RosettaCommons/UTexasAptamer huggingface dataset:
Aptamer: 22B
Target: Basic fibroblast growth factor (bFGF)
Type of nucleic acid: ssRNA
Sequence: 5'GGGAGAUGCCUGUCGAGCAUGCUGAGGGUAACGUACUGGCAAGCUCACCUCAGCGUAGCUAAACAGCUUUGUCGACGGG3'
Sequence length: 79
GC content: 0.569620253164557
Affinity: Kd: exhibits biphasic binding, 0.13 ± 0.03 nM, 510 ± 30 nM
Pool type: 5'-GGGAGAUGCCUGUCGAGCAUGCUG-N30-GUAGCUAAACAGCUUUGUCGACGGG-3'
Pool random region: 30
Binding buffer/conditions: PBS = 10.1 mMNa2HPO4, 1.8 mM KH2PO4, 137 mM NaCl, 2.7 mM KCl, pH 7.4
Buffer type: PBS/phosphate buffers
pH: 7.4
Molecular weight of target: 18007 Da
Post-SELEX modifications: Not applicable
Application as quoted in the referenced paper: Detection: " Describe and characterize a set of high-affinity RNA ligands for bFGF that were selected from a pool of 10^14 molecules and show that these ligands inhibit binding of the growth factor to its cell-surface receptors. The idea that bFGF antagonists may have useful medicinal applications is not new (reviewed in ref. 5). bFGF is believed to play a key role in the development of smooth-muscle cell lesions following vascular injury. Overexpression of bFGF (and other members of the FGF family) is correlated with many malignant disorders"
Reference (1993, Proc Natl Acad Sci U S A ): Jellinek, D., Lynott, C. K., Rifkin, D. B., & Janjić, N. (1993). High-affinity RNA ligands to basic fibroblast growth factor inhibit receptor binding. Proceedings of the National Academy of Sciences of the United States of America, 90(23), 11227–11231. https://doi.org/10.1073/pnas.90.23.11227
Aptamer: 4
Target: Rev protein of HIV-1 (minimal Rev-binding element (RBE) found within the Rev Responsive Element (RRE))
Type of nucleic acid: ssRNA
Sequence: 5'AUUCUGUAGGUUGAGGUACGCAGACGGCUCUCUACAG3'
Sequence length: 37
GC content: 0.5135135135135135
Affinity: Kd: 1.9*
Pool type: 5'-AUUCUGU-N6.9-GUACGCAAGUAC-N6.9-ACAG-3'
Pool random region: 15
Binding buffer/conditions: 50 mM KCl, 50 mM Tris-Cl, pH 8.0
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: " A population of improved Rev-binding aptamers can be used to inhibit viral
replication, as opposed to a single RNA species. In contrast to other pharmaceuticals, this approach will make it extremely difficult for HIV-1 to accumulate mutations that can simultaneously evade a multitude of different RRE decays."
Additional information: *Activity values are described as "representing relative Kd's" with no units

6.9 means Both random sequence tracts were systematically varied from 6 to 9 nts in length.

Sequences at the defined 5' and 3' ends of the 79.9
pool are, respectively, 5'-GGTAATACGACTCACTATAGGG_x0002_AACTCG4TG4AGCGAATT-3' and 5'-GCCTATCTATCGGAT_x0002_CCACG-3'.
Reference (1993, Nucleic Acids Res ): Giver, L., Bartel, D., Zapp, M., Pawul, A., Green, M., & Ellington, A. D. (1993). Selective optimization of the Rev-binding element of HIV-1. Nucleic acids research, 21(23), 5509–5516. https://doi.org/10.1093/nar/21.23.5509
Aptamer: Aptamer 1
Target: Alpha thrombin (α-thrombin), Human
Type of nucleic acid: ssDNA
Sequence: 5'GGTTGGATTGGTTGG3'
Sequence length: 15
GC content: 0.5333333333333333
Affinity: IC50: 3-5uM
Pool type: Not reported
Binding buffer/conditions: 20 Mm Tris-acetate, 150 mM NaCl, 5mM Kcl, 1 mM CaCl2, 1 mM MgCl2 at pH 7.4
Divalent salt: MgCl/CaCl
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: " All aptamers were potent inhibitors of thrombin-induced platelet aggregation, thromboxane biosynthesis, Ca++ and fibrin clot formation, effective concentrations being in the nanomolar range. In the present study, we demonstrate that related aptamer sequences also exist in defibrotide and are involved in its antithrombin actions. These apatamers may also contribute to the antithrombotic and antiatherosclerotic activity of defibrotide in vivo."
