RosettaCommons/UTexasAptamer huggingface dataset:
Aptamer: R1-1
Target: Hepatitis C virus NS5B protein (HCV NS5B protein)
Type of nucleic acid: ssRNA
Sequence: 5'GGGAGCUCAGAAUAAACGCUCAACUCCUAACCUCUCCGCAUGNGCUGUUACCUACACAGCUCAGCAUGCAUGAGGCCCGGAUCCGGC3'
Sequence length: 86
GC content: 0.5697674418604651
Affinity: Kd: 100 ± 6 (1/s)
Pool type: 5'-GGGAGCUCAGAAUAAACGCUCAA-N40-GCAUGCAUGAGGCCCGGAUCCGGC-3'
Pool random region: 40
Binding buffer/conditions: 40 mM Tris–HCl, pH 8, 5 mM MgCl2, 5% glycerol
Divalent salt: MgCl
Buffer type: Tris Buffers
pH: 8
Molecular weight of target: 66 kDa
Post-SELEX modifications: Not applicable
Application as quoted in the referenced paper: Therapeutic and Detection: " Successful isolation of high-affinity RNA molecules would provide useful templates for further binding and enzymatic characterization of NS5B, as well as potential therapeutic application if these RNAs inhibit NS5B RdRp activity"
Reference (2003, Virology ): Vo, N. V., Oh, J. W., & Lai, M. M. (2003). Identification of RNA ligands that bind hepatitis C virus polymerase selectively and inhibit its RNA synthesis from the natural viral RNA templates. Virology, 307(2), 301–316. https://doi.org/10.1016/s0042-6822(02)00095-8
Aptamer: R20-43
Target: Hepatitis C virus NS5B protein (HCV NS5B protein)
Type of nucleic acid: ssRNA
Sequence: 5'GGGAGCUCAGAAUAAACGCUCAAUGUAGAGACUUUUCGAAAAGCGUGUUCCCAAUGAGUCUAUGCAUGCAUGAGGCCCGGAUCCGGC3'
Sequence length: 87
GC content: 0.5057471264367817
Affinity: Kd × 10e4: 1.0 ± 0.1 (1/s)
Pool type: 5'-GGGAGCUCAGAAUAAACGCUCAA-N40-GCAUGCAUGAGGCCCGGAUCCGGC-3'
Pool random region: 40
Binding buffer/conditions: 40 mM Tris–HCl, pH 8, 5 mM MgCl2, 5% glycerol
Divalent salt: MgCl
Buffer type: Tris Buffers
pH: 8
Molecular weight of target: 66 kDa
Post-SELEX modifications: Not applicable
Application as quoted in the referenced paper: Therapeutic and Detection: " Successful isolation of high-affinity RNA molecules would provide useful templates for further binding and enzymatic characterization of NS5B, as well as potential therapeutic application if these RNAs inhibit NS5B RdRp activity"
Reference (2003, Virology ): Vo, N. V., Oh, J. W., & Lai, M. M. (2003). Identification of RNA ligands that bind hepatitis C virus polymerase selectively and inhibit its RNA synthesis from the natural viral RNA templates. Virology, 307(2), 301–316. https://doi.org/10.1016/s0042-6822(02)00095-8
Aptamer: R20-15
Target: Hepatitis C virus NS5B protein (HCV NS5B protein)
Type of nucleic acid: ssRNA
Sequence: 5'GGGAGCUCAGAAUAAACGCUCAAUGUAGGCUAGUACCGACCUGCGUGCCUCGCUCCUUUUCAUGCAUGCAUGAGGCCCGGAUCCGGC3'
Sequence length: 87
GC content: 0.5747126436781609
Affinity: Kd × 10e4: 100 ± 6 (1/s)
Pool type: 5'-GGGAGCUCAGAAUAAACGCUCAA-N40-GCAUGCAUGAGGCCCGGAUCCGGC-3'
Pool random region: 40
Binding buffer/conditions: 40 mM Tris–HCl, pH 8, 5 mM MgCl2, 5% glycerol
Divalent salt: MgCl
Buffer type: Tris Buffers
pH: 8
Molecular weight of target: 66 kDa
Post-SELEX modifications: Not applicable
Application as quoted in the referenced paper: Therapeutic and Detection: " Successful isolation of high-affinity RNA molecules would provide useful templates for further binding and enzymatic characterization of NS5B, as well as potential therapeutic application if these RNAs inhibit NS5B RdRp activity"
Reference (2003, Virology ): Vo, N. V., Oh, J. W., & Lai, M. M. (2003). Identification of RNA ligands that bind hepatitis C virus polymerase selectively and inhibit its RNA synthesis from the natural viral RNA templates. Virology, 307(2), 301–316. https://doi.org/10.1016/s0042-6822(02)00095-8
