586. https://doi.org/10.1093/nar/gkl326
Aptamer: Aptamer 45
Target: DNA polymerase kappa (polκ)
Type of nucleic acid: ssRNA
Sequence: 5′GGGAAUGGAUCCACAUCUACGAAUUUCGGGGGGGUUGUUCGUGGAAAAUGCUUGCGUUCACUGCAGACUUGACGAAGCUU3′
Sequence length: 80
GC content: 0.5
Affinity: Kd: 750  ± 160 nM
Pool type: 5′-GGGAAUGGAUCCACAUCUACGAAUUU-N30-UUCACUGCAGACUUGACGAAGCUU-3′
Pool random region: 30
Binding buffer/conditions: 20 mM Tris–HCl, pH 7.7, 120 mM NaCl, 5 mM KCl, 1 mM MgCl2, 1 mM CaCl2
Divalent salt: MgCl/CaCl
Buffer type: Tris Buffers
pH: 7.7
Molecular weight of target: Not reported
Post-SELEX modifications: Not applicable
Application as quoted in the referenced paper: Therapeutic: " DNA polymerase beta (polbeta), a member of the X family of DNA polymerases, is the major polymerase in the base excision repair pathway. Using in vitro selection, we obtained RNA aptamers for polbeta. These semi-selective RNA aptamers that inhibit error-prone repair polymerases could prove useful for understanding the role of repair in the initiation and progression of cancer as well as in the development of resistance to chemotherapeutic DNA damaging agents."
Additional information: aptamer inhibits polκ activity
Reference (2006, Nucleic Acids Res ): Gening, L. V., Klincheva, S. A., Reshetnjak, A., Grollman, A. P., & Miller, H. (2006). RNA aptamers selected against DNA polymerase beta inhibit the polymerase activities of DNA polymerases beta and kappa. Nucleic acids research, 34(9), 2579–2586. https://doi.org/10.1093/nar/gkl326
Aptamer: Aptamer 31
Target: DNA polymerase beta (polβ)
Type of nucleic acid: ssRNA
Sequence: 5′GGGAAUGGAUCCACAUCUACGAAUUCGUUAACUGACCCAGGGAAGUGCCACCCCCCUUCACUGCAGACUUGACGAAGCUU3′
Sequence length: 80
GC content: 0.525
Affinity: Not reported
Pool type: 5′-GGGAAUGGAUCCACAUCUACGAAUUC-N30-UUCACUGCAGACUUGACGAAGCUU-3′
Pool random region: 30
Binding buffer/conditions: 20 mM Tris–HCl, pH 7.7, 120 mM NaCl, 5 mM KCl, 1 mM MgCl2, 1 mM CaCl2
Divalent salt: MgCl/CaCl
Buffer type: Tris Buffers
pH: 7.7
Molecular weight of target: Not reported
Post-SELEX modifications: Not applicable
Application as quoted in the referenced paper: Therapeutic: " DNA polymerase beta (polbeta), a member of the X family of DNA polymerases, is the major polymerase in the base excision repair pathway. Using in vitro selection, we obtained RNA aptamers for polbeta. These semi-selective RNA aptamers that inhibit error-prone repair polymerases could prove useful for understanding the role of repair in the initiation and progression of cancer as well as in the development of resistance to chemotherapeutic DNA damaging agents."
