Details of experiments between Q12923 and P03126 Note that the results of all experiments are listed, regardless of the modification states of the fragments.
Experiment series 1 Protein A Protein: PTPN13 Fragment: 1085-1188 Site: PDZ_1 Construct: his6-MBP-TEVsite-PDZ
Protein B Protein: HPV16-E6 Fragment: 149-158 Site: PBM Sequence: SSRTRRETQL Construct: biotin-ttds-SSRTRRETQL
Average holdup BI: 0.06
Normalized holdup BI: 0.06
Immobilized partner concentration (10-6 M): 18
Experiment method: DAPF_holdup
Details of affinity fitting: fluorescein + mCherry internal standards + normalization based on CALIP_holdup data + reverse layout
Number of measurements: 1
Measured pK d : 3.56
Experiment series 2 Protein A Protein: PTPN13 Fragment: 1085-1188 Site: PDZ_1 Construct: his6-MBP-TEVsite-PDZ
Protein B Protein: HPV16-E6 Fragment: 149-158 Site: PBM Sequence: SSRTRRETQL Construct: Biotin-ado-ado-SSRTRRETQL
Average holdup BI: -0.03
Normalized holdup BI: -0.03
Immobilized partner concentration (10-6 M): 18
Experiment method: DAPF_holdup
Details of affinity fitting: fluorescein + mCherry internal standards + normalization based on CALIP_holdup data + reverse layout
Number of measurements: 1
The affinity was below the detection threshold of the assay.
Experimental Details Crude peptide synthesis product. The peptide concentration in the affinity conversion step may differ from reality. Not reported internal standards of holdup layout #6
Experiment series 3 Protein A Protein: PTPN13 Fragment: 1085-1188 Site: PDZ_1 Construct: his6-MBP-TEVsite-PDZ
Protein B Protein: HPV16-E6 Fragment: 149-158 Site: PBM Sequence: SSRTRRETQL Construct: biotin-ttds-SSRTRRETQL
Average holdup BI: -0.01
Normalized holdup BI: -0.01
Immobilized partner concentration (10-6 M): 18
Experiment method: DAPF_holdup
Details of affinity fitting: fluorescein + mCherry internal standards + normalization based on CALIP_holdup data + reverse layout
Number of measurements: 1
The affinity was below the detection threshold of the assay.
Experimental Details not reported internal standards of holdup layout #5
Experiment series 4 Protein A Protein: PTPN13 Fragment: 1085-1188 Site: PDZ_1 Construct: his6-MBP-TEVsite-PDZ
Protein B Protein: HPV16-E6 Fragment: 149-158 Site: PBM Sequence: SSRTRRETQL Construct: biotin-ttds-SSRTRRETQL
Average holdup BI: -0.03
Holdup BI standard deviation: 0.04
Immobilized partner concentration (10-6 M): 15
Experiment method: CALIP_holdup
Details of affinity fitting: BSA and lysozyme internal standards + bacterial cell lysate + normal layout
Number of measurements: 8
The affinity was below the detection threshold of the assay.
Experiment series 5 Protein A Protein: PTPN13 Fragment: 1362-1455 Site: PDZ_2 Construct: his6-MBP-TEVsite-PDZ
Protein B Protein: HPV16-E6 Fragment: 149-158 Site: PBM Sequence: SSRTRRETQL Construct: biotin-ttds-SSRTRRETQL
Average holdup BI: 0.07
Holdup BI standard deviation: 0.05
Immobilized partner concentration (10-6 M): 15
Experiment method: CALIP_holdup
Details of affinity fitting: BSA and lysozyme internal standards + bacterial cell lysate + normal layout
Number of measurements: 7
The affinity was below the detection threshold of the assay.
Experiment series 6 Protein A Protein: PTPN13 Fragment: 1495-1591 Site: PDZ_3 Construct: his6-MBP-TEVsite-PDZ
Protein B Protein: HPV16-E6 Fragment: 149-158 Site: PBM Sequence: SSRTRRETQL Construct: biotin-ttds-SSRTRRETQL
Average holdup BI: 0.03
Holdup BI standard deviation: 0.11
Immobilized partner concentration (10-6 M): 15
Experiment method: CALIP_holdup
Details of affinity fitting: BSA and lysozyme internal standards + bacterial cell lysate + normal layout
Number of measurements: 8
The affinity was below the detection threshold of the assay.
Experiment series 7 Protein A Protein: PTPN13 Fragment: 1779-1873 Site: PDZ_4 Construct: his6-MBP-TEVsite-PDZ
Protein B Protein: HPV16-E6 Fragment: 149-158 Site: PBM Sequence: SSRTRRETQL Construct: biotin-ttds-SSRTRRETQL
Average holdup BI: 0.04
Holdup BI standard deviation: 0.07
Immobilized partner concentration (10-6 M): 15
Experiment method: CALIP_holdup
Details of affinity fitting: BSA and lysozyme internal standards + bacterial cell lysate + normal layout
Number of measurements: 7
The affinity was below the detection threshold of the assay.
