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
247,Human thrombin,protein,P00734,Lin08-08,,0.4 nM,-9.398,non_intrinsic,Kd,Gold,v4,extraction_verified,pending_supp_oa,,KEEP_seq_in_figure,SPR,,7.4,"PBS [pH 7.4], 0.05 [v/v%] surfactant Tween 20",,DNA,,37621412,10.1016/j.omtn.2023.07.038,Lin(08-08) | 1.63 10^6 | 6.94 10^-4 | 0.4,step2c_literal_v3
249,Human thrombin,protein,P00734,Pse08-08,,0.4 nM,-9.398,non_intrinsic,Kd,Gold,v4,extraction_verified,pending_supp_oa,,KEEP_seq_in_figure,SPR,,7.4,"PBS [pH 7.4], 0.05 [v/v%] surfactant Tween 20",,DNA,,37621412,10.1016/j.omtn.2023.07.038,Pse(08-08) | 1.19 10^6 | 5.10 10^-4 | 0.4,step2c_literal_v3
724,Heparin-binding protein,protein,P21246,Apt-13,,1.04 nM,-8.983,intrinsic,Kd,Gold,elsevier,extraction_verified,pending_supp_oa,,,,,,text,,,,38675537,10.3390/molecules29081717,"The KD values of the three aptamers were 3.42, 1.44, and 1.04 nM, respectively",elsevier_step2c
328,ATP,protein,P00846,Huizenga-Szostak ATP aptamer,,1.3e-09 M,-8.886,intrinsic,Kd,Gold,v4,multi_agent_verified,pending_supp_oa,,,fluorescence,,,,,DNA,,25170558,10.1021/bc500286r,binding a ffi nity can be tuned over 4 orders of magnitude (1.3 nM -203 μ M),step2c_acs_v1
723,Heparin-binding protein,protein,P21246,Apt-02,,1.44 nM,-8.842,intrinsic,Kd,Gold,elsevier,extraction_verified,pending_supp_oa,,,,,,text,,,,38675537,10.3390/molecules29081717,"The KD values of the three aptamers were 3.42, 1.44, and 1.04 nM, respectively",elsevier_step2c
202,CD8a,protein,P01732,A3,,1.9 nM,-8.721,non_intrinsic,Kd,Gold,v4,extraction_verified,pending_supp_oa,,,flow_cytometry,,,,,DNA,,31209354,10.1038/s41551-019-0411-6,"the A1, A3 and A8 aptamers have apparent K D values of 18.3 ± 4.6, 1.9 ± 0.8 and 2.4 ± 0.9  nM, respectively",step2c_literal_v3
203,CD8a,protein,P01732,A8,,2.4 nM,-8.62,non_intrinsic,Kd,Gold,v4,extraction_verified,pending_supp_oa,,,flow_cytometry,,,,,DNA,,31209354,10.1038/s41551-019-0411-6,"the A1, A3 and A8 aptamers have apparent K D values of 18.3 ± 4.6, 1.9 ± 0.8 and 2.4 ± 0.9  nM, respectively",step2c_literal_v3
226,transferrin receptor 1,protein,P02786,JBA8.26,,3.3 nM,-8.481,non_intrinsic,Kd,Gold,v4,extraction_verified,pending_supp_oa,,,flow_cytometry,,,,,DNA,,35875870,10.1021/jacs.2c05349,JBA8.26 bound TfR1 hi H9 T-lymphoma cells with an apparent K D of 3.3 ± 0.6 nM,step2c_literal_v3
250,Mouse thrombin,protein,,Pse08-08,,4.2 nM,-8.377,non_intrinsic,Kd,Gold,v4,extraction_verified,pending_supp_oa,,KEEP_seq_in_figure,SPR,,7.4,"PBS [pH 7.4], 0.05 [v/v%] surfactant Tween 20",,DNA,,37621412,10.1016/j.omtn.2023.07.038,Pse(08-08) | 7.35 10^5 | 3.06 10^-3 | 4.2,step2c_literal_v3
224,transferrin receptor 1,protein,P02786,JBA8.1,,5.5 nM,-8.26,non_intrinsic,Kd,Gold,v4,extraction_verified,pending_supp_oa,,,flow_cytometry,,,,,DNA,fluorescein-labeled,35875870,10.1021/jacs.2c05349,JBA8.1 has an apparent binding affinity (K D ) of 5.5 ± 1.2 nM,step2c_literal_v3
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
