RosettaCommons/UTexasAptamer huggingface dataset:
Aptamer: GRO29A 
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: removed the 5' 3T cap and 3'aminoalkyl because they were found to be unnecessary for serum stability and protection from nuclease activity resulting in the AS1411/AGRO100 sequence 
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
One notable early modification made to the GRO29A sequence (Node 1A) removed the 5' 3T cap and 3'aminoalkyl because they were found to be unnecessary for serum stability and protection from nuclease activity resulting in the AS1411/AGRO100 sequence
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
Aptamer: B2
Target: Phenylalanine tRNA, Yeast
Type of nucleic acid: ssRNA
Sequence: 5'GGGAAUUCCGCGUGUGCUACGUAUCUUCAGGCGGUAACUAACUGUGCUGAGUCUAAUCUUUGUGAGGGACGGUAACAUAUGGUUCCCGCGUGGUCCGUUCGGGAUCCUC3'
Sequence length: 109
GC content: 0.5321100917431193
Affinity: binding efficiency: recovery as percentage of load: 66%; Kd: 12 ± 1.2 nM
Pool type: 5'-GGGAATTCCGCGTGTGC-N80-GTCCGTTCGGGATCCTC-3'
Pool random region: 80
Binding buffer/conditions: 0.25 M NaCl, 50 mM Tris–HCl pH 7.5, 10 mM MgCl2, 2 mM spermidine, 0.2 mM EDTA
Divalent salt: MgCl
Buffer type: Tris Buffers
pH: 7.5
Molecular weight of target: Not reported
Application as quoted in the referenced paper: Research: " Six RNA aptamers that bind to yeast phenylalanine tRNA were identified by in vitro selection from a random-sequence pool. The in vitro selection approach can be employed to address experimentally how prevalent different kinds of binding partners are for various target RNAs in unbiased searches of RNA sequence space"
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, EMBO J ): Scarabino, D., Crisari, A., Lorenzini, S., Williams, K., & Tocchini-Valentini, G. P. (1999). tRNA prefers to kiss. The EMBO journal, 18(16), 4571–4578. https://doi.org/10.1093/emboj/18.16.4571
Aptamer: QH'
Target: Integration host factor (IHF)
Type of nucleic acid: ssDNA
Sequence: 5′GCCTGCTTTTTTATACTAAGTTGGCAATTATAAAAAAGCATTGCTTATCAATTTGTTGCAACGAACAGGTCACTA3′
Sequence length: 75
GC content: 0.3333333333333333
Affinity: IC50: 11 nM
Pool type: 5′-GCCTGCTTTTTTATACTAAGTTGGCA-N21-CAATTTGTTGCAACGAACAGGTCACTA-3′
Pool random region: 21
Binding buffer/conditions: 50 mM Tris-Cl–50 mM KCl–50 μg of bovine serum albumin (BSA) per ml–3.75 μg of salmon sperm DNA per ml–10% glycerol–1 mM EDTA at pH 7.8
Buffer type: Tris Buffers
pH: 7.8
Molecular weight of target: Not reported
Application as quoted in the referenced paper: Research: " Integration host factor (IHF) is a bacterial protein that binds and severely bends a specific DNA target. To understand the essential determinants of IHF function, a similar selection will be used with recombination as the partition selector in order to ask how efficient recombination is associated with DNA affinity."