Aptamer: 11-1
Target: Angiopoietin-2 (Ang2)
Type of nucleic acid: ssRNA
Sequence: 5′GGGAGGACGAUGCGGACUAGCCUCAUCAGCUCAUGUGCCCCUCCGCCUGGAUCACCAGACGACUCGCUGAGGAUCCGAGA3′
Sequence length: 80
GC content: 0.625
Affinity: Kd: 3.1 nM
Pool type: 5′-GGGAGGACGATGCGG-N40-CAGACGACTCGCTGAGGATCCGAGA-3′
Pool random region: 40
Binding buffer/conditions: 20 mM Hepes, pH 7.4/150 mM NaCl/2 mM CaCl2/0.01% BSA
Divalent salt: CaCl
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: Therapeutic: "These data join growing evidence that Ang2 is proangiogenic but are the first to directly demonstrate that specific inhibition of Ang2 is antiangiogenic. This aptamer not only validates Ang2 as a target for other inhibition strategies but may also be adapted itself as a therapeutic agent"
Reference (2003, Proc Natl Acad Sci U S A ): White, R. R., Shan, S., Rusconi, C. P., Shetty, G., Dewhirst, M. W., Kontos, C. D., & Sullenger, B. A. (2003). Inhibition of rat corneal angiogenesis by a nuclease-resistant RNA aptamer specific for angiopoietin-2. Proceedings of the National Academy of Sciences of the United States of America, 100(9), 5028–5033. https://doi.org/10.1073/pnas.0831159100
Aptamer: 11-1.41
Target: Angiopoietin-2 (Ang2)
Type of nucleic acid: ssRNA
Sequence: 5′GAGGACGAUGCGGACUAGCCUCAUCAGCUCAUGUGCCCCUC3′
Sequence length: 41
GC content: 0.6097560975609756
Affinity: Kd: 2.2 nM
Pool type: 5′-GGGAGGACGATGCGG-N40-CAGACGACTCGCTGAGGATCCGAGA-3′
Pool random region: 40
Binding buffer/conditions: 20 mM Hepes, pH 7.4/150 mM NaCl/2 mM CaCl2/0.01% BSA
Divalent salt: CaCl
Buffer type: Other Buffers
pH: 7.4
Molecular weight of target: Not reported
Post-SELEX modifications: 41-nt truncate of aptamer 11-1
Application as quoted in the referenced paper: Therapeutic: " These data join growing evidence that Ang2 is proangiogenic but are the first to directly demonstrate that specific inhibition of Ang2 is antiangiogenic. This aptamer not only validates Ang2 as a target for other inhibition strategies but may also be adapted itself as a therapeutic agent"
Reference (2003, Proc Natl Acad Sci U S A ): White, R. R., Shan, S., Rusconi, C. P., Shetty, G., Dewhirst, M. W., Kontos, C. D., & Sullenger, B. A. (2003). Inhibition of rat corneal angiogenesis by a nuclease-resistant RNA aptamer specific for angiopoietin-2. Proceedings of the National Academy of Sciences of the United States of America, 100(9), 5028–5033. https://doi.org/10.1073/pnas.0831159100
Aptamer: Spiegelmer STAR-F12
Target: Migraine-associated calcitonin gene-related peptide 1 (alpha-CGRP; α-CGRP)
Type of nucleic acid: 2'-O-Me-RNA
Sequence: 5′GGACUGAUGGCGCGGUCCUAUUACGCCGAAAGGGAGAGGGGAGACAGG3'
Sequence length: 48
GC content: 0.625
Affinity: Kd: 2.5 nM
Pool type: 5′-GGAC-N40-GACAGG-3'
Pool random region: 40
Binding buffer/conditions: 10 mM HEPES/KOH pH 7.4, 150 mM NaCl, 4 mM KCl with CaCl2 (final 1 mM), MgCl2 (final 1 mM) and Tween (final 0.05%)
Divalent salt: MgCl/CaCl
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: Therapeutic: " In order to prove the efficiency of Tailored-SELEX, we carried out an in vitro selection approach against the optical antipode of the neuropeptide calcitonin gene-related peptide 1 (α-CGRP) of rat. α-CGRP has been recognized as a potent vasodilator and has recently attracted attention as a novel target in acute migraine treatment"