248,Mouse thrombin,protein,,Lin08-08,,6.7 nM,-8.174,non_intrinsic,Kd,Gold,v4,extraction_verified,pending_supp_oa,,KEEP_seq_in_figure,SPR,,7.4,"PBS [pH 7.4], 0.05 [v/v%] surfactant Tween 20",,DNA,,37621412,10.1016/j.omtn.2023.07.038,Lin(08-08) | 6.41 10^5 | 4.30 10^-3 | 6.7,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
689,EN2,protein,P19622,EBA,,8.26 nM,-8.083,intrinsic,Kd,Gold,elsevier,extraction_verified,pending_supp_oa,,,,,,text,,,,35798816,10.1038/s41598-022-15556-1,EBA had K d =  8.26 nM (R 2 =  0.971),elsevier_step2c
225,transferrin receptor 1,protein,P02786,tJBA8.1,,10.9 nM,-7.963,non_intrinsic,Kd,Gold,v4,extraction_verified,pending_supp_oa,,,flow_cytometry,,,,,DNA,,35875870,10.1021/jacs.2c05349,versus that of 10.9 ± 2.4 nM for tJBA8.1,step2c_literal_v3
697,β-conglutin,protein,,unmodified β-CBA II aptamer,,11.1 nM,-7.955,intrinsic,Kd,Gold,elsevier,extraction_verified,pending_supp_oa,,,,,,text,,,,36354481,10.3390/bios12110972,"with a similar KD of 11.1 nM and 18.5 nM obtained for the unmodified and modified aptamer, respectively.",elsevier_step2c
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
201,CD8a,protein,P01732,A1,,18.3 nM,-7.738,non_intrinsic,Kd,Gold,v4,extraction_verified,pending_supp_oa,,,flow_cytometry,,,,,DNA,,31209354,10.1038/s41551-019-0411-6,"the A1, A3 and A8 aptamers have apparent K D values of 18.3 ± 4.6, 1.9 ± 0.8 and 2.4 ± 0.9  nM, respectively",step2c_literal_v3
698,β-conglutin,protein,,biotinylated dUTPs aptamer,,18.5 nM,-7.733,intrinsic,Kd,Gold,elsevier,extraction_verified,pending_supp_oa,,,,,,text,,,,36354481,10.3390/bios12110972,"with a similar KD of 11.1 nM and 18.5 nM obtained for the unmodified and modified aptamer, respectively.",elsevier_step2c
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
677,saxitoxin,protein,O60939,45e,,21.2 nM,-7.674,intrinsic,Kd,Gold,elsevier,extraction_verified,pending_supp_oa,,,,,,text,,,,35324725,10.3390/toxins14030228,aptamer 45e with a K d value of 21.2 nM,elsevier_step2c
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
302,prostate-cancer-derived small extracellular vesicles,cell/EV,Q99523,seq25,,24.02 nM,-7.619,non_intrinsic,Kd,Gold,v4,extraction_verified,pending_supp_oa,,,SPR,,,PBST buffer,,DNA,5'-FAM,41646885,10.1016/j.omtn.2026.102836,"The affinity of seq25 for positive selection was significantly higher than that of the other aptamers, with a KD of 24.02 nM",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
227,transferrin receptor 1,protein,P02786,tJBA8.1,,25.6 nM,-7.592,non_intrinsic,Kd,Gold,v4,extraction_verified,pending_supp_oa,,,flow_cytometry,,,,,DNA,,35875870,10.1021/jacs.2c05349,compared to tJBA8.1's apparent K D of 25.6 ± 13.0 nM for these cells,step2c_literal_v3
716,Enrofloxacin,protein,P05177,ENR-Apt 6,,35.08 nM,-7.455,intrinsic,Kd,Gold,elsevier,extraction_verified,pending_supp_oa,,,,,,text,,,,38540931,10.3390/foods13060941,"Figure 4A shows the non-linear fitting curve of ENR-Apt 6, with a Kd value of 35.08 nM.",elsevier_step2c
