RosettaCommons/UTexasAptamer huggingface dataset:
Aptamer: Apt1
Target: Prion protein rPrP23-231 (rPrPc) fused to glutathione S-transferase (GST), Recombinant Syrian golden hamster
Type of nucleic acid: ssRNA
Sequence: 5'GGAGCUCAGCCUUCACUGCACGAAUUCGUUGUGCGGGAAUUUGAGGGACGAUGGGGAAGUGGGACGAAUGACUCAUUGCCGCGGUAGGGUUAGGCACCACGGUCGGAUCC3'
Sequence length: 110
GC content: 0.5818181818181818
Affinity: Not reported 
Pool type: 5'-GGAGCTCAGCCTT-CACTGC-N74-GGCACC-ACGGTCGGATCC-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: SRB-2
Target: Fluorophore sulforhodamine B
Type of nucleic acid: ssRNA
Sequence: 5'GGAACACUAUCCGACUGGCACCUGUGCUCUAUAGCAGAAUGCUAACAUUAGAUGAUGGAGGGGCGCAAGGUUAACCGCCUCAGUACAUCGGUGCCUUGGUCAUUAGGAUCCCG3'
Sequence length: 113
GC content: 0.5221238938053098
Affinity: Kd: 70 ± 10 nM
Pool type: 5'-AACACTATCCGACTGGCACC-N72-CCTTGGTCATTAGGATCCCG-3'
Pool random region: 72
Binding buffer/conditions: 100 mM KCl, 5 mM MgCl2, 10 mM Na-HEPES, pH 7.4
Divalent salt: MgCl
Buffer type: Other Buffers
pH: 7.4
Molecular weight of target: Not reported
Application as quoted in the referenced paper: Detection and Diagnostic: "In addition to serving as a model system for understanding the basis of RNA folding and function, these experiments demonstrate potential applications for the aptamers in transcript double labeling or fluorescence resonance energy transfer studies. Fluorophore-specific aptamers would also serve as a logical starting point for the evolution of ribozymes capable of utilizing fluorigenic substrates; such ribozymes could be readily introduced into diagnostic assays, possibly coupled directly with PCR-based detection methods."
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, Fold Des ): Holeman, L. A., Robinson, S. L., Szostak, J. W., & Wilson, C. (1998). Isolation and characterization of fluorophore-binding RNA aptamers. Folding & design, 3(6), 423–431. https://doi.org/10.1016/S1359-0278(98)00059-5
Aptamer: C #128
Target: Streptomycin
Type of nucleic acid: ssRNA
Sequence: 5'GGAGCUCAGCCUUCACUGCACCCCUUUGUGGGAACGCAAAACUAAAGGAAGAUCUCAAGAAAGGUGGAUCGCAUUUGGACUUCUGCCCAGGGUGGCACCACGGUCGGAUCCAC3'
Sequence length: 113
GC content: 0.5486725663716814
Affinity: Not reported
Pool type: 5'-GGAGCUCAGCCUUCACUGC-N74-GGCACCACGGUCGGAUCCAC3'
Pool random region: 74
Binding buffer/conditions: 5 mM MgCl2, 50 mM Tris-HCl, pH 7.6, 250 mM NaCl
Divalent salt: MgCl
Buffer type: Tris Buffers
pH: 7.6
Molecular weight of target: Not reported
Application as quoted in the referenced paper: Drug Development: "A growing body of evidence points to RNA as a crucial target for antibacterial and antiviral drugs. For example, the aminocyclitol antibiotic streptomycin interacts with the 16S ribosomal RNA and, in addition, inhibits group I intron splicing. To understand the mode of binding of streptomycin to RNA, we isolated small, streptomycin-binding RNA aptamers via in vitro selection"
Reference (1998, RNA ): Wallace, S. T., & Schroeder, R. (1998). In vitro selection and characterization of streptomycin-binding RNAs: recognition discrimination between antibiotics. RNA (New York, N.Y.), 4(1), 112–123.