Reference (1999, J Bacteriol ): Goodman, S. D., Velten, N. J., Gao, Q., Robinson, S., & Segall, A. M. (1999). In vitro selection of integration host factor binding sites. Journal of bacteriology, 181(10), 3246–3255. https://doi.org/10.1128/JB.181.10.3246-3255.1999
Aptamer: WT
Target: Integration host factor (IHF)
Type of nucleic acid: ssDNA
Sequence: 5′GCCTGCTTTTTTATACTAAGTTGGCAATTATAAAAAAGCATTGCTTATCAATTTGTTGCAACGAACAGGTCACTA3′
Sequence length: 75
GC content: 0.3333333333333333
Affinity: IC50: 0.8 nM
Pool type: 5′-GCCTGCTTTTTTATACTAAGTTGGCA-N21-CAATTTGTTGCAACGAACAGGTCACTA-3′
Pool random region: 21
Binding buffer/conditions: 50 mM Tris-Cl–50 mM KCl–50 μg of bovine serum albumin (BSA) per ml–3.75 μg of salmon sperm DNA per ml–10% glycerol–1 mM EDTA at pH 7.8
Buffer type: Tris Buffers
pH: 7.8
Molecular weight of target: Not reported
Application as quoted in the referenced paper: Research: " Integration host factor (IHF) is a bacterial protein that binds and severely bends a specific DNA target. To understand the essential determinants of IHF function, a similar selection will be used with recombination as the partition selector in order to ask how efficient recombination is associated with DNA affinity."
Reference (1999, J Bacteriol ): Goodman, S. D., Velten, N. J., Gao, Q., Robinson, S., & Segall, A. M. (1999). In vitro selection of integration host factor binding sites. Journal of bacteriology, 181(10), 3246–3255. https://doi.org/10.1128/JB.181.10.3246-3255.1999
Aptamer: 1-52
Target: Integration host factor (IHF)
Type of nucleic acid: ssDNA
Sequence: 5′GCCTGCTTTTTTATACTAAGTTGGCAAGGATTCGTCTTGTCCCGAAATCAATTTGTTGCAACGAACAGGTCACTA3′
Sequence length: 75
GC content: 0.4133333333333333
Affinity: IC50: 42 nM
Pool type: 5′-GCCTGCTTTTTTATACTAAGTTGGCA-N21-CAATTTGTTGCAACGAACAGGTCACTA-3′
Pool random region: 21
Binding buffer/conditions: 50 mM Tris-Cl–50 mM KCl–50 μg of bovine serum albumin (BSA) per ml–3.75 μg of salmon sperm DNA per ml–10% glycerol–1 mM EDTA at pH 7.8
Buffer type: Tris Buffers
pH: 7.8
Molecular weight of target: Not reported
Application as quoted in the referenced paper: Research: " Integration host factor (IHF) is a bacterial protein that binds and severely bends a specific DNA target. To understand the essential determinants of IHF function, a similar selection will be used with recombination as the partition selector in order to ask how efficient recombination is associated with DNA affinity."
Additional information: class II site, modest affinity for IHF but no formation of a discrete complex, poor in both excisive and integrative recombination
Reference (1999, J Bacteriol ): Goodman, S. D., Velten, N. J., Gao, Q., Robinson, S., & Segall, A. M. (1999). In vitro selection of integration host factor binding sites. Journal of bacteriology, 181(10), 3246–3255. https://doi.org/10.1128/JB.181.10.3246-3255.1999
Aptamer: R-39
Target: Trans-activation responsive (TAR) RNA element of HIV-1
Type of nucleic acid: ssRNA
Sequence: 5'GGUUACCAGCCUUCACUGCACAGCCUCACUCCGGUCCCAGACGAAGUGACGGCACCAUGUGAGAAGCCCUACUGUGCCCGCACCACGGUCGGUCACAC3'
Sequence length: 98
GC content: 0.6224489795918368
Affinity: Not reported 
Pool type: 5'-GGUUACCAGCCUUCACUGC-N60-GCACCACGGUCGGUCACAC-3'
Pool random region: 60
Binding buffer/conditions: R buffer (20 mM HEPES, pH 7.3, at 208C contain-ing 20 mM sodium acetate, 140 mM potassium acetate,and 3 mM magnesium acetate)
Buffer type: Other Buffers
pH: 7.3
Molecular weight of target: Not reported
Application as quoted in the referenced paper: Research: " Numerous RNA structures act as regulatory domains of gene expression, generally through the binding of proteins. Tertiary RNA interactions are known to play a key role in several biological processes. A pseudo-knot is responsible for the ribosomal frame-shifting on the mRNA of the Infectious Bronchitis Virus. Loop–loop interactions are also involved in the regulation of the copy number of the plasmid ColE1. Ligands specific for such structures would constitute an efficient means for interfering with the regulatory processes that they mediate. This strategy offered a way to identify key determinants of loop–loop interactions and to generate high affinity ligands of TAR RNA structure."