222,CD20,protein,P11836,WB1-CD20,,73.0 nM,-7.137,non_intrinsic,Kd,Gold,v4,extraction_verified,pending_supp_oa,,,flow_cytometry,298.15,,Cell Suspension Buffer (CSB),,DNA,5'-FAM,35829681,10.1021/acs.biochem.2c00105,"The apparent affinities of WB1-CD20 and WB2-CD20 were calculated as 73 nM and 163 nM at 25°C, respectively",step2c_literal_v3
97,N-acetylneuraminic acid,protein,Q8NFW8,Neu5Ac aptamer,,91.0 nM,-7.041,intrinsic,Kd,Gold,v4,extraction_verified,pending_supp_oa,,,ITC,310.15,7.4,"1× aptamer binding buffer (50 mM Tris-HCl, 5 mM KCl, 100 mM NaCl and 1 mM MgCl2, pH 7.4)",1.0,DNA,,37217750,10.1038/s41587-023-01801-z,"To validate ARPLA, we first determined the binding affinity ( K d ) of the Neu5Ac aptamer by isothermal titration calorimetry (ITC) as 91 nM (Extended Data Fig. 2a,b)",step2c_literal_v3
687,mouse IL-2,protein,,M20,,91.0 nM,-7.041,intrinsic,Kd,Gold,elsevier,extraction_verified,pending_supp_oa,,,,,,text,,,,35756119,10.1016/j.heliyon.2022.e09721,"The results indicated that the af fi nity of the M20 aptamer was greater than the M15, and its predicted Kd was 91 nM",elsevier_step2c
678,saxitoxin,protein,O60939,75a,,136.0 nM,-6.866,intrinsic,Kd,Gold,elsevier,extraction_verified,pending_supp_oa,,,,,,text,,,,35324725,10.3390/toxins14030228,aptamer 75a with a K d value of 136 nM,elsevier_step2c
220,CD19,protein,P15391,WB15-CD19,,153.0 nM,-6.815,non_intrinsic,Kd,Gold,v4,extraction_verified,pending_supp_oa,,,flow_cytometry,298.15,,Cell Suspension Buffer (CSB),,DNA,5'-FAM,35829681,10.1021/acs.biochem.2c00105,"At 25 °C, WB15-CD19 showed an apparent affinity of 153 nM",step2c_literal_v3
223,CD20,protein,P11836,WB2-CD20,,163.0 nM,-6.788,non_intrinsic,Kd,Gold,v4,extraction_verified,pending_supp_oa,,,flow_cytometry,298.15,,Cell Suspension Buffer (CSB),,DNA,5'-FAM,35829681,10.1021/acs.biochem.2c00105,"The apparent affinities of WB1-CD20 and WB2-CD20 were calculated as 73 nM and 163 nM at 25°C, respectively",step2c_literal_v3
221,CD19,protein,P15391,WB17-CD19,,187.0 nM,-6.728,non_intrinsic,Kd,Gold,v4,extraction_verified,pending_supp_oa,,,flow_cytometry,298.15,,Cell Suspension Buffer (CSB),,DNA,5'-FAM,35829681,10.1021/acs.biochem.2c00105,and WB17-CD19 showed an apparent affinity of 187 nM (Figure S12A-B).,step2c_literal_v3
419,cortisol,protein,P08185,CSS.3,,2.4000000000000003e-07 M,-6.62,intrinsic,Kd,Gold,v4,multi_agent_verified,pending_supp_oa,,,,,,,,,,38270529,10.1021/acssensors.3c02004,Our own internal work confirmed that CSS.3 had the best binding affinity in binding buffer with a K D of 240 nM,step2c_acs_v1
673,kanamycin,protein,,Apt 1/Apt 2 (split aptamers),,247.0 nM,-6.607,intrinsic,Kd,Gold,elsevier,extraction_verified,pending_supp_oa,,,,,,text,,,,35316405,10.1007/s00604-022-05235-3,"With the (GlcN)5 added in the binding buffer, the Kd was measured to be 247 nM",elsevier_step2c
