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
434,Ara h1,protein,P35354,CB-APT1,GTGCTCGGACTCCACTTGCGCTTCATTAACCGGGTTGCTCATTTATTCA,3.63e-08 M,-7.44,avidity_multivalent,Kd,Gold,v4,multi_agent_verified,verified_in_text_or_SI,original,,MST,298.15,7.2,1 × binding buffer,,DNA,,40083221,10.1021/acs.analchem.5c00270,"Among them, CBAPT1 exhibited the strongest binding to Ara h1 with a K d value of 36.3 nM in aqueous solutions.",step2c_acs_v1
435,Ara h1,protein,P35354,CB-APT1,GTGCTCGGACTCCACTTGCGCTTCATTAACCGGGTTGCTCATTTATTCA,4.5000000000000006e-08 M,-7.347,avidity_multivalent,Kd,Gold,v4,multi_agent_verified,verified_in_text_or_SI,original,,MST,298.15,7.2,1 × binding buffer with 80% w/w total peanut proteins,,DNA,,40083221,10.1021/acs.analchem.5c00270,"Notably, a similar binding affinity was observed even in a complex matrix that contained 80% w/w total peanut proteins ( K d = 45.0 nM, Figures 3 and S5).",step2c_acs_v1