Additional information: slightly weaker binder than R-06 24
Reference (1999, RNA ): Ducongé, F., & Toulmé, J. J. (1999). In vitro selection identifies key determinants for loop-loop interactions: RNA aptamers selective for the TAR RNA element of HIV-1. RNA (New York, N.Y.), 5(12), 1605–1614. https://doi.org/10.1017/s1355838299991318
Aptamer: 26-5'
Target: Hematoporphyrin IX (HPIX)
Type of nucleic acid: ssDNA
Sequence: 5'ATGGGGTCGGGCGGGCCGGGTGTC3'
Sequence length: 24
GC content: 0.7916666666666666
Affinity: Kd: 1.5x10^-5 M
Pool type: 5'-TAGGGAATTCGTCGACGGATCC-N59-CTGCAGGTCGACGCATGCGCCG-3'
Pool random region: 59
Binding buffer/conditions: 100 mM Tris±acetate pH 8.0, 200 mM sodium acetate,50 mM potassium acetate, 25 mM magnesium acetate,5% dioxane
Buffer type: Tris Buffers
pH: 8
Molecular weight of target: Not reported
Post-SELEX modifications: To determine which sequence is necessary to recognize hpix, these two ssdnas were synthesized for aptamer 26 and their binding affinity to hpix was analyzed.
Application as quoted in the referenced paper: Detection: " In the present study, we selected single-stranded DNAs (ssDNAs) which were capable of binding to hematoporphyrin IX (HPIX) with μM order of dissociation constants. Structural analysis of these aptamers indicated that guanine-rich (G-rich) sequences are necessary for recognition of HPIX. From the CD spectrum of the binding site of the aptamer, the structure of G-rich sequence is indicated to form the parallel guanine-quartet (G-quartet)."
Reference (2000, Bioorg Med Chem Lett ): Okazawa, A., Maeda, H., Fukusaki, E., Katakura, Y., & Kobayashi, A. (2000). In vitro selection of hematoporphyrin binding DNA aptamers. Bioorganic & medicinal chemistry letters, 10(23), 2653–2656. https://doi.org/10.1016/s0960-894x(00)00540-0
Aptamer: B-6
Target: R5 helix peptide
Type of nucleic acid: ssRNA
Sequence: 5'GGGAAACUGGAUGGAAUGGGCUCGCAAGGCCCCCUGAGCUGCACAAGUUCAUGGCGAGGUCCUGCUGUAAGUGUGCCA3'
Sequence length: 78
GC content: 0.5897435897435898
Affinity: Kd: 10 nM
Pool type: 5'-GGGAAACUGG AUGGAAUGGGCUCG -N30-CGAGGUCCUGCUGUAAGUGUGCCA-3'
Pool random region: 30
Binding buffer/conditions: 10 mM HEPES, pH7.5, lOOmMNaCI
Buffer type: Other Buffers
Molecular weight of target: Not reported
Post-SELEX modifications: Not applicable
Application as quoted in the referenced paper: Drug delivery and inhibition: "RNA-binding proteins play a key role in fundamental cellular processes such as translation mRNA processing and early development, and in viral processes on infection by RNA viruses. Understanding RNA-protein interactions is important to study how RNA-binding proteins recognize specifically the target RNA and for drug design to inhibit infection of RNA viruses."
