Details of experiments between Q15418 and Q8TDM6 Note that the results of all experiments are listed, regardless of the modification states of the fragments.
Experiment series 1 Protein A Protein: RPS6KA1 Fragment: 725-735 Site: PBM Sequence: RVRKLPSTTL Construct: biotin-ttds-RRVRKLPSTTL
Protein B Protein: DLG5 Fragment: 1336-1439 Site: PDZ_3 Construct: his6-MBP-TEVsite-PDZ
Average holdup BI: -0.01
Holdup BI standard deviation: 0.06
Immobilized partner concentration (10-6 M): 31
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 2 Protein A Protein: RPS6KA1 Fragment: 725-735 Site: PBM Sequence: RVRKLPSTTL Construct: biotin-ttds-RRVRKLPSTTL
Protein B Protein: DLG5 Fragment: 1492-1595 Site: PDZ_4 Construct: his6-MBP-TEVsite-PDZ
Average holdup BI: -0.01
Holdup BI standard deviation: 0.02
Immobilized partner concentration (10-6 M): 31
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 3 Protein A Protein: RPS6KA1 Fragment: 725-735 Site: PBM Sequence: RVRKLPSTTL Construct: biotin-ttds-RRVRKLPSTTL
Protein B Protein: DLG5 Fragment: 616-713 Site: PDZ_1 Construct: his6-MBP-TEVsite-PDZ
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 4 Protein A Protein: RPS6KA1 Fragment: 725-735 Site: PBM Sequence: RVRKLPSTTL Construct: biotin-ttds-RRVRKLPSTTL
Protein B Protein: DLG5 Fragment: 616-713 Site: PDZ_1 Construct: his6-MBP-TEVsite-PDZ
Average holdup BI: -0.07
Holdup BI standard deviation: 0.04
Immobilized partner concentration (10-6 M): 31
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 5 Protein A Protein: RPS6KA1 Fragment: 725-735 Site: PBM Sequence: RVRKLPSTTL Construct: biotin-ttds-RRVRKLPSTTL
Protein B Protein: DLG5 Fragment: 714-800 Site: PDZ_2 Construct: his6-MBP-TEVsite-PDZ
Average holdup BI: -0.02
Holdup BI standard deviation: 0.07
Immobilized partner concentration (10-6 M): 31
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 6 Protein A Protein: RPS6KA1 Fragment: 726-735 Site: PBM Sequence: RVRKLPSTTL Construct: Biotin-ado-ado-RVRKLPSTTL
Protein B Protein: DLG5 Fragment: 616-713 Site: PDZ_1 Construct: his6-MBP-TEVsite-PDZ
Average holdup BI: -0.07
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.
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 7 Protein A Protein: RPS6KA1 Fragment: 725-735 Site: PBM Modification: (SEP)732 Sequence: RVRKLPSTTL Construct: biotin-ttds-RRVRKLPpSTTL
Protein B Protein: DLG5 Fragment: 1336-1439 Site: PDZ_3 Construct: his6-MBP-TEVsite-PDZ
Average holdup BI: -0.08
Holdup BI standard deviation: 0.05
Immobilized partner concentration (10-6 M): 40
Experiment method: CALIP_holdup
Details of affinity fitting: BSA and lysozyme internal standards + bacterial cell lysate + normal layout
Number of measurements: 3
The affinity was below the detection threshold of the assay.
Experiment series 8 Protein A Protein: RPS6KA1 Fragment: 725-735 Site: PBM Modification: (SEP)732 Sequence: RVRKLPSTTL Construct: biotin-ttds-RRVRKLPpSTTL
Protein B Protein: DLG5 Fragment: 1492-1595 Site: PDZ_4 Construct: his6-MBP-TEVsite-PDZ
Average holdup BI: 0.08
Holdup BI standard deviation: 0.03
Immobilized partner concentration (10-6 M): 40
Experiment method: CALIP_holdup
Details of affinity fitting: BSA and lysozyme internal standards + bacterial cell lysate + normal layout
Number of measurements: 3
The affinity was below the detection threshold of the assay.
Experiment series 9 Protein A Protein: RPS6KA1 Fragment: 725-735 Site: PBM Modification: (SEP)732 Sequence: RVRKLPSTTL Construct: biotin-ttds-RRVRKLPpSTTL
Protein B Protein: DLG5 Fragment: 616-713 Site: PDZ_1 Construct: his6-MBP-TEVsite-PDZ
Average holdup BI: -0.02
Normalized holdup BI: -0.02
Immobilized partner concentration (10-6 M): 15
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 10 Protein A Protein: RPS6KA1 Fragment: 725-735 Site: PBM Modification: (SEP)732 Sequence: RVRKLPSTTL Construct: biotin-ttds-RRVRKLPpSTTL
Protein B Protein: DLG5 Fragment: 616-713 Site: PDZ_1 Construct: his6-MBP-TEVsite-PDZ
Average holdup BI: 0.04
Normalized holdup BI: 0.04
Immobilized partner concentration (10-6 M): 15
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 11 Protein A Protein: RPS6KA1 Fragment: 725-735 Site: PBM Modification: (SEP)732 Sequence: RVRKLPSTTL Construct: biotin-ttds-RRVRKLPpSTTL
Protein B Protein: DLG5 Fragment: 616-713 Site: PDZ_1 Construct: his6-MBP-TEVsite-PDZ
Average holdup BI: -0.02
Holdup BI standard deviation: 0.04
Immobilized partner concentration (10-6 M): 40
Experiment method: CALIP_holdup
Details of affinity fitting: BSA and lysozyme internal standards + bacterial cell lysate + normal layout
Number of measurements: 3
The affinity was below the detection threshold of the assay.
Experiment series 12 Protein A Protein: RPS6KA1 Fragment: 725-735 Site: PBM Modification: (SEP)732 Sequence: RVRKLPSTTL Construct: biotin-ttds-RRVRKLPpSTTL
Protein B Protein: DLG5 Fragment: 714-800 Site: PDZ_2 Construct: his6-MBP-TEVsite-PDZ
Average holdup BI: -0.01
Holdup BI standard deviation: 0.01
Immobilized partner concentration (10-6 M): 40
Experiment method: CALIP_holdup
Details of affinity fitting: BSA and lysozyme internal standards + bacterial cell lysate + normal layout
Number of measurements: 3
The affinity was below the detection threshold of the assay.
Experiment series 13 Protein A Protein: RPS6KA1 Fragment: 725-735 Site: PBM Modification: (TPO)733 Sequence: RVRKLPSTTL Construct: biotin-ttds-RRVRKLPSpTTL
Protein B Protein: DLG5 Fragment: 616-713 Site: PDZ_1 Construct: his6-MBP-TEVsite-PDZ
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.
Experiment series 14 Protein A Protein: RPS6KA1 Fragment: 725-735 Site: PBM Modification: (TPO)734 Sequence: RVRKLPSTTL Construct: Biotin-ttds-RRVRKLPSTpTL
Protein B Protein: DLG5 Fragment: 616-713 Site: PDZ_1 Construct: his6-MBP-TEVsite-PDZ
Average holdup BI: 0.05
Normalized holdup BI: 0.05
Immobilized partner concentration (10-6 M): 25
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 .