id,target_name_canonical,target_type,target_uniprot,aptamer_name,aptamer_seq,kd_reported,kd_log10_molar,measurement_class,binding_constant_type,tier,source_origin,verification_level,sequence_status,seq_source,pi_provenance_flag,assay_method,assay_temperature_k,assay_ph,assay_buffer,assay_cations,aptamer_chemistry,aptamer_modifications,source_pmid,doi,verbatim_quote,source_db
135,SCAF4,protein,O95104,PTf-SRiApt,TTAAAGGGGTGGGGAGTCAT,0.073 µM,-7.137,intrinsic,Kd,Gold,v4,extraction_verified,verified_in_text_or_SI,original,,fluorescence,,6.5,"30 mM MES buffer pH 6.5, 25 mm NaCl, 2 mm β-ME, 1 mm CHAPS, and 0.002 mg mL -1 BSA",,DNA,phosphorothioate,40574704,10.1002/advs.202500433,0.073 ± 0.003 µ m for PTf -SRiApt,step2c_literal_v3
52,hemagglutinin (HA) protein of H1N1 influenza virus (A/Puerto Rico/8/1934),protein,,aptamer 1,GGGAGCTCAGAATAAACGCTCAAGGCACGGCATGTGTGGTATGTGGTGCCTGTACTCGTTCGACATGAGGCCCGGATC,78.0 nM,-7.108,intrinsic,Kd,Gold,v4,extraction_verified,verified_in_text_or_SI,original,,fluorescence,310.15,7.35,"binding buffer (20 mM HEPES buffer pH 7.35, 120 mM NaCl, 1 mM MgCl2, 1 mM CaCl2, and 5 mM KCl)",1.0,DNA,,26904922,10.1089/nat.2015.0564,"As it showed a higher binding affinity for HA protein (Kd = 78 -1nM), aptamer 1 was tested",step2c_literal_v3
102,CD9,protein,P21926,CD9-26,ATAGTCCCTTGGCGTGCTTCACAACCTTGAACTTGACGCAGGATCGTTCAGTGCGCACTAGAGCAGGTACGGTGTCA,101.96 nM,-6.992,intrinsic,Kd,Gold,v4,extraction_verified,verified_in_text_or_SI,original,,fluorescence,277.15,,1 × SELEX buffer,,DNA,,37585601,10.1021/acssensors.3c00879,CD9-26 | 5 ′ -ATA GTC CCT TGG CGT GCT TCA CAA CCT TGA ACT TGA CGC AGG ATC GTT CAG TGC GCA CTA GAG CAG GTA CGG TGT CA-3 ′ | - 8.92,step2c_literal_v3
134,SCAF4,protein,O95104,PT1/2-SRiApt,TTAAAGGGGTGGGGAGTCAT,0.121 µM,-6.917,intrinsic,Kd,Gold,v4,extraction_verified,verified_in_text_or_SI,original,,fluorescence,,6.5,"30 mM MES buffer pH 6.5, 25 mm NaCl, 2 mm β-ME, 1 mm CHAPS, and 0.002 mg mL -1 BSA",,DNA,phosphorothioate,40574704,10.1002/advs.202500433,0.121 ± 0.054 µ m for PT1/2 -SRiApt,step2c_literal_v3
133,SCAF4,protein,O95104,PT1/3-SRiApt,TTAAAGGGGTGGGGAGTCAT,0.223 µM,-6.652,intrinsic,Kd,Gold,v4,extraction_verified,verified_in_text_or_SI,original,,fluorescence,,6.5,"30 mM MES buffer pH 6.5, 25 mm NaCl, 2 mm β-ME, 1 mm CHAPS, and 0.002 mg mL -1 BSA",,DNA,phosphorothioate,40574704,10.1002/advs.202500433,0.223 ± 0.030 µ m for PT 1/3 -SRiApt,step2c_literal_v3
103,CD9,protein,P21926,CD9-28,ATAGTCCCTTGGCGTGCTTCACAACCTTGAACTTGACGCAGGATCGTTCAGGGCGCACTAGAGCAGGTACGGTGTCA,289.67 nM,-6.538,intrinsic,Kd,Gold,v4,extraction_verified,verified_in_text_or_SI,original,,fluorescence,277.15,,1 × SELEX buffer,,DNA,,37585601,10.1021/acssensors.3c00879,CD9-28 | 5 ′ -ATA GTC CCT TGG CGT GCT TCA CAA CCT TGA ACT TGA CGC AGG ATC GTT CAG GGC GCA CTA GAG CAG GTA CGG TGT CA-3 ′ | - 8.80,step2c_literal_v3
132,SCAF4,protein,O95104,SRiApt,TTAAAGGGGTGGGGAGTCAT,0.469 µM,-6.329,intrinsic,Kd,Gold,v4,extraction_verified,verified_in_text_or_SI,original,,fluorescence,,6.5,"30 mM MES buffer pH 6.5, 25 mm NaCl, 2 mm β-ME, 1 mm CHAPS, and 0.002 mg mL -1 BSA",,DNA,,40574704,10.1002/advs.202500433,The binding affinities (K D ) were determined to be 0.469 ± 0.010 µ m for unmodified SRiApt,step2c_literal_v3
246,CD9,protein,P21926,CD9-08,TGACACCGTACCTGCTCTAGTGCGCACTGAACGATCCTGCGTCAAGTTCAAGGTTGTGAAGCACGCCAAGGGACTAT,494.37 nM,-6.306,non_intrinsic,Kd,Gold,v4,extraction_verified,verified_in_text_or_SI,original,,fluorescence,277.15,,1 × SELEX buffer,,DNA,,37585601,10.1021/acssensors.3c00879,CD9-08 | 5 ′ -TGA CAC CGT ACC TGC TCT AGT GCG CAC TGA ACG ATC CTG CGT CAA GTT CAA GGT TGT GAA GCA CGC CAA GGG ACT AT-3 ′ | - 11.71,step2c_literal_v3
122,hemin,protein,Q9NP58,Sequence D,GGTTGGTGTGGTTGG,2.9 μM,-5.538,intrinsic,Kd,Gold,v4,extraction_verified,verified_in_text_or_SI,original,,fluorescence,,7.4,"10 mM K-phosphate, pH 7.4, 0.1 M KCl, and 1% DMSO",,DNA,"phosphorothioate (Sp, stereopure)",40368877,10.1021/acs.molpharmaceut.5c00117,"Fitting to a one-site specific binding model using GraphPad Prism software yields the dissociation constant of 8.3 and 2.9 μ M for sequences C and D, respectively.",step2c_literal_v3
123,hemin,protein,Q9NP58,Sequence C,GGTTGGTGTGGTTGG,8.3 μM,-5.081,intrinsic,Kd,Gold,v4,extraction_verified,verified_in_text_or_SI,original,,fluorescence,,7.4,"10 mM K-phosphate, pH 7.4, 0.1 M KCl, and 1% DMSO",,DNA,"phosphorothioate (Rp, stereopure)",40368877,10.1021/acs.molpharmaceut.5c00117,"Fitting to a one-site specific binding model using GraphPad Prism software yields the dissociation constant of 8.3 and 2.9 μ M for sequences C and D, respectively.",step2c_literal_v3