Reference (2000, Nucleic Acids Symp Ser ): Fukusho, S., Furusawa, H., & Okahata, Y. (2000). In vitro selection and analysis of RNA aptamer recognize arginine-rich motif (ARM) model peptide on a QCM. Nucleic acids symposium series, (44), 187–188. https://doi.org/10.1093/nass/44.1.187
Aptamer: RNA5
Target: Release factor 1 (RF1), Thermus thermophilus (T. thermophilus)
Type of nucleic acid: ssRNA
Sequence: 5'GGGAGAGGAUACUACACGUGGUGUGUCAAGCCAGCCCUAGCUUGCUACCUGGGGGCCACUGACCUAUCCAUUGCAUGUAGCAGAAGCUUCCG3'
Sequence length: 92
GC content: 0.5652173913043478
Affinity: Kd: 2 x 10^-5 M
Pool type: 5'-GGGAGAGGAUACUACACGUG-N50-CCAUUGCAUGUAGCAGAAGCUUCCG-3'
Pool random region: 50
Binding buffer/conditions: 50 mM Tris^HCl, pH 7.5, 50 mM NaCl and 7 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: Research: " Specific inhibition of RF1 by RF1 aptamers leads to increased efficiency of read-through of mRNA amber codons during in vitro translation. This effect may be of particular interest in all cases where increased efficiency of suppression is desirable, e.g. to facilitate incorporation of unnatural amino acids into protein via suppression of non-sense codons"
Reference (2002, FEBS Lett ): Szkaradkiewicz, K., Nanninga, M., Nesper-Brock, M., Gerrits, M., Erdmann, V. A., & Sprinzl, M. (2002). RNA aptamers directed against release factor 1 from Thermus thermophilus. FEBS letters, 514(1), 90–95. https://doi.org/10.1016/s0014-5793(02)02308-6
Aptamer: T705
Target: Thrombin, Bovine
Type of nucleic acid: ssRNA
Sequence: 5'GCAAUGGUACGGUACUUCCUUUGGAAGAUAGCUGGAGAACUAACCAAAAGUGCACGCUACUUUGCUAA3'
Sequence length: 68
GC content: 0.4411764705882353
Affinity: Kd: 164 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: #1
Target: Mammalian translation initiation factor 4A (eIF4A)
Type of nucleic acid: ssRNA
Sequence: 5′GGGAGACAAGAAUAAAACGCUCAACAGGCGUUUAGCCUCUAAGUAACAGGGGCCUCCCAUGAGCUUCGACAGGAGGCUCACAACAGGC3′
Sequence length: 88
GC content: 0.5340909090909091
Affinity: Kd: 3 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: #15
Target: Pro‐urokinase (PLAU), Human
Type of nucleic acid: ssDNA
Sequence: 5′GACACCTGCGGATCCAAAGCGATGGCATGAACAGGGTGAAGTATGGGATGCCCATCGCAGCCCTGCAGGCTCTTCAG3'
Sequence length: 77
GC content: 0.5844155844155844
Affinity: Not reported
Pool type: 5′‐GACACCTGCGGATCCAAAGCGATGGC-N24-CCCATCGCAGCCCTGCAGGCTCTTCAG-3'
Pool random region: 24
Binding buffer/conditions: Not reported
Buffer type: Not Reported
Molecular weight of target: Not reported
Post-SELEX modifications: Not applicable
Application as quoted in the referenced paper: Detection: " Detection of Human pro‐urokinase (PLAU) for thrombolytic therapy of acute myocardial infarction and acute ischemic stroke. We have isolated singlestranded DNA molecules with significantly increased binding affinity for human prourokinase by SELEX (systematic evolution of ligands by exponential enrichment) procedure from a pool of 1015 molecules containing 24 randomized positions which are flanked by defined regions."