Aptamer: RNA aptamer 3
Target: Human transcription factor NF-kB as a p50 homodimer (p502)
Type of nucleic acid: ssRNA
Sequence: 5'GGGAUAUCCUCGAGACAUAAGAAACAAGAUAGAUCCUGAAACUGUUUUAAGGUUGGCCGAUCUUCUGCUCGAGAAUGCAUGAAGCGUUCCAUAUUUUU3'
Sequence length: 98
GC content: 0.4081632653061224
Affinity: Kd: 1.34 ± 0.2 nM 
Pool type: 5‘-AAAAATATGGAACGCTTCATGCAT-N60-CTCGAGGATATCCCTATAGTG-3'
Pool random region: 60
Binding buffer/conditions: 10 mM HEPES, pH 7.5, 0.1 M NaCl, 1 mM DTT
Buffer type: Other Buffers
pH: 7.5
Molecular weight of target: Not reported
Application as quoted in the referenced paper: Therapeutic  and Inhibition: "We used in vitro selection to isolate a small RNA aptamer that binds with nanomolar affinity to human transcription factor NF-kappa B, a key regulator of inflammation, HIV-1 gene expression, and apoptosis. Expression of this aptamer structure within heterologous nuclear RNA transcripts may provide a new strategy to inhibit NF-kappa B function in vivo. Aptamers that inhibit transcription factors might be useful in a variety of applications."
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 (1999, Biochemistry ): Lebruska, L. L., & Maher, L. J., 3rd (1999). Selection and characterization of an RNA decoy for transcription factor NF-kappa B. Biochemistry, 38(10), 3168–3174. https://doi.org/10.1021/bi982515x
Aptamer: 109.2-3
Target: Prokaryotic 16s-rRNA region
Type of nucleic acid: ssRNA
Sequence: 5'GGGAGAAUUCCGACCAGAAGCCUUCUCCUGCCGCGCGAUUUUACGCCGACAAGGGUGGCAUGAUGAUGUGUCUNUAUAUAGCAUAUGUGCGUCUACAUGGAUCCUCA3'
Sequence length: 106
GC content: 0.5094339622641509
Affinity: Kd: 1.236 ± 0.051 uM
Pool type: 5'-GGGAGAATTCCGACCAGAAGC-N60-CATATGTGCGTCTACATGGATCCTCA-3'
Pool random region: 60
Binding buffer/conditions: 1 M NaCl, 50 mM Tris–HCl, 3 mM MgCl2, pH 7.4
Divalent salt: MgCl
Buffer type: Tris Buffers
pH: 7.4
Molecular weight of target: Not reported
Post-SELEX modifications: Not applicable
Application as quoted in the referenced paper: Research: " RNA-RNA recognition is a critical process in controlling many key biological events, such as translation and ribozyme functions. The recognition process governing RNA-RNA interactions can involve complementary Watson-Crick (WC) base pair binding, or can involve binding through tertiary structural interaction. These studies suggest that the RNA aptamer 109.2-3 interacts with the simple 27 nt A-site decoding region of 16S rRNA through their respective stem-loops."
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 (2000, Nucleic Acids Res ): Tok, J. B., Cho, J., & Rando, R. R. (2000). RNA aptamers that specifically bind to a 16S ribosomal RNA decoding region construct. Nucleic acids research, 28(15), 2902–2910. https://doi.org/10.1093/nar/28.15.2902
Aptamer: 08-09
Target: Pepocin
Type of nucleic acid: ssRNA
Sequence: 5'GGGAAUGGAUCCACAUCUACGUAUUCAACCAAGUCUAAUGUCGGACUCGAUAUCAAUUCACUGCAGACUUGACGAAGCUU3'
Sequence length: 80
GC content: 0.4375
Affinity: Kd: 21.0 ± 2.0 nM
Pool type: 5'-GGGAAUGGAUCCACAUCUACGUAUUC-N30-UUCACUGCAGACUUGACGAAGCUU-3'
Pool random region: 30
Binding buffer/conditions: 3 mM sodium phosphate, 3 mM MgCl2, 45 mM NaCl, 2.5 mM EDTA, 3 mM Tris-HCl (pH 7.5), 0.15 mM dithiothreitol, and 12% glycerol
Divalent salt: MgCl
Buffer type: PBS/phosphate buffers
pH: 7.5
Molecular weight of target: Not reported
Post-SELEX modifications: Not applicable
Application as quoted in the referenced paper: Therapeutic: " bind to the Ribosome Inactivating Protein (RIP) pepocin, which acts as a toxin. The aptame rinhibit the N-glycosidase activity of pepocin on rat liver 28 S rRNA. Competitive binding experiments using aptamer variants suggest that the conserved hairpin region in the anti-pepocin aptamer binds near the catalytic site on pepocin and prevents the interaction of pepocin and 28 S rRNA. Anti-RIP aptamers have potential use in diagnostic systems for the detection of pepocin or could be used as therapy to prevent the action of pepocin in mammalian cells."