Experiment series 8 Protein A Protein: PTPN13 Fragment: 1875-1973 Site: PDZ_5 Construct: his6-MBP-TEVsite-PDZ
Protein B Protein: HPV16-E6 Fragment: 149-158 Site: PBM Sequence: SSRTRRETQL Construct: biotin-ttds-SSRTRRETQL
Average holdup BI: -0.01
Holdup BI standard deviation: 0.05
Immobilized partner concentration (10-6 M): 15
Experiment method: CALIP_holdup
Details of affinity fitting: BSA and lysozyme internal standards + bacterial cell lysate + normal layout
Number of measurements: 8
The affinity was below the detection threshold of the assay.
Experiment series 9 Protein A Protein: PTPN13 Fragment: 1085-1188 Site: PDZ_1 Construct: his6-MBP-TEVsite-PDZ
Protein B Protein: HPV16-E6 Fragment: 149-158 Site: PBM Modification: (TPO)156 Sequence: SSRTRRETQL Construct: Biotin-ttds-SSRTRREpTQL
Average holdup BI: -0.02
Immobilized partner concentration (10-6 M): 18
Experiment method: CALIP_holdup
Details of affinity fitting: BSA and lysozyme internal standards + bacterial cell lysate + normal layout
Number of measurements: 1
The affinity was below the detection threshold of the assay.
Experiment series 10 Protein A Protein: PTPN13 Fragment: 1085-1188 Site: PDZ_1 Construct: his6-MBP-TEVsite-PDZ
Protein B Protein: HPV16-E6 Fragment: 149-158 Site: PBM Modification: (TPO)156 Sequence: SSRTRRETQL Construct: Biotin-ttds-SSRTRREpTQL
Average holdup BI: 0.02
Normalized holdup BI: 0.02
Immobilized partner concentration (10-6 M): 18
Experiment method: DAPF_holdup
Details of affinity fitting: fluorescein + mCherry internal standards + normalization based on CALIP_holdup data + reverse layout
Number of measurements: 1
The affinity was below the detection threshold of the assay.
Experiment series 11 Protein A Protein: PTPN13 Fragment: 1362-1455 Site: PDZ_2 Construct: his6-MBP-TEVsite-PDZ
Protein B Protein: HPV16-E6 Fragment: 149-158 Site: PBM Modification: (TPO)156 Sequence: SSRTRRETQL Construct: Biotin-ttds-SSRTRREpTQL
Average holdup BI: -0.1
Immobilized partner concentration (10-6 M): 18
Experiment method: CALIP_holdup
Details of affinity fitting: BSA and lysozyme internal standards + bacterial cell lysate + normal layout
Number of measurements: 1
The affinity was below the detection threshold of the assay.
Experiment series 12 Protein A Protein: PTPN13 Fragment: 1495-1591 Site: PDZ_3 Construct: his6-MBP-TEVsite-PDZ
Protein B Protein: HPV16-E6 Fragment: 149-158 Site: PBM Modification: (TPO)156 Sequence: SSRTRRETQL Construct: Biotin-ttds-SSRTRREpTQL
Average holdup BI: -0.08
Immobilized partner concentration (10-6 M): 18
Experiment method: CALIP_holdup
Details of affinity fitting: BSA and lysozyme internal standards + bacterial cell lysate + normal layout
Number of measurements: 1
The affinity was below the detection threshold of the assay.
Experiment series 13 Protein A Protein: PTPN13 Fragment: 1779-1873 Site: PDZ_4 Construct: his6-MBP-TEVsite-PDZ
Protein B Protein: HPV16-E6 Fragment: 149-158 Site: PBM Modification: (TPO)156 Sequence: SSRTRRETQL Construct: Biotin-ttds-SSRTRREpTQL
Average holdup BI: 0.02
Immobilized partner concentration (10-6 M): 18
Experiment method: CALIP_holdup
Details of affinity fitting: BSA and lysozyme internal standards + bacterial cell lysate + normal layout
Number of measurements: 1
The affinity was below the detection threshold of the assay.
Experiment series 14 Protein A Protein: PTPN13 Fragment: 1875-1973 Site: PDZ_5 Construct: his6-MBP-TEVsite-PDZ
Protein B Protein: HPV16-E6 Fragment: 149-158 Site: PBM Modification: (TPO)156 Sequence: SSRTRRETQL Construct: Biotin-ttds-SSRTRREpTQL
Average holdup BI: 0.01
Immobilized partner concentration (10-6 M): 18
Experiment method: CALIP_holdup
Details of affinity fitting: BSA and lysozyme internal standards + bacterial cell lysate + normal layout
Number of measurements: 1
The affinity was below the detection threshold of the assay.
Please cite ProfAff! (Gogl, G. et al., Nature Communications 2022)
© The ProfAff database is developped by the research team of Gergo Gogl .