Additional information: Selection is done with sDNA from this library that was radiolabelled by polynucleotide kinase and hybridized with a 37-nucleotide helper fixture
Reference (2004, Nucleosides Nucleotides Nucleic Acids ): Skrypina, N. A., Savochkina, L. P., & Beabealashvilli, R. S.h (2004). In vitro selection of single-stranded DNA aptamers that bind human pro-urokinase. Nucleosides, nucleotides & nucleic acids, 23(6-7), 891–893. https://doi.org/10.1081/NCN-200026037
Aptamer: 12
Target: Tumor necrosis factor alpha (hTNFα), Human
Type of nucleic acid: ssRNA
Sequence: 5′GGGAGGACGAUGUUACUAGGCGGAUUGUUUCGAUUCUUUGCCUUGUCCCUAGUGCAAGAAGACUCGCAAGA3′
Sequence length: 71
GC content: 0.4929577464788732
Affinity: Not reported
Pool type: 5′-GGGAGGACGATGTTA-N40-AAGAAGACTCGCAAGA-3′
Pool random region: 40
Binding buffer/conditions: PBS with 1 mM MgCl2 and 10 mM DTT
Divalent salt: MgCl
Buffer type: PBS/phosphate buffers
pH: 7.4
Molecular weight of target: Not reported
Post-SELEX modifications: Not applicable
Application as quoted in the referenced paper: Therapeutic and Diagnostic: "Human tumor necrosis factor α (hTNFα), a pleiotropic cytokine with activities ranging from host defense mechanisms in infection and injury to severe toxicity in septic shock or other related diseases, is a promising target for drug screening. Oligonucleotide aptamers described here are potential therapeutics and diagnostics for hTNFα-related diseases."
Reference (2004, Genomics Proteomics Bioinformatics ): Yan, X., Gao, X., & Zhang, Z. (2004). Isolation and characterization of 2'-amino-modified RNA aptamers for human TNFalpha. Genomics, proteomics & bioinformatics, 2(1), 32–42. https://doi.org/10.1016/s1672-0229(04)02005-4
Aptamer: 4.4.1
Target: Immunoglobulin E (IgE), Human
Type of nucleic acid: ssDNA
Sequence: 5'AGCAGCACAGAGGTCAGATGTGCGGTTCACATAAAACTAACTGTGCCCCCATTCCTCATGCCTATGCGTGCTACCGTGAA3'
Sequence length: 80
GC content: 0.5125
Affinity: Not reported
Pool type: 5′-AGCAGCACAGAGGTCAGATG-N40-CCTATGCGTGCTACCGTGAA-3′
Pool random region: 40
Binding buffer/conditions: 10 mM Tris, 50 mM NaCl, and 1 mM EDTA at pH 7.5
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: " Aptamers with high affinity for IgE were selected using capillary electrophoresis to demonstrate the compatibility of this technique with SELEX. The high selectivity and efficiency of CE gave rise to a very high rate of enrichment, allowing high-affinity, high-selectivity aptamers to be obtained in only four rounds of selection."
Reference (2004, Anal Chem ): Mendonsa, S. D., & Bowser, M. T. (2004). In vitro selection of high-affinity DNA ligands for human IgE using capillary electrophoresis. Analytical chemistry, 76(18), 5387–5392. https://doi.org/10.1021/ac049857v
Aptamer: 4.4.7
Target: Immunoglobulin E (IgE), Human
Type of nucleic acid: ssDNA
Sequence: 5′AGCAGCACAGAGGTCAGATGTATCAGCATTGTAAAATTGGTACAATCTGTTTGGTTTCACCTATGCGTGCTACCGTGAA3′
Sequence length: 79
GC content: 0.430379746835443
Affinity: Not reported
Pool type: 5′-AGCAGCACAGAGGTCAGATG-N40-CCTATGCGTGCTACCGTGAA-3′
Pool random region: 40
Binding buffer/conditions: 10 mM Tris, 50 mM NaCl, and 1 mM EDTA at pH 7.5
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: " Aptamers with high affinity for IgE were selected using capillary electrophoresis to demonstrate the compatibility of this technique with SELEX. The high selectivity and efficiency of CE gave rise to a very high rate of enrichment, allowing high-affinity, high-selectivity aptamers to be obtained in only four rounds of selection."