Additional information: In 1992, Bock and collegues reported that single-stranded DNA oligomers, containing the consensus sequence GGNTGG2.5GGNTGG, specifically bind to thrombin and inhibit thrombin-induced fibrin clot formation (5). This study showed that aptamers, originally described as RNA molecules that bind to specific molecular targets (6), also exist in single-stranded DNA.
Reference (1994, Biochem Biophys Res Commun ): Bracht, F., & Schrör, K. (1994). Isolation and identification of aptamers from defibrotide that act as thrombin antagonists in vitro. Biochemical and biophysical research communications, 200(2), 933–937. https://doi.org/10.1006/bbrc.1994.1539
Aptamer: Aptamer 2
Target: Alpha thrombin (α-thrombin), Human
Type of nucleic acid: ssDNA
Sequence: 5'GGTTGGATCGGTTGG3'
Sequence length: 15
GC content: 0.6
Affinity: IC50: 3-5uM
Pool type: Not reported
Binding buffer/conditions: 20 Mm Tris-acetate, 150 mM NaCl, 5mM Kcl, 1 mM CaCl2, 1 mM MgCl2 at pH 7.4
Divalent salt: MgCl/CaCl
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: " All aptamers were potent inhibitors of thrombin-induced platelet aggregation, thromboxane biosynthesis, Ca++ and fibrin clot formation, effective concentrations being in the nanomolar range. In the present study, we demonstrate that related aptamer sequences also exist in defibrotide and are involved in its antithrombin actions. These apatamers may also contribute to the antithrombotic and antiatherosclerotic activity of defibrotide in vivo."
Additional information: In 1992, Bock and collegues reported that single-stranded DNA oligomers, containing the consensus sequence GGNTGG2.5GGNTGG, specifically bind to thrombin and inhibit thrombin-induced fibrin clot formation (5). This study showed that aptamers, originally described as RNA molecules that bind to specific molecular targets (6), also exist in single-stranded DNA.
Reference (1994, Biochem Biophys Res Commun ): Bracht, F., & Schrör, K. (1994). Isolation and identification of aptamers from defibrotide that act as thrombin antagonists in vitro. Biochemical and biophysical research communications, 200(2), 933–937. https://doi.org/10.1006/bbrc.1994.1539
Aptamer: Aptamer 3
Target: Alpha thrombin (α-thrombin), Human
Type of nucleic acid: ssDNA
Sequence: 5'GGATGGATCGGTTGG3'
Sequence length: 15
GC content: 0.6
Affinity: IC50: 3-5uM
Pool type: Not reported
Binding buffer/conditions: 20 Mm Tris-acetate, 150 mM NaCl, 5mM Kcl, 1 mM CaCl2, 1 mM MgCl2 at pH 7.4
Divalent salt: MgCl/CaCl
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: " All aptamers were potent inhibitors of thrombin-induced platelet aggregation, thromboxane biosynthesis, Ca++ and fibrin clot formation, effective concentrations being in the nanomolar range. In the present study, we demonstrate that related aptamer sequences also exist in defibrotide and are involved in its antithrombin actions. These apatamers may also contribute to the antithrombotic and antiatherosclerotic activity of defibrotide in vivo."
Additional information: Aptamer 3 was found in the PCR product from the double-stranded defibrotide precursor.