Reference (2000, J Biol Chem ): Hirao, I., Madin, K., Endo, Y., Yokoyama, S., & Ellington, A. D. (2000). RNA aptamers that bind to and inhibit the ribosome-inactivating protein, pepocin. The Journal of biological chemistry, 275(7), 4943–4948. https://doi.org/10.1074/jbc.275.7.4943
Aptamer: Clone 3
Target: N-methyl mesoporphyrin IX (NMM)
Type of nucleic acid: 2'-amino-RNA
Sequence: 5'UAGGGAAUUCGUCGACGGAUCCUGAACGGAGGGCGGAUGUAGAACAGGGGCUGGAAUGAUUCGGGAUUUUCUGCUGCAGGUCGACGCAUGCGCCG3'
Sequence length: 95
GC content: 0.5789473684210527
Affinity: Kd: 0.25 μM
Pool type: 5'-TAGGGAATTCGTCGACGGATCC-N59-CTGCAGGTCGACGCATGCGCCG-3'
Pool random region: 59
Binding buffer/conditions: 100 mM Tris-acetate (pH 7.4), 200 mM NaOAc, 25 mM KOAc,10 mM Mg(OAc)2, 0.5% Triton X-100, and 5% DSMO
Buffer type: Tris Buffers
pH: 7.4
Molecular weight of target: 580.7
Post-SELEX modifications: Not applicable
Application as quoted in the referenced paper: Bisosensor: " Peroxidase activities of RNAs containing 2'-amino groups, which were selected as aptamers binding to N-methylmesoporphyrin IX, were investigated. Some clones promoted the oxidation reaction of 2,2'-azinobis(3-ethylbenzothiazoline-6-sulfonic acid) (ABTS) with hydrogen peroxide (H(2)O(2)) in the presence of iron(III)-protoporphyrin (hemin), whereas others did not. By in vitro selection, we can produce various types of peroxidase-like non-natural RNAs."
Additional information: RNA is modified with 2' amino groups (2'-AmCTP)
Reference (2001, Biotechnol Bioeng ): Teramoto, N., Ichinari, H., Kawazoe, N., Imanishi, Y., & Ito, Y. (2001). Peroxidase activity of in vitro-selected 2'-amino RNAs. Biotechnology and bioengineering, 75(4), 463–468. https://doi.org/10.1002/bit.10078
Aptamer: D8
Target: Sephadex G-100
Type of nucleic acid: ssRNA
Sequence: 5′GGGAGUCGACCGACCAGAAGUCCGAGUAAUUUACGUUUUGAUACGGUUGCGGAACUUGCUAUGUGCGUCUACAUCUAGACUCAU3′
Sequence length: 84
GC content: 0.4761904761904761
Affinity: Not reported
Pool type: 5′-GGGAGUCGACCGACCAGAA-N40-UAUGUGCGUCUACAUCUAGACUCAU-3′
Pool random region: 40
Binding buffer/conditions: 50 mM HEPES pH 7.4, 10 mM MgCl2 and 100 mM NaCl
Divalent salt: MgCl
Buffer type: Other Buffers
pH: 7.4
Molecular weight of target: Not reported
Post-SELEX modifications: Not applicable
Application as quoted in the referenced paper: Detection: " Anti-Sephadex aptamers provide the means for rapid and powerful purification using the readily available Sephadex matrix as an affinity resin. This could find utility in a variety of applications."