Additional information: Three complexities of a combinatorial RNA library (5′-GGAC-N40-GACAGG) of 1015 different molecules, that was obtained by in vitro transcription of a synthetic ssDNA library (5′-COMeCOMeTGTC-N40-GTCCTATAGTGAGTCGTATTAGTAGTCGC) in the presence of a 1.5-fold excess of the forward primer (5′-GCGACTACTAATACGACTCACTATAGGAC), were used as the starting library. The last two nucleotides of the 5′ terminus of the DNA library were modified with 2′-methoxy-cytidines in order to reduce the non-templated nucleotide addition at the 3′ terminus of the in vitro transcripts.
Reference (2003, Nucleic Acids Res ): Vater, A., Jarosch, F., Buchner, K., & Klussmann, S. (2003). Short bioactive Spiegelmers to migraine-associated calcitonin gene-related peptide rapidly identified by a novel approach: tailored-SELEX. Nucleic acids research, 31(21), e130. https://doi.org/10.1093/nar/gng130
Aptamer: V-2
Target: Ribonucleases (RNase) H1, Human
Type of nucleic acid: ssDNA
Sequence: 5'GCCTGTTGTGAGCCTCCTCTCGAAGCTGGTCTCTGCGGGTTGTTGCGCCGCGGCACCCTTGGCATTGAGCGTTTATTCTTGTCTCCC3'
Sequence length: 87
GC content: 0.5977011494252874
Affinity: Kd: 26.5 ± 2.5 nM
Pool type: 5'-GCCTGTTGTGAGCCTCCTCTCGAA-N40-TTGAGCGTTTATTCTTGTCTCCC-3'
Pool random region: 40
Binding buffer/conditions: 30 mM Tris–HCl pH 8.5, 40 mM ammonium sulfate, 20 mM magnesium chloride, and 0.01% 2-mercaptoethanol
Buffer type: Tris Buffers
pH: 8.5
Molecular weight of target: Not reported
Post-SELEX modifications: Not applicable
Application as quoted in the referenced paper: Detection: " inhibition by the aptamers of the human RNase H1 and not RNase H2, and their ability to function in the reticulocyte lysate opens the way for their use as specific inhibitory tools to examine the roles of the two classes of RNase H in the general physiology of the cell and their relative participation in the success of antisense oligonucleotides"
Reference (2003, Nucleic Acids Res ): Pileur, F., Andreola, M. L., Dausse, E., Michel, J., Moreau, S., Yamada, H., Gaidamakov, S. A., Crouch, R. J., Toulmé, J. J., & Cazenave, C. (2003). Selective inhibitory DNA aptamers of the human RNase H1. Nucleic acids research, 31(19), 5776–5788. https://doi.org/10.1093/nar/gkg748
Aptamer: VI-2
Target: Ribonucleases (RNase) H2, Human
Type of nucleic acid: ssDNA
Sequence: 5'CGGTCGCTCCGTGTGGCTTGGGTTGGGTGTGGCAGTGAC3'
Sequence length: 39
GC content: 0.6666666666666666
Affinity: Kd: 11 ± 0.8 nM
Pool type: 5'-GCCTGTTGTGAGCCTCCTCTCGAA-N40-TTGAGCGTTTATTCTTGTCTCCC-3'
Pool random region: 40
Binding buffer/conditions: 30 mM Tris–HCl pH 8.5, 40 mM ammonium sulfate, 20 mM magnesium chloride, and 0.01% 2-mercaptoethanol
Buffer type: Tris Buffers
pH: 8.5
Molecular weight of target: Not reported
Post-SELEX modifications: Not applicable
Application as quoted in the referenced paper: Detection: " inhibition by the aptamers of the human RNase H1 and not RNase H2, and their ability to function in the reticulocyte lysate opens the way for their use as specific inhibitory tools to examine the roles of the two classes of RNase H in the general physiology of the cell and their relative participation in the success of antisense oligonucleotides"
Reference (2003, Nucleic Acids Res ): Pileur, F., Andreola, M. L., Dausse, E., Michel, J., Moreau, S., Yamada, H., Gaidamakov, S. A., Crouch, R. J., Toulmé, J. J., & Cazenave, C. (2003). Selective inhibitory DNA aptamers of the human RNase H1. Nucleic acids research, 31(19), 5776–5788. https://doi.org/10.1093/nar/gkg748
Aptamer: T710
Target: Thrombin, Bovine
Type of nucleic acid: ssRNA