In 1992, Bock and collegues reported that single-stranded DNA oligomers, containing the consensus sequence GGNTGG2.5GGNTGG, specifically bind to thrombin and inhibit thrombin-induced fibrin clot formation (5). This study showed that aptamers, originally described as RNA molecules that bind to specific molecular targets (6), also exist in single-stranded DNA.
Reference (1994, Biochem Biophys Res Commun ): Bracht, F., & Schrör, K. (1994). Isolation and identification of aptamers from defibrotide that act as thrombin antagonists in vitro. Biochemical and biophysical research communications, 200(2), 933–937. https://doi.org/10.1006/bbrc.1994.1539
Aptamer: RT8
Target: Reverse Transcriptase of Type 1 Human Immunodeficiency Virus (HIV-1 RT)
Type of nucleic acid: ssDNA
Sequence: 5'CCCCTGCAGGTGATTTTGCTCAAGTAGCCAGTCAAGTTAATGGGTGCCATGCAGAAGCAAGTATCGCTAATCAGGCGGAT3'
Sequence length: 80
GC content: 0.5
Affinity: Kd: 5 nM; Ki: 13 nM
Pool type: 5'-CCCCTGCAGGTGATTTTGCTCAAGT-N35-AGTATCGCTAATCAGGCGGAT-3'
Pool random region: 35
Binding buffer/conditions: 200 mM KOAc, 50 mM TrisHC1, pH 8.0, 6 mM MgCl2, and 10 mM DTT
Divalent salt: MgCl
Buffer type: Tris Buffers
pH: 8
Molecular weight of target: 66 kDa (p66) polypeptide chain complexed with a 51 kDa (p51) polypeptide chain for a total weight of 117 kDa
Post-SELEX modifications: Not applicable
Application as quoted in the referenced paper: Therapeutic: " The importance of RT in the life cycle of HIV-1 and the lack of a natural function in the host cell make RT a preferred target for antiviral agents; high affinity and specificity for HIV-1 RT exhibited by the selected DNA ligands, along with their inhibitory effects, make them good candidates for structural investigations and potentially for therapeutic application"
Reference (1995, Biochemistry ): Schneider, D. J., Feigon, J., Hostomsky, Z., & Gold, L. (1995). High-affinity ssDNA inhibitors of the reverse transcriptase of type 1 human immunodeficiency virus. Biochemistry, 34(29), 9599–9610. https://doi.org/10.1021/bi00029a037
Aptamer: RT26
Target: Reverse Transcriptase of Type 1 Human Immunodeficiency Virus (HIV-1 RT)
Type of nucleic acid: ssDNA
Sequence: 5'CCCCTGCAGGTGATTTTGCTCAAGTTACGTGAGCGTGCTGTCCCCTAAAGGTGATACGTCAGTATCGCTAATCAGGCGGAT3'
Sequence length: 81
GC content: 0.5185185185185185
Affinity: Kd: 1 nM; Ki: 2.7 nM
Pool type: 5'-CCCCTGCAGGTGATTTTGCTCAAGT-N35-AGTATCGCTAATCAGGCGGAT-3'
Pool random region: 35
Binding buffer/conditions: 200 mM KOAc, 50 mM TrisHC1, pH 8.0, 6 mM MgCl2, and 10 mM DTT
Divalent salt: MgCl
Buffer type: Tris Buffers
pH: 8
Molecular weight of target: 66 kDa (p66) polypeptide chain complexed with a 51 kDa (p51) polypeptide chain for a total weight of 117 kDa
Post-SELEX modifications: Not applicable
Application as quoted in the referenced paper: Therapeutic: " The importance of RT in the life cycle of HIV-1 and the lack of a natural function in the host cell make RT a preferred target for antiviral agents; high affinity and specificity for HIV-1 RT exhibited by the selected DNA ligands, along with their inhibitory effects, make them good candidates for structural investigations and potentially for therapeutic application"