Reference (2001, Nucleic Acids Res ): Srisawat, C. (2001). Sephadex-binding RNA ligands: rapid affinity purification of RNA from complex RNA mixtures. In Nucleic Acids Research (Vol. 29, Issue 2, pp. 4e–44). Oxford University Press (OUP). https://doi.org/10.1093/nar/29.2.e4
Aptamer: RNA 12 E4
Target: Adenine
Type of nucleic acid: ssRNA
Sequence: 5'GGGAGAGGAUACUACACGUGAUAGGACGAUUAUCGAAAAUCACCAGAUUGGACCCUGGUUAACGAUCCAUUGCAUGUAGCAGAAGCUUCCG3'
Sequence length: 91
GC content: 0.4725274725274725
Affinity: Kd: 10 uM
Pool type: 5'-CGGAAGCTTCTGCTACATGCAATGG-N50-CACGTGTAGTATCCTCTCCC-3'
Pool random region: 50
Binding buffer/conditions: 100 mM HEPES, 500 mM NaCl, 5 mM MgCl2, pH 7.3
Divalent salt: MgCl
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: Therapeutic: " RNA aptamers that are able to complex free adenine have been isolated by a SELEX (systematic evolution of ligands by exponential enrichment) procedure. Such binding is of great interest because the imidazole moiety is not trapped in the binding site, and would easily be available for catalytic activity."
Reference (2001, J Biol Chem ): Meli, M., Vergne, J., Décout, J. L., & Maurel, M. C. (2002). Adenine-aptamer complexes: a bipartite RNA site that binds the adenine nucleic base. The Journal of biological chemistry, 277(3), 2104–2111. https://doi.org/10.1074/jbc.M107130200
Aptamer: #30
Target: Mammalian translation initiation factor 4A (eIF4A)
Type of nucleic acid: ssRNA
Sequence: 5′GGGAGACAAGAAUAAAACGCUCAAUGUGGAUGAUUUGUAUGAUCGCGCAUACAAUUCGACAGGAGGCUCACAACAGGC3′
Sequence length: 78
GC content: 0.4615384615384615
Affinity: Kd: 1 μM
Pool type: 5′-GGGAGACAAGAATAAAACGCTCAA-N40-TTCGACAGGAGGCTCACAACAGGC-3′
Pool random region: 40
Binding buffer/conditions: Buffer A (20 mM Tris, pH 7.6, 80 mM potassium acetate, 2.5 mM magnesium acetate and 5% glycerol) and 100 Units RNase inhibitor (TaKaRa Co.)
Buffer type: Tris Buffers
pH: 7.6
Molecular weight of target: Not reported
Post-SELEX modifications: Not applicable
Application as quoted in the referenced paper: Therapeutic: " The mammalian translation initiation factor 4A (eIF4A) is a prototype member of the DEAD-box RNA helicase family that couples ATPase activity to RNA binding and unwinding. The selected RNAs, therefore, represent a new class of specific inhibitors that are suitable for the analysis of eukaryotic initiation, and which pose a potential therapeutic against malignancies that are caused by aberrant translational control."
Reference (2003, RNA ): Oguro, A., Ohtsu, T., Svitkin, Y. V., Sonenberg, N., & Nakamura, Y. (2003). RNA aptamers to initiation factor 4A helicase hinder cap-dependent translation by blocking ATP hydrolysis. RNA (New York, N.Y.), 9(4), 394–407. https://doi.org/10.1261/rna.2161303
Aptamer: A22
Target: Hemagglutinin (HA) glycoprotein; Influenza virus
Type of nucleic acid: ssDNA
Sequence: 5′AATTAACCCTCACTAAAGGGCTGAGTCTCAAAACCGCAATACACTGGTTGTATGGTCGAATAAGTTAA3′
Sequence length: 68
GC content: 0.3970588235294117
Affinity: Not reported
Pool type: 5′-AATTAACCCTCACTAAAGGG-N30-TATGGTCGAATAAGTTAA-3′
Pool random region: 30
Binding buffer/conditions: 50 mM Tris-HCl, pH 7.4, 5 mM KCl, 100 mM NaCl, 1 mM MgCl2, 100 μg tRNA, 0.2% bovine serum albumin
Divalent salt: MgCl
Buffer type: Tris Buffers
pH: 7.4
Molecular weight of target: Not reported
Post-SELEX modifications: Not applicable
Application as quoted in the referenced paper: Therapeutic: " Design of a novel molecule, comprising a ssDNA aptamer, which inhibits influenza infection by interfering with the virus-host cell interaction, via blocking of the receptor-binding region of the surface glycoprotein HA. This novel aptamer is therefore of interest, as it might be considered a suitable candidate for development as an alternative, selective inhibitory anti-influenza agent."
