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
188,PDGF-BB,protein,P01127,36aApt,,0.036 pM,-13.444,non_intrinsic,Kd,Gold,v4,extraction_verified,pending_manual_supp,,,ELISA,298.0,,,,DNA,,28825469,10.1021/acscombsci.6b00163,36aApt | 0.036 ± 0.012 | - 18.33,step2c_literal_v3
186,PDGF-BB,protein,P01127,38aApt,,0.094 pM,-13.027,non_intrinsic,Kd,Gold,v4,extraction_verified,pending_manual_supp,,,ELISA,298.0,,,,DNA,,28825469,10.1021/acscombsci.6b00163,38aApt | 0.094 ± 0.008 | - 17.76,step2c_literal_v3
208,SW480 cells,cell/EV,Q16520,Apt-nanovesicle,,3.66 pM,-11.437,non_intrinsic,Kd,Gold,v4,extraction_verified,pending_manual_supp,,,,,,,,DNA,cholesterol; multivalent,32049531,10.1021/jacs.9b13782,The dissociation constant ( K d ) value of Apt-nanovesicle against SW480 cells was found to be 3.66 ± 0.34 pM (Figure 2B),step2c_literal_v3
184,PDGF-BB,protein,P01127,FullApt,,5.33 pM,-11.273,non_intrinsic,Kd,Gold,v4,extraction_verified,pending_manual_supp,,,ELISA,298.0,,,,DNA,,28825469,10.1021/acscombsci.6b00163,FullApt | 5.33 ± 2.36 | - 15.37,step2c_literal_v3
185,PDGF-BB,protein,P01127,40Apt,,5.92 pM,-11.228,non_intrinsic,Kd,Gold,v4,extraction_verified,pending_manual_supp,,,ELISA,298.0,,,,DNA,,28825469,10.1021/acscombsci.6b00163,40Apt | 5.92 ± 1.13 | - 15.31,step2c_literal_v3
187,PDGF-BB,protein,P01127,38bApt,,7.03 pM,-11.153,non_intrinsic,Kd,Gold,v4,extraction_verified,pending_manual_supp,,,ELISA,298.0,,,,DNA,,28825469,10.1021/acscombsci.6b00163,38bApt | 7.03 ± 1.28 | - 15.21,step2c_literal_v3
269,thrombin,protein,P00734,HD1-12A-DAB,,13.1 pM,-10.883,non_intrinsic,Kd,Gold,v4,extraction_verified,pending_manual_supp,,,filter_binding,,,selection buffer,,DNA,,41053535,10.1002/advs.202509867,HD1-12A-DAB EXACT inhibitor bound to thrombin and prothrombin with K D s of 13.1 pm,step2c_literal_v3
209,SW480 cells,cell/EV,Q16520,Fixed Apt-nanovesicle,,28.06 pM,-10.552,non_intrinsic,Kd,Gold,v4,extraction_verified,pending_manual_supp,,,,,,,,DNA,cholesterol; crosslinked,32049531,10.1021/jacs.9b13782,the K d value of fi xed Apt-nanovesicles to SW480 cells was increased to 28.06 ± 3.31 pM (Figure 2D),step2c_literal_v3
219,CCRF-CEM cells,cell/EV,Q9NRR3,CDN-sgc8,,0.08 nM,-10.097,non_intrinsic,Kd,Gold,v4,extraction_verified,pending_manual_supp,,,fluorescence,,,"1 × PBS, 5 mM MgCl2",5.0,DNA,biotinylated,35670775,10.1021/acs.analchem.2c01359,Kd=0.08±0.01 nM,step2c_literal_v3
218,CCRF-CEM cells,cell/EV,Q9NRR3,mono-CDN-sgc8,,0.48 nM,-9.319,non_intrinsic,Kd,Gold,v4,extraction_verified,pending_manual_supp,,,fluorescence,,,"1 × PBS, 5 mM MgCl2",5.0,DNA,biotinylated,35670775,10.1021/acs.analchem.2c01359,Kd= 0.48 ± 0.04 nM,step2c_literal_v3
205,thrombin,protein,P00734,TBA29,,0.5 nM,-9.301,non_intrinsic,Kd,Gold,v4,extraction_verified,pending_manual_supp,,,,,,,,DNA,,31614078,10.1021/acs.analchem.9b03368,The 29-nt TBA29 aptamer has a bimodular duplex-antiparallel G4 structure and binds to thrombin with a binding a ffi nity of 0.5 nM. 30,step2c_literal_v3
303,EGFR,protein,P00533,Anti-EGF receptor aptamer,,0.62 nM,-9.208,non_intrinsic,Kd,Gold,v4,extraction_verified,pending_manual_supp,,,,,,,,DNA,3' end sulfhydryl group (-SH),41877526,10.1021/acs.molpharmaceut.5c01966,"Anti-EGF receptor aptamers ( K d : 0.62 nM, DNA aptamers)",step2c_literal_v3
