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
63,CD8a,protein,P01732,A8,,5.59 nM,-8.253,intrinsic,Kd,Gold,v4,extraction_verified,pending_supp_oa,,,BLI,298.15,,binding buffer with 0.01% Tween 20,,DNA,,31209354,10.1038/s41551-019-0411-6,"the A1, A3 and A8 aptamers bound the protein with binding affinities ( K D values) of 20.1 ± 0.2,  14.7 ± 0.1  and  5.59 ± 0.11  nM, respectively",step2c_literal_v3
87,transferrin receptor 1,protein,P02786,JBA8.26,,6.87 nM,-8.163,intrinsic,Kd,Gold,v4,extraction_verified,pending_supp_oa,,,BLI,,,,,DNA,,35875870,10.1021/jacs.2c05349,"Using BLI, JBA8.26 was found to bind immobilized TfR1 with a K D of 6.87 ± 0.04 nM",step2c_literal_v3
92,Okadaic Acid,protein,O95232,OA-LC2-TF,,8.735 nM,-8.059,intrinsic,Kd,Gold,v4,extraction_verified,pending_manual_supp,,,BLI,,7.5,"50 mM Tris, 150 mM NaCl, 2 mM MgCl2, and 0.02% Tween-20 (pH 7.5)",2.0,DNA,terminal fixation with GC-rich sequences,36322695,10.1021/acs.analchem.2c02653,The terminal-fixed OA-LC2 (OA-LC2-TF) exhibited a K d of 8.735 ± 0.606 nM,step2c_literal_v3
101,thrombin,protein,P00734,Uyne A - AUyne,,12.16 nM,-7.915,intrinsic,Kd,Gold,v4,extraction_verified,pending_manual_supp,,,BLI,,,"buffer used for the bead-based selection, which contains Tween-20",,DNA,5-ethynyl-2′-deoxyuridine (Uyne); Biotin (5' end),37531184,10.1021/acschembio.3c00183,U yne A - AUyne | 12.16 ± 0.02,step2c_literal_v3
100,thrombin,protein,P00734,Uyne A - Uyne Uyne,,13.96 nM,-7.855,intrinsic,Kd,Gold,v4,extraction_verified,pending_manual_supp,,,BLI,,,"buffer used for the bead-based selection, which contains Tween-20",,DNA,5-ethynyl-2′-deoxyuridine (Uyne); Biotin (5' end),37531184,10.1021/acschembio.3c00183,U yne A - U yne U yne | 13.96 ± 0.03,step2c_literal_v3
62,CD8a,protein,P01732,A3,,14.7 nM,-7.833,intrinsic,Kd,Gold,v4,extraction_verified,pending_supp_oa,,,BLI,298.15,,binding buffer with 0.01% Tween 20,,DNA,,31209354,10.1038/s41551-019-0411-6,"the A1, A3 and A8 aptamers bound the protein with binding affinities ( K D values) of 20.1 ± 0.2,  14.7 ± 0.1  and  5.59 ± 0.11  nM, respectively",step2c_literal_v3
95,Dinophysistoxin,protein,,DTX-SL1-TF,,15.45 nM,-7.811,intrinsic,Kd,Gold,v4,extraction_verified,pending_manual_supp,,,BLI,,7.5,"50 mM Tris, 150 mM NaCl, 2 mM MgCl2, and 0.02% Tween-20 (pH 7.5)",2.0,DNA,terminal fixation,36322695,10.1021/acs.analchem.2c02653,DTX-SL1-TF showed a K d of 15.45 ± 1.92 nM,step2c_literal_v3
61,CD8a,protein,P01732,A1,,20.1 nM,-7.697,intrinsic,Kd,Gold,v4,extraction_verified,pending_supp_oa,,,BLI,298.15,,binding buffer with 0.01% Tween 20,,DNA,,31209354,10.1038/s41551-019-0411-6,"the A1, A3 and A8 aptamers bound the protein with binding affinities ( K D values) of 20.1 ± 0.2,  14.7 ± 0.1  and  5.59 ± 0.11  nM, respectively",step2c_literal_v3