Additional information: The pool specifies N30 but is only 29nt long after the selection (39 contant region + 30 random regions was the anticipated result)
Reference (2004, J Biol Chem ): Jeon, S. H., Kayhan, B., Ben-Yedidia, T., & Arnon, R. (2004). A DNA aptamer prevents influenza infection by blocking the receptor binding region of the viral hemagglutinin. The Journal of biological chemistry, 279(46), 48410–48419. https://doi.org/10.1074/jbc.M409059200
Aptamer: #10
Target: T-Cell Factor-1 (TCF-1) protein
Type of nucleic acid: ssRNA
Sequence: 5'GGGGAGCUCGGUACCGGUGCGAUCCCCUGUUUACAUUGCAUGCUAGGACGACGCGCCCGAGCGGGUACCCAUUGUGUCGUCGGAAGCUUUGCAGAGGAUC3'
Sequence length: 100
GC content: 0.61
Affinity: Kd: 100~500 nM
Pool type: 5'-CGGAATTCCGGGGAGCTCGGTACC-N70-AAGCTTTGCAGAGGATCCTT-3'
Pool random region: 70
Binding buffer/conditions: 30 mM Tris-HCl (pH 7.5), 150 mM NaCl, 1.5 mM MgCl2, 2 mM DTT, 0.1% BSA, 100 ug/ml tRNA
Divalent salt: MgCl
Buffer type: Tris Buffers
pH: 7.5
Molecular weight of target: Not reported
Application as quoted in the referenced paper: Therapeutic: " TCF proteins are architectural transcription factors that bind to beta-catenin when the Wnt signaling pathway is activated. TCF-1 is specifically expressed in T-cell lineages and its interaction with beta-catenin is thought to be critical for early T-cell development. However, the mechanisms underlying activation of TCF-1 during T-cell development are not completely understood. It is hoped that the selected aptamers will regulate TCF-1 activity in vivo, thereby providing a unique tool for modulating TCF-1 function in early T-cell development."
Reference (2004, Mol Cells ): Lee, S. Y., & Jeong, S. (2004). In vitro selection and characterization of TCF-1 binding RNA aptamers. Molecules and cells, 17(1), 174–179.
Aptamer: R9-43
Target: Carbon storage regulation protein A, Escherichia coli (CsrA of E. coli)
Type of nucleic acid: ssRNA
Sequence: 5′ACCGAGUCCAGAAGCUUGUAGUACACAAGGAUGUGCCAUGCCUAGAUGGAGUUGAAUUCUCCCUAUAGUGAGUCGUAUUAC3′
Sequence length: 81
GC content: 0.4567901234567901
Affinity: Kd: 7.1 ± 0.8 nM
Pool type: 5′-ACCGAGTCCAGAAGCTTGTAGTAC-N15-GCCTAGATGGAGTTGAATTCTCCCTATAGTGAGTCGTATTAC-3′
Pool random region: 15
Binding buffer/conditions: 10 mM Tris-HCl, pH 7.5, 10 mM MgCl2, 100 mM KCl, 0.5 mg of yeast RNA, and 7.5% glycerol
Divalent salt: MgCl
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: Detection: " SELEX was used to isolate high-affinity CsrA ligands. The results presented herein establish that both the primary sequence and secondary structure of selected RNA ligands are important for high-affinity CsrA interaction. CsrA represses various processes such as gluconeogenesis, glycogen metabolism, and biofilm formation. CsrA also activates glycolysis, acetate metabolism, and flagellum biosynthesis."