Sequence: 5'GCAAUGGUACGGUACUUCCAAGUGCGGGGGGGAGGUGGUGGUUCCAAAAGUGCACGCUACUUUGCUAA3'
Sequence length: 68
GC content: 0.5441176470588235
Affinity: Kd: 240 nM
Pool type: 5'-CAATGGTACGGTACTTCC-N25-CAAAAGTGCACGCTACTTTGCTAA-3'
Pool random region: 25
Binding buffer/conditions: SHMCK, 20 mM Hepes, pH 7.35, 120 mM NaCl,
5 mM KCl, 1 mM CaCl2,1mM MgCl2 and 0.1% geletin, 0.05% Tween 20
Divalent salt: MgCl/CaCl
Buffer type: Other Buffers
pH: 7.35
Molecular weight of target: Not reported
Post-SELEX modifications: Not applicable
Application as quoted in the referenced paper: Therapeutic: " Bovine-specific thrombin inhibitor might be used in some clinical applications (i.e. cardiovascular surgery, otolaryngologic surgery and neurosurgery) when bovine thrombin activity needs to be contained or in research where human and bovine thrombin need to be distinguished"
Additional information: Pool includes T7 promotor region
Reference (2003, J Mol Recognit ): Liu, X., Zhang, D., Cao, G., Yang, G., Ding, H., Liu, G., Fan, M., Shen, B., & Shao, N. (2003). RNA aptamers specific for bovine thrombin. Journal of molecular recognition : JMR, 16(1), 23–27. https://doi.org/10.1002/jmr.604
Aptamer: A30
Target: Oligomeric state of the extracellular domains of human epidermal growth factor receptor-3 (HER3ECD)
Type of nucleic acid: ssRNA
Sequence: 5'GGGAAUUCCGCGUGUGCCAGCGAAAGUUGCGUAUGGGUCACAUCGCAGGCACAUGUCAUCUGGGCGGUCCGUUCGGGAUCCUC3'
Sequence length: 83
GC content: 0.6024096385542169
Affinity: Kd: 45 nM in hrg-unbound; 400 nM in hrg-bound
Pool type: 5'-GGAATTCCGCGTGTGC-N49-GTCCGTTCGGGATCCTC-3'
Pool random region: 49
Binding buffer/conditions: 10 mM Hepes, pH 7.4/100 mM NaCl/2.5 mM MgCl2
Divalent salt: MgCl
Buffer type: Other Buffers
pH: 7.4
Molecular weight of target: 82 kDa
Post-SELEX modifications: Not applicable
Application as quoted in the referenced paper: Therapeutic: " A30 can serve as a tool for the analysis of receptor interactions and may serve as a lead compound for the development of inhibitors against overexpressed receptor tyrosine kinases in carcinoma. Interference by large macromolecules with this first level of the signaling cascade holds therapeutic potential"
Reference (2003, Proc Natl Acad Sci U S A ): Chen, C. H., Chernis, G. A., Hoang, V. Q., & Landgraf, R. (2003). Inhibition of heregulin signaling by an aptamer that preferentially binds to the oligomeric form of human epidermal growth factor receptor-3. Proceedings of the National Academy of Sciences of the United States of America, 100(16), 9226–9231. https://doi.org/10.1073/pnas.1332660100
Aptamer: cl. 9
Target: Variant surface glycoprotein 221 (sVSG 221)
Type of nucleic acid: 2'-fluoro-RNA
Sequence: 5'GAAUUCAGUCGGACAGCGGGAUGAUGCCGCACUGACGCCACGUAGGUGGCGCACAGCCGAUGGACGAAUAUCGUCUCCC3'
Sequence length: 79
GC content: 0.6075949367088608
Affinity: Kd: 0.16 ± 0.02 nM
Pool type: 5' GAATTCAGTCGGACAGCG-N40-GATGGACGAATATCGTCTCCC-3'
Pool random region: 40
Binding buffer/conditions: buffer A (20 mM NaxHyPO4 [pH 7.4], 2 mM MgCl2, 130 mM NaCl, 5 mM KCl), 0.5 mM DTT, 1 μM 32P-labeled pool RNA, and 1 μM sVSG
Divalent salt: MgCl
Buffer type: PBS/phosphate buffers
pH: 7.4
Molecular weight of target: 60 kDa
Post-SELEX modifications: Not applicable
Application as quoted in the referenced paper: Detection and 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. Here, we generated RNA aptamers with high affinity for eIF4A by in vitro RNA selection-amplification. On binding, the RNAs inhibit ATP hydrolysis. 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."