Reference (1995, Biochemistry ): Schneider, D. J., Feigon, J., Hostomsky, Z., & Gold, L. (1995). High-affinity ssDNA inhibitors of the reverse transcriptase of type 1 human immunodeficiency virus. Biochemistry, 34(29), 9599–9610. https://doi.org/10.1021/bi00029a037
Aptamer: 41t
Target: Platelet-derived growth factor (PDGF)-AB
Type of nucleic acid: ssDNA
Sequence: 5'CCGAAGCTTAATACGACTCACTATAGGGATCCGCCTGATTAGCGATACTTACTCAGGGCACTGCAAGCAATTGTGGTCCCAATGGGCTGAGTA3'
Sequence length: 94
GC content: 0.4893617021276595
Affinity: Kd: 0.138 ± 0.009 nM
Pool type: 5‘-CCGAAGCTTAATACGACTCACTATAGGGATCCGCCTGATTAGCGATACT-N40-ACTTGAGCAAAATCACCTGCAGGGG-3‘
Pool random region: 40
Binding buffer/conditions: PBSM (10.1 mM Na2HPO4, 1.8 mM KH2PO4, 137 mM NaCl and 2.7 mM KCl, 1 mM MgCl2, pH 7.4) containing 0.01% human serum albumin (HSA)
Divalent salt: MgCl
Buffer type: PBS/phosphate buffers
pH: 7.4
Molecular weight of target: Not reported
Post-SELEX modifications: Truncated versions of ligand 41
Application as quoted in the referenced paper: Therapeutic: " Many tumor cell lines have since been shown to produce and secrete PDGF, some of which also express the cognate PDGF receptors; paracrine effect on the tumor stroma and, in some tumor cell lines, autocrine growth stimulation by PDGF are therefore possible; These DNA ligands therefore represent lead compounds for a novel class of high-affinity, specific antagonists of PDGF-AB and PDGF-BB."
Additional information: [3′T] represents a 3′-3′-linked thymidine nucleotide added to reduce 3′-exonuclease-mediated degradation
Reference (1996, Biochemistry ): Green, L. S., Jellinek, D., Jenison, R., Ostman, A., Heldin, C. H., & Janjic, N. (1996). Inhibitory DNA ligands to platelet-derived growth factor B-chain. Biochemistry, 35(45), 14413–14424. https://doi.org/10.1021/bi961544+
Aptamer: 41t
Target: Platelet-derived growth factor (PDGF)-AA
Type of nucleic acid: ssDNA
Sequence: 5'CCGAAGCTTAATACGACTCACTATAGGGATCCGCCTGATTAGCGATACTTACTCAGGGCACTGCAAGCAATTGTGGTCCCAATGGGCTGAGTA3'
Sequence length: 94
GC content: 0.4893617021276595
Affinity: Kd: 49 ± 8 nM
Pool type: 5‘-CCGAAGCTTAATACGACTCACTATAGGGATCCGCCTGATTAGCGATACT-N40-ACTTGAGCAAAATCACCTGCAGGGG-3‘
Pool random region: 40
Binding buffer/conditions: PBSM (10.1 mM Na2HPO4, 1.8 mM KH2PO4, 137 mM NaCl and 2.7 mM KCl, 1 mM MgCl2, pH 7.4) containing 0.01% human serum albumin (HSA)
Divalent salt: MgCl
Buffer type: PBS/phosphate buffers
pH: 7.40000000000001
Molecular weight of target: Not reported
Post-SELEX modifications: Truncated versions of ligand 41
Application as quoted in the referenced paper: Therapeutic: " Many tumor cell lines have since been shown to produce and secrete PDGF, some of which also express the cognate PDGF receptors; paracrine effect on the tumor stroma and, in some tumor cell lines, autocrine growth stimulation by PDGF are therefore possible; These DNA ligands therefore represent lead compounds for a novel class of high-affinity, specific antagonists of PDGF-AB and PDGF-BB."