94,Dinophysistoxin,protein,,DTX-SL1,,21.75 nM,-7.663,intrinsic,Kd,Gold,v4,extraction_verified,pending_manual_supp,,,BLI,,7.5,"50 mM Tris, 150 mM NaCl, 2 mM MgCl2, and 0.02% Tween-20 (pH 7.5)",2.0,DNA,,36322695,10.1021/acs.analchem.2c02653,DTX-SL1 showed the lowest K d at 21.75 ± 1.42 nM,step2c_literal_v3
128,CD117,protein,P10721,Apta02,,21.8 nM,-7.662,intrinsic,Kd,Gold,v4,extraction_verified,pending_supp_oa,,,BLI,298.15,,,,DNA,,40487293,10.1002/adfm.202425394,"Apta02 and Apta04 exhibited K D 's of 21.8 nm and 1.10 µ m, respectively ( Figure 2 a,b).",step2c_literal_v3
86,transferrin receptor 1,protein,P02786,tJBA8.1,,25.11 nM,-7.6,intrinsic,Kd,Gold,v4,extraction_verified,pending_supp_oa,,,BLI,,,,,DNA,biotinylated,35875870,10.1021/jacs.2c05349,tJBA8.1 bound the TfR1 protein with a K D value of 25.11 ± 0.19 nM,step2c_literal_v3
253,rmCD3 d ε,protein,,CD3_Apt1 dimer,CCCGATTGATTCGCAATGTGCGTCCCCTCGTGCC,25.2 nM,-7.599,non_intrinsic,Kd,Gold,v4,extraction_verified,verified_in_text_or_SI,backfill_text_verified,,BLI,298.15,,PBS +/+ buffer,,2'F-RNA,dimerized via ssDNA scaffold,38745854,10.1016/j.omtn.2024.102198,The affinity of the dimeric aptamer was determined by OCTET and was 25.2 nM for Apt1 dimer,step2c_literal_v3
98,thrombin,protein,P00734,HD22 (TA-TT),AGTCCGTGGTAGGGCAGGTTGGGGTGACTGTAAACGCTCGCTTCGATCTAGTCCGTGGGGGCAGGGGGGTGACTAGCAGATATGCATCCGTAGC,27.8 nM,-7.556,intrinsic,Kd,Gold,v4,extraction_verified,verified_in_text_or_SI,original,,BLI,,,"buffer used for the bead-based selection, which contains Tween-20",,DNA,Biotin (5' end),37531184,10.1021/acschembio.3c00183,TA - TT | 27.80 ± 0.09,step2c_literal_v3
99,thrombin,protein,P00734,TA-AT,,38.7 nM,-7.412,intrinsic,Kd,Gold,v4,extraction_verified,pending_manual_supp,,,BLI,,,"buffer used for the bead-based selection, which contains Tween-20",,DNA,Biotin (5' end),37531184,10.1021/acschembio.3c00183,TA - AT | 38.7 ± 0.5,step2c_literal_v3
91,Okadaic Acid,protein,O95232,OA-LC2,,91.13 nM,-7.04,intrinsic,Kd,Gold,v4,extraction_verified,pending_manual_supp,,,BLI,,7.5,"50 mM Tris, 150 mM NaCl, 2 mM MgCl2, and 0.02% Tween-20 (pH 7.5)",2.0,DNA,,36322695,10.1021/acs.analchem.2c02653,OA-LC2 exhibited K d of 91.13 ± 4.64 nM,step2c_literal_v3
89,Okadaic Acid,protein,O95232,OA-SL2,,103.4 nM,-6.985,intrinsic,Kd,Gold,v4,extraction_verified,pending_manual_supp,,,BLI,,7.5,"50 mM Tris, 150 mM NaCl, 2 mM MgCl2, and 0.02% Tween-20 (pH 7.5)",2.0,DNA,,36322695,10.1021/acs.analchem.2c02653,"from OA-SL1 to OASL2, K d was lowered from 340.5 ± 14.5 to 103.4 ± 7.0 nM",step2c_literal_v3