Additional information: Pool taken from cited article (14) here: https://www.ncbi.nlm.nih.gov/pmc/articles/PMC148414/pdf/272006.pdf, 2′ F-modified RNA aptamers showed increased serum stability. The pool was 32P-labeled.
Reference (2003, Eukaryot Cell ): Lorger, M., Engstler, M., Homann, M., & Göringer, H. U. (2003). Targeting the variable surface of African trypanosomes with variant surface glycoprotein-specific, serum-stable RNA aptamers. Eukaryotic cell, 2(1), 84–94. https://doi.org/10.1128/EC.2.1.84-94.2003
Aptamer: cl. 9
Target: Variant surface glycoprotein 117 (sVSG 117)
Type of nucleic acid: 2'-fluoro-RNA
Sequence: 5'GAAUUCAGUCGGACAGCGGGAUGAUGCCGCACUGACGCCACGUAGGUGGCGCACAGCCGAUGGACGAAUAUCGUCUCCC3'
Sequence length: 79
GC content: 0.6075949367088608
Affinity: Not reported
Pool type: 5' GAATTCAGTCGGACAGCG-N40-GATGGACGAATATCGTCTCCC-3'
Pool random region: 40
Binding buffer/conditions: buffer A (20 mM NaxHyPO4 [pH 7.4], 2 mM MgCl2, 130 mM NaCl, 5 mM KCl), 0.5 mM DTT, 1 μM 32P-labeled pool RNA, and 1 μM sVSG
Divalent salt: MgCl
Buffer type: PBS/phosphate buffers
pH: 7.4
Molecular weight of target: 60 kDa
Post-SELEX modifications: Not applicable
Application as quoted in the referenced paper: Detection and 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. Here, we generated RNA aptamers with high affinity for eIF4A by in vitro RNA selection-amplification. On binding, the RNAs inhibit ATP hydrolysis. 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."
Additional information: Pool taken from cited article (14) here: https://www.ncbi.nlm.nih.gov/pmc/articles/PMC148414/pdf/272006.pdf, 2′ F-modified RNA aptamers showed increased serum stability. The pool was 32P-labeled.
Reference (2003, Eukaryot Cell ): Lorger, M., Engstler, M., Homann, M., & Göringer, H. U. (2003). Targeting the variable surface of African trypanosomes with variant surface glycoprotein-specific, serum-stable RNA aptamers. Eukaryotic cell, 2(1), 84–94. https://doi.org/10.1128/ec.2.1.84-94.2003
Aptamer: cl. 57
Target: Variant surface glycoprotein 221 (sVSG 221)
Type of nucleic acid: 2'-fluoro-RNA
Sequence: 5'GAAUUCAGUCGGACAGCGAGCGCGCACCUACUGUGAUGUAGAAGUCACAGCAAGGCCCGAUGGACGAAUAUCGUCUCCC3'
Sequence length: 79
GC content: 0.5569620253164557
Affinity: Kd: 0.03 ± 0.05
Pool type: 5' GAATTCAGTCGGACAGCG-N40-GATGGACGAATATCGTCTCCC-3'
Pool random region: 40
Binding buffer/conditions: buffer A (20 mM NaxHyPO4 [pH 7.4], 2 mM MgCl2, 130 mM NaCl, 5 mM KCl), 0.5 mM DTT, 1 μM 32P-labeled pool RNA, and 1 μM sVSG
Divalent salt: MgCl
Buffer type: PBS/phosphate buffers
pH: 7.4
Molecular weight of target: 60 kDa
Post-SELEX modifications: Not applicable
Application as quoted in the referenced paper: Detection and 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. Here, we generated RNA aptamers with high affinity for eIF4A by in vitro RNA selection-amplification. On binding, the RNAs inhibit ATP hydrolysis. 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."
