Details of experiments between Q8TBB1 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: LNX1 Fragment: 261-371 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: 0.05
Normalized holdup BI: 0.05
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 : 3.51
Experiment series 2 Protein A Protein: LNX1 Fragment: 500-596 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: 0.05
Normalized holdup BI: 0.05
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 : 3.51
Experiment series 3 Protein A Protein: LNX1 Fragment: 371-470 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: 0.05
Normalized holdup BI: 0.05
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 : 3.47
Experiment series 4 Protein A Protein: LNX1 Fragment: 261-371 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 5 Protein A Protein: LNX1 Fragment: 261-371 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: 0.04
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 6 Protein A Protein: LNX1 Fragment: 261-371 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: 0.08
Holdup BI standard deviation: 0.14
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: 4
The affinity was below the detection threshold of the assay.
Experiment series 7 Protein A Protein: LNX1 Fragment: 371-470 Site: PDZ_2 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: -0.04
Normalized holdup BI: -0.04
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 8 Protein A Protein: LNX1 Fragment: 371-470 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
Normalized holdup BI: -0
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 9 Protein A Protein: LNX1 Fragment: 371-470 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: 0.03
Holdup BI standard deviation: 0.09
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: 6
The affinity was below the detection threshold of the assay.
Experiment series 10 Protein A Protein: LNX1 Fragment: 500-596 Site: PDZ_3 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: -0.01
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 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 11 Protein A Protein: LNX1 Fragment: 500-596 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: 0.01
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 12 Protein A Protein: LNX1 Fragment: 500-596 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: 0.1
Holdup BI standard deviation: 0.18
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: 6
The affinity was below the detection threshold of the assay.
Experiment series 13 Protein A Protein: LNX1 Fragment: 631-726 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: 0.08
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: 4
The affinity was below the detection threshold of the assay.
Experiment series 14 Protein A Protein: LNX1 Fragment: 261-371 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: -0.04
Normalized holdup BI: -0.07
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 15 Protein A Protein: LNX1 Fragment: 371-470 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: -0.03
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.
Experiment series 16 Protein A Protein: LNX1 Fragment: 371-470 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
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 17 Protein A Protein: LNX1 Fragment: 500-596 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: -0.03
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.
Please cite ProfAff! (Gogl, G. et al., Nature Communications 2022)
© The ProfAff database is developped by the research team of Gergo Gogl .