Additional information: [3′T] represents a 3′-3′-linked thymidine nucleotide added to reduce 3′-exonuclease-mediated degradation
Reference (1996, Biochemistry ): Green, L. S., Jellinek, D., Jenison, R., Ostman, A., Heldin, C. H., & Janjic, N. (1996). Inhibitory DNA ligands to platelet-derived growth factor B-chain. Biochemistry, 35(45), 14413–14424. https://doi.org/10.1021/bi961544+
Aptamer: 41t
Target: Platelet-derived growth factor (PDGF)-BB
Type of nucleic acid: ssDNA
Sequence: 5'CCGAAGCTTAATACGACTCACTATAGGGATCCGCCTGATTAGCGATACTTACTCAGGGCACTGCAAGCAATTGTGGTCCCAATGGGCTGAGTA3'
Sequence length: 94
GC content: 0.4893617021276595
Affinity: Kd: 0.129 ± 0.011 nM
Pool type: 5‘-CCGAAGCTTAATACGACTCACTATAGGGATCCGCCTGATTAGCGATACT-N40-ACTTGAGCAAAATCACCTGCAGGGG-3‘
Pool random region: 40
Binding buffer/conditions: PBSM (10.1 mM Na2HPO4, 1.8 mM KH2PO4, 137 mM NaCl and 2.7 mM KCl, 1 mM MgCl2, pH 7.4) containing 0.01% human serum albumin (HSA)
Divalent salt: MgCl
Buffer type: PBS/phosphate buffers
pH: 7.40000000000001
Molecular weight of target: Not reported
Post-SELEX modifications: Truncated versions of ligand 41
Application as quoted in the referenced paper: Therapeutic: " Many tumor cell lines have since been shown to produce and secrete PDGF, some of which also express the cognate PDGF receptors; paracrine effect on the tumor stroma and, in some tumor cell lines, autocrine growth stimulation by PDGF are therefore possible; These DNA ligands therefore represent lead compounds for a novel class of high-affinity, specific antagonists of PDGF-AB and PDGF-BB."
Additional information: [3′T] represents a 3′-3′-linked thymidine nucleotide added to reduce 3′-exonuclease-mediated degradation
Reference (1996, Biochemistry ): Green, L. S., Jellinek, D., Jenison, R., Ostman, A., Heldin, C. H., & Janjic, N. (1996). Inhibitory DNA ligands to platelet-derived growth factor B-chain. Biochemistry, 35(45), 14413–14424. https://doi.org/10.1021/bi961544+
Aptamer: LD174
Target: L-selectin–IgG fusion protein (LS-Rg)
Type of nucleic acid: ssDNA
Sequence: 5'CTACCTACGATCTGACTAGCCATTCACCATGGCCCCTTCCTACGTATGTTCTGCGGGTGGCTTACTCTCATGTAGTTCC3'
Sequence length: 79
GC content: 0.5189873417721519
Affinity: Kd: 5.5 ± 5.1 nM
Pool type: 5'-CTACCTACGATCTGACTAGC-N40-GCTTACTCTCATGTAGTTCC-3'
Pool random region: 40
Binding buffer/conditions: 20 mM Hepes, pH 7.5, 125 mM NaCl, 1 mM MgCl2, 1 mM CaCl2, 5 mM KCl) plus 0.01% (wt/vol) human serum albumin (Sigma Chemical Co., St. Louis, MO)
Divalent salt: MgCl/CaCl
Buffer type: Other Buffers
pH: 7.5
Molecular weight of target: Not reported
Post-SELEX modifications: Truncated at both the 5' and 3' ends (ld174t1)
Application as quoted in the referenced paper: Therapeutic: " Aptamers that bind with nanomolar affinity to L-selectin's lectin domain, prevent L-selectin from binding to SLex, and function in vivo to prevent the homing of human lymphocytes to lymph nodes in severe combined immunodeficiency (SCID) mice"