217,CCRF-CEM cells,cell/EV,Q9NRR3,individual sgc8,,0.82 nM,-9.086,non_intrinsic,Kd,Gold,v4,extraction_verified,pending_manual_supp,,,fluorescence,,,"1 × PBS, 5 mM MgCl2",5.0,DNA,biotinylated,35670775,10.1021/acs.analchem.2c01359,Kd=0.82 ± 0.12 nM,step2c_literal_v3
228,CD8,protein,P01732,A3t,,2.0 nM,-8.699,non_intrinsic,Kd,Gold,v4,extraction_verified,pending_manual_supp,,,,,,,,DNA,,36149728,10.1021/acsami.2c11783,"A3t, a CD8 receptor-binding aptamer, which binds CD8-expressing cells with an equilibrium dissociation constant K D of 2 nM.",step2c_literal_v3
232,CD8,protein,P01732,rvCD8apt,,2.0 nM,-8.699,non_intrinsic,Kd,Gold,v4,extraction_verified,pending_manual_supp,,,,,,,,DNA,8 nt toehold,36149728,10.1021/acsami.2c11783,apparent K D = 2 nM for CD8 + cells,step2c_literal_v3
211,K562,protein,Q8WUY8,PAM,,3.2 nM,-8.495,non_intrinsic,Kd,Gold,v4,extraction_verified,pending_manual_supp,,,,,,,,DNA,FAM,32307868,10.1002/anie.202004206,the K d value (3.2 nM) of PAM in binding the K562 cell is one order of magnitude lower than that of the aptamer alone (41 nM).,step2c_literal_v3
267,Thyroid-Stimulating Hormone Receptor (TSHR) 6X His tag,protein,,ZMXLY-2a,,11.5 nM,-7.939,non_intrinsic,Kd,Gold,v4,extraction_verified,pending_manual_supp,,,flow_cytometry,,,phosphate-buffered saline,,DNA,FITC-labeled 5' primer used for synthesis,40588369,10.1021/acs.analchem.5c02024,"As determined by flow cytometry, the K d of ZMXLY-2a was 11.5 ± 9.3 nM (Figure 2G)",step2c_literal_v3
183,human immunoglobulin E,protein,Q96D42,T40-AptIgE-3'-TMR,,15.0 nM,-7.824,non_intrinsic,Kd,Gold,v4,extraction_verified,pending_manual_supp,,,CE-LIF,298.15,7.5,sample bu ff er containing 10 mM Tris-HCl (pH 7.5) and 1 mM MgCl2,1.0,DNA,TMR label at 3'-end; polyT tail (40 T) at 5'-end,28763192,10.1021/acs.analchem.7b02313,The K d of T40-AptIgE-3 ′ -TMR was about 15 nM,step2c_literal_v3
212,M2-like macrophage,protein,Q8IYS5,A2,,22.81 nM,-7.642,non_intrinsic,Kd,Gold,v4,extraction_verified,pending_manual_supp,,,flow_cytometry,277.15,,Wash Buffer (WB) supplemented with 10% FBS and 100 μg/mL tRNA,,DNA,Cy5-label,32589412,10.1021/acs.bioconjchem.0c00247,"apparent dissociation constants ( K d ) of 44.12 ± 8.0 and 22.81 ± 5.6 nM to M0- and M2-like macrophages, respectively",step2c_literal_v3
210,K562,protein,Q8WUY8,aptamer-FAM,,41.0 nM,-7.387,non_intrinsic,Kd,Gold,v4,extraction_verified,pending_manual_supp,,,,,,,,DNA,FAM,32307868,10.1002/anie.202004206,the K d value (3.2 nM) of PAM in binding the K562 cell is one order of magnitude lower than that of the aptamer alone (41 nM).,step2c_literal_v3
257,CD71,protein,P02786,XQ 2d,,42.34 nM,-7.373,non_intrinsic,Kd,Gold,v4,extraction_verified,pending_manual_supp,,,flow_cytometry,,,PBS supplemented with 0.5 mM MgCl2 and 0.05% BSA (BB buffer),0.5,DNA,FAM,40156524,10.1021/acs.analchem.5c00711,"aptamers (HG1-9, K d = 43.23 ± 4.62 nM and XQ-2d, K d = 42.34 ± 5.15 nM))",step2c_literal_v3
258,CD71,protein,P02786,HG1-9,,43.23 nM,-7.364,non_intrinsic,Kd,Gold,v4,extraction_verified,pending_manual_supp,,,flow_cytometry,,,PBS supplemented with 0.5 mM MgCl2 and 0.05% BSA (BB buffer),0.5,DNA,FAM,40156524,10.1021/acs.analchem.5c00711,"aptamers (HG1-9, K d = 43.23 ± 4.62 nM and XQ-2d, K d = 42.34 ± 5.15 nM))",step2c_literal_v3