672,kanamycin,protein,,Apt 1/Apt 2 (split aptamers),,304.0 nM,-6.517,intrinsic,Kd,Gold,elsevier,extraction_verified,pending_supp_oa,,,,,,text,,,,35316405,10.1007/s00604-022-05235-3,"The split aptamers exhibited high affinity towards the kanamycin, with an Kd of 304 nM.",elsevier_step2c
263,H-6 cells,cell/EV,O14756,Apta25,,0.42 µM,-6.377,non_intrinsic,Kd,Gold,v4,extraction_verified,pending_supp_oa,,,flow_cytometry,310.15,,,,DNA,,40487293,10.1002/adfm.202425394,H-6 cells showed binding with Apta25 ( K D value-0.42 ± 0.093 µ m),step2c_literal_v3
688,mouse IL-2,protein,,M15,,600.0 nM,-6.222,intrinsic,Kd,Gold,elsevier,extraction_verified,pending_supp_oa,,,,,,text,,,,35756119,10.1016/j.heliyon.2022.e09721,"The calculation of the dissociation constant predicted 91 and 600 nM Kd for M20 and M15, respectively",elsevier_step2c
261,K-1 cells,cell/EV,O60814,Apta30,,0.66 µM,-6.18,non_intrinsic,Kd,Gold,v4,extraction_verified,pending_supp_oa,,,flow_cytometry,310.15,,,,DNA,,40487293,10.1002/adfm.202425394,Apta30 ( K D -0.66 ± 0.12 µ m),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
264,H-6 cells,cell/EV,O14756,Apta30,,1.107 µM,-5.956,non_intrinsic,Kd,Gold,v4,extraction_verified,pending_supp_oa,,,flow_cytometry,310.15,,,,DNA,,40487293,10.1002/adfm.202425394,H-6 cells showed binding with ... Apta30 ( K D -1.107 ± 0.208 µ m),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
262,K-1 cells,cell/EV,O60814,Apta25,,1.358 µM,-5.867,non_intrinsic,Kd,Gold,v4,extraction_verified,pending_supp_oa,,,flow_cytometry,310.15,,,,DNA,,40487293,10.1002/adfm.202425394,Apta25 ( K D value-1.358 ± 0.201 µ m),step2c_literal_v3
259,K-1 cells,cell/EV,O60814,Apta02,,1.821 µM,-5.74,non_intrinsic,Kd,Gold,v4,extraction_verified,pending_supp_oa,,,flow_cytometry,310.15,,,,DNA,,40487293,10.1002/adfm.202425394,Apta02 ( K D value-1.821 ± 0.117 µ m),step2c_literal_v3
260,K-1 cells,cell/EV,O60814,Apta04,,1.867 µM,-5.729,non_intrinsic,Kd,Gold,v4,extraction_verified,pending_supp_oa,,,flow_cytometry,310.15,,,,DNA,,40487293,10.1002/adfm.202425394,Apta04 ( K D value-1.867 ± 0.19 µ m),step2c_literal_v3
121,CTNNA1,protein,P35221,EA2,,2.07 µM,-5.684,intrinsic,Kd,Gold,v4,extraction_verified,pending_supp_oa,,,MST,,,,,DNA,biotinylated,40265971,10.1002/advs.202411930,The K d values (2.07 ± 0.60 µ M) obtained from MST assay (Figure 2l) further corroborated the specific binding between CTNNA1 and EA2.,step2c_literal_v3
265,H-9 cells,cell/EV,Q8IVB4,Apta02,,4.93 µM,-5.307,non_intrinsic,Kd,Gold,v4,extraction_verified,pending_supp_oa,,,flow_cytometry,310.15,,,,DNA,,40487293,10.1002/adfm.202425394,H-9 cells showed binding with Apta02 ( K D value-4.93 ± 0.367 µ m),step2c_literal_v3
266,H-9 cells,cell/EV,Q8IVB4,Apta04,,5.402 µM,-5.267,non_intrinsic,Kd,Gold,v4,extraction_verified,pending_supp_oa,,,flow_cytometry,310.15,,,,DNA,,40487293,10.1002/adfm.202425394,H-9 cells showed binding with ... Apta04 ( K D value-5.402 ± 0.795 µ m),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