Reference (1996, J Clin Invest ): Hicke, B. J., Watson, S. R., Koenig, A., Lynott, C. K., Bargatze, R. F., Chang, Y. F., Ringquist, S., Moon-McDermott, L., Jennings, S., Fitzwater, T., Han, H. L., Varki, N., Albinana, I., Willis, M. C., Varki, A., & Parma, D. (1996). DNA aptamers block L-selectin function in vivo. Inhibition of human lymphocyte trafficking in SCID mice. The Journal of clinical investigation, 98(12), 2688–2692. https://doi.org/10.1172/JCI119092
Aptamer: BBS #4,14,15
Target: B52 protein
Type of nucleic acid: ssRNA
Sequence: 5'GGGAGAAUUCAACUGCCAUCUAGGCAGGGUAACGAUCAACCUGGCGACAGCUGCCCUGCCGUCCAAGUACUACAAGCUUCUGGACUCGGU3'
Sequence length: 90
GC content: 0.5555555555555556
Affinity: Kd: 50nM
Pool type: DNA Pool Version: 5'-ACCGAGTCCAGAAGCTTGTAGTACT-N40-GCCTAGATGGCAGTTGAATTCTCCCTATAGTGAGTCGTATTAC-3' & RNA Pool Version: 5'-GGGAGAAUUCAACUGCCAUCUAGGC-N40-AGUACUACAAGCUUCUGGACUCGGU-3'
Pool random region: 40
Binding buffer/conditions: 50 mM Tris-Cl [pH 7.6], 200 mM potassium acetate, 5 mM MgCl2, 2.5 mM dithiothreitol
Divalent salt: MgCl
Buffer type: Tris Buffers
pH: 7.6
Molecular weight of target: Not reported
Application as quoted in the referenced paper: Detection: " This has encouraged us to make use of BBS RNA as a genetic tool for dissecting B52 function in vivo, by creating Drosophila fly lines designed to overproduce BBS RNAs (40). We envision that the controlled and modulated expression of these RNA aptamers in living flies will serve as a specific, reversible, fast-acting B52 inhibitor that should provide insight into the function of B52 in vivo"
Additional information: The Drosophila SR protein B52 was cloned from an embryonic cDNA expression library by using a monoclonal antibody against a Drosophila protein associated with transcriptionally active loci on polytene chromosomes. The 59 constant sequence included a promoter for T7 RNA polymerase
Reference (1997, Mol Cell Biol ): Shi, H., Hoffman, B. E., & Lis, J. T. (1997). A specific RNA hairpin loop structure binds the RNA recognition motifs of the Drosophila SR protein B52. Molecular and cellular biology, 17(5), 2649–2657. https://doi.org/10.1128/MCB.17.5.2649
Aptamer: FC
Target: RNA polymerase II (Pol II), Saccharomyces cerevisiae (S. cerevisiae)
Type of nucleic acid: ssRNA
Sequence: 5'GGGCCGCUAAGUCCUCGCUCACGAUACAGCACUGAUUGCGGUCGAGGUAGCUUGAUGGGCCACGCGCGACUCGGAUCCAC3'
Sequence length: 80
GC content: 0.625
Affinity: Not reported
Pool type: 5'-GGGCCGCUAAGUCCUCGCUCA-N40-ACGCGCGACUCGGAUCCAC-3'
Pool random region: 40
Binding buffer/conditions: 50 mM Tris-HCl, pH 8, 100 mM ammonium sulfate
Buffer type: Tris Buffers
pH: 8
Molecular weight of target: Not reported
Application as quoted in the referenced paper: Research: " To probe the complex nucleic acid binding domains of yeast RNA polymerase II (Pol II), we have isolated in the presence of heparin RNA molecules that selectively bind to yeast Pol II. This possibility would open up a new experimental avenue for identifying vital functional domains of Pol II by genetic approaches."