Additional information: aptamer inhibits polβ activity
Reference (2006, Nucleic Acids Res ): Gening, L. V., Klincheva, S. A., Reshetnjak, A., Grollman, A. P., & Miller, H. (2006). RNA aptamers selected against DNA polymerase beta inhibit the polymerase activities of DNA polymerases beta and kappa. Nucleic acids research, 34(9), 2579–2586. https://doi.org/10.1093/nar/gkl326
Aptamer: RM312
Target: Recombinant ovine PrP (Prion protein) of the susceptible-specific (V136R154Q171) or resistant-specific (A136R154R171) alleles
Type of nucleic acid: ssRNA
Sequence: 5'GAGGAUCCGCCGAGUAACAGACGUCGGGGAUUGGCAAACCCCGUUUCCUUGAGCGACCCCCUUGAGGCUCGAAUUCGCCC3'
Sequence length: 80
GC content: 0.6125
Affinity: Kd: 28.9 ± 0.8 nM (VRQ), Kd: 14.6 ± 1.3 nM (ARR)
Pool type: 5'-GAGGATCCGCCGAGTAACAG-N40-CTTGAGGCTCGAATTCGCCC-3'
Pool random region: 40
Binding buffer/conditions: 50 mM Tris, 125 mM NaCl, 5 mM MgCl2, pH 8
Divalent salt: MgCl
Buffer type: Tris Buffers
pH: 8
Molecular weight of target: Not reported
Post-SELEX modifications: Not applicable
Application as quoted in the referenced paper: Therapeutic and Detection: "Identify RNA motifs that bind recombinant ovine PrP of the susceptible-specific or resistant-specific alleles. Since the main phenotype in prion diseases consists in alterations of PrP’s properties, uncertainties about PrP’s functions represent a major obstacle in our understanding of the pathological process and impedes any attempt towards prevention and therapeutics of prion diseases."
Reference (2006, Arch Virol ): Mercey, R., Lantier, I., Maurel, M. C., Grosclaude, J., Lantier, F., & Marc, D. (2006). Fast, reversible interaction of prion protein with RNA aptamers containing specific sequence patterns. Archives of virology, 151(11), 2197–2214. https://doi.org/10.1007/s00705-006-0790-3
Aptamer: RM312c (truncated RM312)
Target: Recombinant ovine PrP (Prion protein) of the susceptible-specific (V136R154Q171) or resistant-specific (A136R154R171) alleles
Type of nucleic acid: ssRNA
Sequence: 5'GAGGAUCCGCCGAGUAACAGACGUCGGGGAUUGGCAAACCCCGUUUCCUUGAG3'
Sequence length: 53
GC content: 0.5849056603773585
Affinity: Not reported
Pool type: 5'-GAGGATCCGCCGAGTAACAG-N40-CTTGAGGCTCGAATTCGCCC-3'
Pool random region: 40
Binding buffer/conditions: 50 mM Tris, 125 mM NaCl, 5 mM MgCl2, pH 8
Divalent salt: MgCl
Buffer type: Tris Buffers
pH: 8
Molecular weight of target: Not reported
Post-SELEX modifications: This is the truncated version of rm312
Application as quoted in the referenced paper: Therapeutic and Detection: "Identify RNA motifs that bind recombinant ovine PrP of the susceptible-specific or resistant-specific alleles. Since the main phenotype in prion diseases consists in alterations of PrP’s properties, uncertainties about PrP’s functions represent a major obstacle in our understanding of the pathological process and impedes any attempt towards prevention and therapeutics of prion diseases."
Reference (2006, Arch Virol ): Mercey, R., Lantier, I., Maurel, M. C., Grosclaude, J., Lantier, F., & Marc, D. (2006). Fast, reversible interaction of prion protein with RNA aptamers containing specific sequence patterns. Archives of virology, 151(11), 2197–2214. https://doi.org/10.1007/s00705-006-0790-3
Aptamer: RM312e (truncated RM312)
Target: Recombinant ovine PrP (Prion protein) of the susceptible-specific (V136R154Q171) or resistant-specific (A136R154R171) alleles
Type of nucleic acid: ssRNA
Sequence: 5'GGCAAACCCCGUUUCCUUGAGCGACCCCCUUGAGGCUCGAAUUCGCCC3'
Sequence length: 48
GC content: 0.625
Affinity: Not reported
Pool type: 5-GAGGATCCGCCGAGTAACAG-N40-CTTGAGGCTCGAATTCGCCC-3
Pool random region: 40
Binding buffer/conditions: 50 mM Tris, 125 mM NaCl, 5 mM MgCl2, pH 8
Divalent salt: MgCl
Buffer type: Tris Buffers
pH: 8
Molecular weight of target: Not reported
Post-SELEX modifications: This is the truncated version of rm312
Application as quoted in the referenced paper: Therapeutic and Detection: "Identify RNA motifs that bind recombinant ovine PrP of the susceptible-specific or resistant-specific alleles. Since the main phenotype in prion diseases consists in alterations of PrP’s properties, uncertainties about PrP’s functions represent a major obstacle in our understanding of the pathological process and impedes any attempt towards prevention and therapeutics of prion diseases."