213,M0-like macrophage,protein,P01854,A2,,44.12 nM,-7.355,non_intrinsic,Kd,Gold,v4,extraction_verified,pending_manual_supp,,,flow_cytometry,277.15,,Wash Buffer (WB) supplemented with 10% FBS and 100 μg/mL tRNA,,DNA,Cy5-label,32589412,10.1021/acs.bioconjchem.0c00247,"apparent dissociation constants ( K d ) of 44.12 ± 8.0 and 22.81 ± 5.6 nM to M0- and M2-like macrophages, respectively",step2c_literal_v3
214,monocyte,protein,P13500,A2,,45.0 nM,-7.347,non_intrinsic,Kd,Gold,v4,extraction_verified,pending_manual_supp,,,flow_cytometry,277.15,,Wash Buffer (WB) supplemented with 10% FBS and 100 μg/mL tRNA,,DNA,Cy5-label,32589412,10.1021/acs.bioconjchem.0c00247,aptamer A2 bound CD14 + cells (monocytes) with high speci fi city ( K d ∼ 45 ± 9.1 nM),step2c_literal_v3
300,CD71,protein,P02786,ATL,,48.17 nM,-7.317,non_intrinsic,Kd,Gold,v4,extraction_verified,pending_manual_supp,,,flow_cytometry,277.15,6.5,binding buffer,,DNA,Cy5-labeled; Cy3-labeled; Triplex motif,41412185,10.1021/acs.nanolett.5c04783,K(pH 6.5) = 48.17 ± 2.70 nM,step2c_literal_v3
182,human immunoglobulin E,protein,Q96D42,AptIgE-3'-TMR,,50.0 nM,-7.301,non_intrinsic,Kd,Gold,v4,extraction_verified,pending_manual_supp,,,CE-LIF,298.15,7.5,sample bu ff er containing 10 mM Tris-HCl (pH 7.5) and 1 mM MgCl2,1.0,DNA,TMR label at 3'-end,28763192,10.1021/acs.analchem.7b02313,The apparent K d of AptIgE-3 ′ -TMR was about 50 nM,step2c_literal_v3
268,Thyroid-Stimulating Hormone Receptor (TSHR),protein,P16473,TSHRly-1c,,54.37 nM,-7.265,non_intrinsic,Kd,Gold,v4,extraction_verified,pending_manual_supp,,,flow_cytometry,,,binding buffer,,DNA,AlexaFluor 647-labeled,40588369,10.1021/acs.analchem.5c02024,"As shown in Figure 4E, the apparent equilibrium dissociation constant ( K d) of TSHRly-1c was determined to be 54.37 ± 8.22 nM.",step2c_literal_v3
207,SW480 cells,cell/EV,Q16520,SYL3C,,142.5 nM,-6.846,non_intrinsic,Kd,Gold,v4,extraction_verified,pending_manual_supp,,,,,,,,DNA,cholesterol,32049531,10.1021/jacs.9b13782,"monovalent SYL3C aptamer ( K d = 142.50 ± 20.55 nM, Figure 2A)",step2c_literal_v3
179,human α-thrombin,protein,P00734,T25-Apt15-3'-TMR,,228.0 nM,-6.642,non_intrinsic,Kd,Gold,v4,extraction_verified,pending_manual_supp,,,CE-LIF,298.15,7.5,sample bu ff er containing 10 mM Tris-HCl (pH 7.5) and 5 mM KCl,,DNA,TMR label at 3'-end; polyT tail (25 T) at 5'-end,28763192,10.1021/acs.analchem.7b02313,"The apparent K d values of T25-Apt15-3 ′ -TMR and 5 ′ -TMR-T25-Apt15 were estimated as 228 nM and 8.8 nM, respectively",step2c_literal_v3
270,prothrombin,protein,P00734,HD1-12A-DAB,,296.0 nM,-6.529,non_intrinsic,Kd,Gold,v4,extraction_verified,pending_manual_supp,,,filter_binding,,,selection buffer,,DNA,,41053535,10.1002/advs.202509867,and prothrombin with K D s of 13.1 pm and 296 nm,step2c_literal_v3
301,CD71,protein,P02786,ATL,,696.7 nM,-6.157,non_intrinsic,Kd,Gold,v4,extraction_verified,pending_manual_supp,,,flow_cytometry,277.15,7.5,binding buffer,,DNA,Cy5-labeled; Cy3-labeled; Triplex motif,41412185,10.1021/acs.nanolett.5c04783,K(pH 7.5)= 696.7 ± 68.03 nM,step2c_literal_v3