Reference (2004, Anal Chem ): Mendonsa, S. D., & Bowser, M. T. (2004). In vitro selection of high-affinity DNA ligands for human IgE using capillary electrophoresis. Analytical chemistry, 76(18), 5387–5392. https://doi.org/10.1021/ac049857v
Aptamer: 4.4.14
Target: Immunoglobulin E (IgE), Human
Type of nucleic acid: ssDNA
Sequence: 5′AGCAGCACAGAGGTCAGATGTAGGATTTTTCTCAGACCGATACGCGTCGCTGTGCCTAGTCCTATGCGTGCTACCGTGAA3′
Sequence length: 80
GC content: 0.525
Affinity: Not reported
Pool type: 5′-AGCAGCACAGAGGTCAGATG-N40-CCTATGCGTGCTACCGTGAA-3′
Pool random region: 40
Binding buffer/conditions: 10 mM Tris, 50 mM NaCl, and 1 mM EDTA at pH 7.5
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: " Aptamers with high affinity for IgE were selected using capillary electrophoresis to demonstrate the compatibility of this technique with SELEX. The high selectivity and efficiency of CE gave rise to a very high rate of enrichment, allowing high-affinity, high-selectivity aptamers to be obtained in only four rounds of selection."
Reference (2004, Anal Chem ): Mendonsa, S. D., & Bowser, M. T. (2004). In vitro selection of high-affinity DNA ligands for human IgE using capillary electrophoresis. Analytical chemistry, 76(18), 5387–5392. https://doi.org/10.1021/ac049857v
Aptamer: 4.4.26
Target: Immunoglobulin E (IgE), Human
Type of nucleic acid: ssDNA
Sequence: 5′AGCAGCACAGAGGTCAGATGTCAAATATGTAATGTAGGTCCGTTTCGGGTGGGCCATGGGCCTATGCGTGCTACCGTGAA3′
Sequence length: 80
GC content: 0.525
Affinity: Not reported
Pool type: 5′-AGCAGCACAGAGGTCAGATG-N40-CCTATGCGTGCTACCGTGAA-3′
Pool random region: 40
Binding buffer/conditions: 10 mM Tris, 50 mM NaCl, and 1 mM EDTA at pH 7.5
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: " Aptamers with high affinity for IgE were selected using capillary electrophoresis to demonstrate the compatibility of this technique with SELEX. The high selectivity and efficiency of CE gave rise to a very high rate of enrichment, allowing high-affinity, high-selectivity aptamers to be obtained in only four rounds of selection."
Reference (2004, Anal Chem ): Mendonsa, S. D., & Bowser, M. T. (2004). In vitro selection of high-affinity DNA ligands for human IgE using capillary electrophoresis. Analytical chemistry, 76(18), 5387–5392. https://doi.org/10.1021/ac049857v
Aptamer: Apt-50
Target: Liver X receptors alpha (LXRalpha, LXRα)
Type of nucleic acid: ssDNA
Sequence: 5′ATGACCATGACCCTCCACACACCCTACGCGTGTCAGACTGTGGCAGGGAAAC3′
Sequence length: 52
GC content: 0.5769230769230769
Affinity: Kd: 19 pM
Pool type: 5′-ATGACCATGACCCTCCACAC-N12-TCAGACTGTGGCAGGGAAAC-3′
Pool random region: 12
Binding buffer/conditions: 20 mM Tris, 5 mM MgCl2, and 150 mM NaCl at pH 7.5
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: " Selection and use of small ssDNAs as alternative binders for HDL proteins. An essential function of HDL is linked with reverse cholesterol transport (RCT). Two sterol-responsive transcription factors, LXRa and LXRb, are directly involved in RCT. Crossreactivity studies show that the aptamer sequences, analyzed in this paper, would be more suitable as binders for LXRb"
Reference (2005, Biochem Biophys Res Commun ): Surugiu-Wärnmark, I., Wärnmark, A., Toresson, G., Gustafsson, J. A., & Bülow, L. (2005). Selection of DNA aptamers against rat liver X receptors. Biochemical and biophysical research communications, 332(2), 512–517. https://doi.org/10.1016/j.bbrc.2005.04.147