Reference (1997, J Biol Chem ): Thomas, M., Chédin, S., Carles, C., Riva, M., Famulok, M., & Sentenac, A. (1997). Selective targeting and inhibition of yeast RNA polymerase II by RNA aptamers. The Journal of biological chemistry, 272(44), 27980–27986. https://doi.org/10.1074/jbc.272.44.27980
Aptamer: G4
Target: Farnesylated peptide modeled after the carboxyl terminus of K ras
Type of nucleic acid: ssRNA
Sequence: 5'GGGAGAAUUCCGACCAGAAGCCUGCUCAGGGGUGGGUCGUAUAAUUAGCGUAGGGAGGUAGUGGAUGAGUAAGCCUGGGAUGUCAUAUGUGCGUCUACAUGGAUCCUCA3'
Sequence length: 109
GC content: 0.5229357798165137
Affinity: Kd: 139 ± 12 nM
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: Cel#202
Target: Cellobiose
Type of nucleic acid: ssDNA
Sequence: 5′GTCAAGGTGGGTGGGTGGGGTTGGTTGTTGTTTTGA3'
Sequence length: 36
GC content: 0.5277777777777778
Affinity: Kd: 10−7 to 10−5 M
Pool type: 5′-ATAGGAGTCGACCGACCAGAA-N40-TATGTGCGTCTACATCTAGACTCAT-3'
Pool random region: 40
Binding buffer/conditions: 20 mM Tris, pH 7.5/100 mM NaCl/5 mM MgCl2
Divalent salt: MgCl
Buffer type: Tris Buffers
pH: 7.5
Molecular weight of target: Not reported
Post-SELEX modifications: Trunction:  Only the internal variable region of three aptamers in were used: the 41 mer of Cel#16, the 40 mer of Cel#183, and the 36 mer of Cel#204
Application as quoted in the referenced paper: Detection: " The results of this study suggest it should be possible to develop specific aptamers against a wide array of carbohydrate antigens. This work demonstrates that relatively simple carbohydrate antigens are potential targets for highly selective DNA ligands, suggesting that it should be possible to select DNA, RNA, and modified polynucleotide aptamers from random sequence pools as recognition tools for a array of surface antigens."
Reference (1998, Proc Natl Acad Sci U S A ): Yang, Q., Goldstein, I. J., Mei, H. Y., & Engelke, D. R. (1998). DNA ligands that bind tightly and selectively to cellobiose. Proceedings of the National Academy of Sciences of the United States of America, 95(10), 5462–5467. https://doi.org/10.1073/pnas.95.10.5462
Aptamer: 29A-OH
Target: Nucleolin
Type of nucleic acid: ssDNA
Sequence: 5'TTTGGTGGTGGTGGTTGTGGTGGTGGTGG3'
Sequence length: 29
GC content: 0.5862068965517241
Affinity: Not reported
Pool type: Not reported
Binding buffer/conditions: HEPES binding buffer (25 mmHEPES, pH 7.9, 4 mm KCl, 3 mmMgCl2)
Divalent salt: MgCl
Buffer type: Other Buffers
pH: 7.9
Molecular weight of target: 106-kDa
Application as quoted in the referenced paper: Therapeutic: " We present strong evidence that this protein is nucleolin, a multifunctional phos- phoprotein whose levels are related to the rate of cell proliferation. Our results indicate that binding of G-rich oligonucleotides to nucleolin may be responsible for their non-sequence-specific effects. Furthermore, these oligonucleotides represent a new class of potentially therapeutic agents with a novel mechanism of action"
Additional information: 3′-Modified oligonucleotides were purchased from Oligos Etc. (Wilsonville, OR) or synthesized at the University of Alabama at Birmingham using 3′-C3-amine CPG columns from Glen Research (Sterling, VA). Unmodified oligonucleotides were purchased from Life Technologies, Inc. 
Both 29A-OH (a 3′-unmodified analog of GRO29A) and TEL inhibited the growth of cells
Reference (1999, J Biol Chem ): Bates, P. J., Kahlon, J. B., Thomas, S. D., Trent, J. O., & Miller, D. M. (1999). Antiproliferative activity of G-rich oligonucleotides correlates with protein binding. The Journal of biological chemistry, 274(37), 26369–26377. https://doi.org/10.1074/jbc.274.37.26369