Additional information: Pool taken from cited article (14) here: https://www.ncbi.nlm.nih.gov/pmc/articles/PMC148414/pdf/272006.pdf, 2′ F-modified RNA aptamers showed increased serum stability. The pool was 32P-labeled.
Reference (2003, Eukaryot Cell ): Lorger, M., Engstler, M., Homann, M., & Göringer, H. U. (2003). Targeting the variable surface of African trypanosomes with variant surface glycoprotein-specific, serum-stable RNA aptamers. Eukaryotic cell, 2(1), 84–94. https://doi.org/10.1128/ec.2.1.84-94.2003
Aptamer: cl. 57
Target: Variant surface glycoprotein 117 (sVSG 117)
Type of nucleic acid: 2'-fluoro-RNA
Sequence: 5'GAAUUCAGUCGGACAGCGAGCGCGCACCUACUGUGAUGUAGAAGUCACAGCAAGGCCCGAUGGACGAAUAUCGUCUCCC3'
Sequence length: 79
GC content: 0.5569620253164557
Affinity: Kd: 0.4 ± 0.09 nM 
Pool type: 5' GAATTCAGTCGGACAGCG-N40-GATGGACGAATATCGTCTCCC-3'
Pool random region: 40
Binding buffer/conditions: buffer A (20 mM NaxHyPO4 [pH 7.4], 2 mM MgCl2, 130 mM NaCl, 5 mM KCl), 0.5 mM DTT, 1 μM 32P-labeled pool RNA, and 1 μM sVSG
Divalent salt: MgCl
Buffer type: PBS/phosphate buffers
pH: 7.4
Molecular weight of target: 60 kDa
Post-SELEX modifications: Not applicable
Application as quoted in the referenced paper: Detection and 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. Here, we generated RNA aptamers with high affinity for eIF4A by in vitro RNA selection-amplification. On binding, the RNAs inhibit ATP hydrolysis. 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."
Additional information: Pool taken from cited article (14) here: https://www.ncbi.nlm.nih.gov/pmc/articles/PMC148414/pdf/272006.pdf, 2′ F-modified RNA aptamers showed increased serum stability. The pool was 32P-labeled.
Reference (2003, Eukaryot Cell ): Lorger, M., Engstler, M., Homann, M., & Göringer, H. U. (2003). Targeting the variable surface of African trypanosomes with variant surface glycoprotein-specific, serum-stable RNA aptamers. Eukaryotic cell, 2(1), 84–94. https://doi.org/10.1128/ec.2.1.84-94.2003
Aptamer: #11
Target: Mammalian translation initiation factor 4A (eIF4A)
Type of nucleic acid: ssRNA
Sequence: 5′GGGAGACAAGAAUAAAACGCUCAAACAUUGCAUCGACAGCUGCAAGGCUCCCGCCGUACAAACCUUCGACAGGAGGCUCACAACAGGC3′
Sequence length: 88
GC content: 0.5340909090909091
Affinity: Kd: 8 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: #20
Target: Mammalian translation initiation factor 4A (eIF4A)
Type of nucleic acid: ssRNA
Sequence: 5′GGGAGACAAGAAUAAAACGCUCAAGGGGACCGCGCCCCACAUGUGAGUGAGGCCGAAACGUAGAUUCGACAGGAGGCUCACAACAGGC3′
Sequence length: 88
GC content: 0.5681818181818182
Affinity: Kd: 44 nM
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