96,Phosphatidylserine,protein,Q9UG56,PS-LC3-TF,,166.2 nM,-6.779,intrinsic,Kd,Gold,v4,extraction_verified,pending_manual_supp,,,BLI,,7.6,150 mM NaCl and 50 mM K2HPO4 (pH 7.6),,DNA,terminal fixation,36322695,10.1021/acs.analchem.2c02653,The terminal-fixed PS-LC3-TF exhibited an even lower K d at 166.2 ± 10.7 nM,step2c_literal_v3
254,rmCD3 d ε,protein,,CD3_Apt12 dimer,TCCCCTGTCGATATCCACCGTCTGGCCCGCATTGA,218.0 nM,-6.662,non_intrinsic,Kd,Gold,v4,extraction_verified,verified_in_text_or_SI,backfill_text_verified,,BLI,298.15,,PBS +/+ buffer,,2'F-RNA,dimerized via ssDNA scaffold,38745854,10.1016/j.omtn.2024.102198,218 nM for Apt12 dimer,step2c_literal_v3
90,Okadaic Acid,protein,O95232,OA-SL3,,234.4 nM,-6.63,intrinsic,Kd,Gold,v4,extraction_verified,pending_manual_supp,,,BLI,,7.5,"50 mM Tris, 150 mM NaCl, 2 mM MgCl2, and 0.02% Tween-20 (pH 7.5)",2.0,DNA,,36322695,10.1021/acs.analchem.2c02653,"When OA-SL1 was tripled to get the chimera OA-SL3, K d rose to 234.4 ± 15.6 nM",step2c_literal_v3
93,Dinophysistoxin,protein,,anti-DTX parent aptamer,,778.1 nM,-6.109,intrinsic,Kd,Gold,v4,extraction_verified,pending_manual_supp,,,BLI,,7.5,"50 mM Tris, 150 mM NaCl, 2 mM MgCl2, and 0.02% Tween-20 (pH 7.5)",2.0,DNA,,36322695,10.1021/acs.analchem.2c02653,antiDTX parent aptamer ( K d = 778.1 ± 73.5 nM),step2c_literal_v3
129,CD117,protein,P10721,Apta04,,1100.0 nM,-5.959,intrinsic,Kd,Gold,v4,extraction_verified,pending_supp_oa,,,BLI,298.15,,,,DNA,,40487293,10.1002/adfm.202425394,"Apta02 and Apta04 exhibited K D 's of 21.8 nm and 1.10 µ m, respectively ( Figure 2 a,b).",step2c_literal_v3
131,CD123,protein,O75794,Apta25,,1.16 µM,-5.936,intrinsic,Kd,Gold,v4,extraction_verified,pending_supp_oa,,,BLI,298.15,,,,DNA,,40487293,10.1002/adfm.202425394,"BLI binding assays of both aptamers demonstrated binding to human recombinant CD123 with K D s of 1.16 µ m for ZW25 and 15.6 µ m for CY30 (Figure S2, Supporting Information).",step2c_literal_v3
88,Okadaic Acid,protein,O95232,anti-OA parent aptamer,,1402.0 nM,-5.853,intrinsic,Kd,Gold,v4,extraction_verified,pending_manual_supp,,,BLI,,7.5,"50 mM Tris, 150 mM NaCl, 2 mM MgCl2, and 0.02% Tween-20 (pH 7.5)",2.0,DNA,,36322695,10.1021/acs.analchem.2c02653,"anti-OA aptamer with high affinity from its parent aptamer ( K d = 1402 ± 58 nM, Figure 1a)",step2c_literal_v3
130,CD123,protein,O75794,Apta30,,15.6 µM,-4.807,intrinsic,Kd,Gold,v4,extraction_verified,pending_supp_oa,,,BLI,298.15,,,,DNA,,40487293,10.1002/adfm.202425394,"BLI binding assays of both aptamers demonstrated binding to human recombinant CD123 with K D s of 1.16 µ m for ZW25 and 15.6 µ m for CY30 (Figure S2, Supporting Information).",step2c_literal_v3