Reference (2005, RNA ): Dubey, A. K., Baker, C. S., Romeo, T., & Babitzke, P. (2005). RNA sequence and secondary structure participate in high-affinity CsrA-RNA interaction. RNA (New York, N.Y.), 11(10), 1579–1587. https://doi.org/10.1261/rna.2990205
Aptamer: F52
Target: RNA-dependent RNA polymerase (3Dpol)
Type of nucleic acid: ssRNA
Sequence: 5'GGGAAUGGAUCCACAUCUACGAAUUCCUUACCCGUGAACCGCAGUUGCUGAGUUGUUCGAAGCAGUUCAGACGUCACUU3'
Sequence length: 79
GC content: 0.4936708860759494
Affinity: Kd: 625 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."
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: aptamer-2
Target: Biased conformation(s) of calsenilin
Type of nucleic acid: ssRNA
Sequence: 5′GGGACGCGUGGUACCGACGGAGGCUUGUUUAUGUAGGGAUGUAAGGGGAUGGGCAAUGUGGCGACAGCUUCCGCGGGGAUC3′
Sequence length: 81
GC content: 0.6049382716049383
Affinity: Kd: 43 nM for Ca2+ bound, 79 nM for Ca2+ unbound
Pool type: 5′-CGGAATTCGGGACGCGTGGTACC-N50-AAGCTTCCGCGGGGATCCAA-3′
Pool random region: 50
Binding buffer/conditions: 30 mM Tris (pH 7.5 at 25 °C), 150 mM NaCl, 1 mM MgCl2, 1 mM DTT, 5 mM EGTA, or 1 mM CaCl2
Divalent salt: MgCl/CaCl
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: Detection: " We have used SELEX (Systematic Evolution of Ligands by EXponential enrichment) technology to produce aptamers that bind in a conformationally selective manner to calsenilin, which involved in Ca(2+)-mediated apoptotic signaling. Aptamers selected against the two different conformations of calsenilin have different characteristics suggest that aptamers can serve as a plausible tool for recognizing various conformations of proteins, even those caused by interactions with small molecules or ions such as Ca(2+)."
Additional information: Aptamer-2, does not discriminate between the calcium-bound dimeric conformation and the calcium-deficient conformation of the protein. The paper given fixed region which has less nucleotides than the given pool (5′-Fixed region: GGGACGCGTGGTACC, 3′-fixed region: AGCTTCCGCGGGGAT). The given fixed region is used to construct the aptamer sequence. 
Since this is an RNA aptamer sequence, All the thymine converted to Uridine.
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 (2007, Bioorg Med Chem ): Lee, K. H., Jeong, S., Yang, E. G., Park, Y. K., & Yu, J. (2007). An RNA aptamer that recognizes a specific conformation of the protein calsenilin. Bioorganic & medicinal chemistry, 15(24), 7545–7552. https://doi.org/10.1016/j.bmc.2007.09.013
Aptamer: E2
Target: Amyloid beta-peptide (Aβ)
Type of nucleic acid: ssRNA
Sequence: 5'GGGAUGUUCUAGGCGGUUGAUGAUUUGGGGUGUCGGGCGAUUUUUAGGGUUGGGCCAGGCCGUCAUCCAGAGUAGCAUAAUUGAUCCGA3'
Sequence length: 89
GC content: 0.5280898876404494
Affinity: Kd: 10.9 μM
Pool type: 5′-GGGATGTTCTAGGCCGGTTGATGA-N40-CATCCAGAGTAGCATAATTTGATCCGA-3′
Pool random region: 40
Binding buffer/conditions: 10 mM Tris·HCl, pH 7.5, containing 150 mM NaCl, 5 mM MgCl2
Divalent salt: MgCl
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: " Aggregation of amyloid beta-peptide (Abeta) is closely related to the pathogenesis of Alzheimer's disease (AD). Using a systematic evolution of ligands using the exponential enrichment (SELEX) procedure, we have constructed RNA aptamers that bind to Abeta1-40 and inhibit aggregation. The selected RNA aptamers may have potential as therapeutic agents for AD pathogenesis."
Reference (2009, Mol Biosyst ): Takahashi, T., Tada, K., & Mihara, H. (2009). RNA aptamers selected against amyloid beta-peptide (Abeta) inhibit the aggregation of Abeta. Molecular bioSystems, 5(9), 986–991. https://doi.org/10.1039/b903391b