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
64,von Willebrand factor,protein,P04275,42-nt DNA aptamer,,2.0 nM,-8.699,intrinsic,Kd,Gold,v4,extraction_verified,pending_manual_figure,,FLAG_cited_data,ELISA,,,PBS with 1% BSA,,DNA,biotinylated,31493779,10.1055/s-0039-1696713,a biotinylated DNA aptamer was able to bind an antibody-captured VWF in a concentration-dependent manner with a dissociation constant ( KD ) of 2.0 nM  0.3.,step2c_literal_v3
109,HNP 1-3,protein,P59666,6J,ACAGCACCACAGACCATACCGACCGGGTGTGCCTGGCGCGGTGGTTGTGGGGCGGCCTGCTGTTTGTCTTCCTGCC,35.0 nM,-7.456,intrinsic,Kd,Gold,v4,extraction_verified,verified_in_text_or_SI,original,,ELISA,,,0.01 M PBS,,DNA,biotin,38591344,10.1021/acssensors.3c02034,Regression analysis (Figure 4a) yielded a K d value of 35 nM,step2c_literal_v3
46,thrombospondin-1,protein,P07996,M55,ATACCAGCTTATTCAATTCCCAAATTGCCACCACTTACAGCATGATAACATACTACATCTTTTCATCAAGATAGTAAGTGCAATCT,0.5 μM,-6.301,intrinsic,Kd,Gold,v4,extraction_verified,verified_in_text_or_SI,original,,ELISA,,,PBS,,DNA,5'-NH2; 5'-8-carbon PEG spacer; 3'-dT,24434496,10.1016/j.bios.2013.12.012,The K D value of the aptamer M55 binding to thrombospondin-1 was determined as 0.5 7 0.2 μ M,step2c_literal_v3