Reference (2006, Arch Virol ): Mercey, R., Lantier, I., Maurel, M. C., Grosclaude, J., Lantier, F., & Marc, D. (2006). Fast, reversible interaction of prion protein with RNA aptamers containing specific sequence patterns. Archives of virology, 151(11), 2197–2214. https://doi.org/10.1007/s00705-006-0790-3
Aptamer: RM120
Target: Recombinant ovine PrP (Prion protein) of the susceptible-specific (V136R154Q171) or resistant-specific (A136R154R171) alleles
Type of nucleic acid: ssRNA
Sequence: 5'GAGGAUCCGCCGAGUAACAGAGUAGCAACAGAAUUGGAUCCCGACCACUAAGAACCCGGCCUUGAGGCUCGAAUUCGCCC3'
Sequence length: 80
GC content: 0.5625
Affinity: Kd: 72.6 ± 3.7 nM (VRQ), Kd: 23.2 ± 0.5 nM (ARR)
Pool type: 5'-GAGGATCCGCCGAGTAACAG-N40-CTTGAGGCTCGAATTCGCCC-3'
Pool random region: 40
Binding buffer/conditions: 50 mM Tris, 125 mM NaCl, 5 mM MgCl2, pH 8
Divalent salt: MgCl
Buffer type: Tris Buffers
pH: 8
Molecular weight of target: Not reported
Post-SELEX modifications: Not applicable
Application as quoted in the referenced paper: Therapeutic and Detection: "Identify RNA motifs that bind recombinant ovine PrP of the susceptible-specific or resistant-specific alleles. Since the main phenotype in prion diseases consists in alterations of PrP’s properties, uncertainties about PrP’s functions represent a major obstacle in our understanding of the pathological process and impedes any attempt towards prevention and therapeutics of prion diseases."
Reference (2006, Arch Virol ): Mercey, R., Lantier, I., Maurel, M. C., Grosclaude, J., Lantier, F., & Marc, D. (2006). Fast, reversible interaction of prion protein with RNA aptamers containing specific sequence patterns. Archives of virology, 151(11), 2197–2214. https://doi.org/10.1007/s00705-006-0790-3
Aptamer: RM207
Target: Recombinant ovine PrP (Prion protein) of the susceptible-specific (V136R154Q171)
Type of nucleic acid: ssRNA
Sequence: 5'GAGGAUCCGCCGAGUAACAGUGCCAUGAGUGAAAUAAAACCAUCCGGAACUAAGACUGCGCUUGAGGCUCGAAUUCGCCC3'
Sequence length: 80
GC content: 0.525
Affinity: Kd: 55.3 ± 1.4 nM (VRQ)
Pool type: 5'-GAGGATCCGCCGAGTAACAG-N40-CTTGAGGCTCGAATTCGCCC-3'
Pool random region: 40
Binding buffer/conditions: 50 mM Tris, 125 mM NaCl, 5 mM MgCl2, pH 8
Divalent salt: MgCl
Buffer type: Tris Buffers
pH: 8
Molecular weight of target: Not reported
Post-SELEX modifications: Not applicable
Application as quoted in the referenced paper: Therapeutic and Detection: "Identify RNA motifs that bind recombinant ovine PrP of the susceptible-specific or resistant-specific alleles. Since the main phenotype in prion diseases consists in alterations of PrP’s properties, uncertainties about PrP’s functions represent a major obstacle in our understanding of the pathological process and impedes any attempt towards prevention and therapeutics of prion diseases."
Reference (2006, Arch Virol ): Mercey, R., Lantier, I., Maurel, M. C., Grosclaude, J., Lantier, F., & Marc, D. (2006). Fast, reversible interaction of prion protein with RNA aptamers containing specific sequence patterns. Archives of virology, 151(11), 2197–2214. https://doi.org/10.1007/s00705-006-0790-3