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spodoptera frugiperda sf9 cells  (Expression Systems Inc)
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IRBIT binding to PLCδ 1 -PH depends on its serine-rich region A. Surface plasmon resonance (SPR) measurements of GST/PLCδ 1 -PH binding to immobilized full-length His 6 -tagged IRBIT produced in <t>Sf9</t> cells. Wild-type IRBIT (IRBIT-WT; black) is compared with variants in which the seven serines highlighted in yellow and numbered in the IRBIT N-terminal sequence fragment shown at the top of the figure were replaced by alanines (IRBIT-A 7 ; gray) or glutamates (IRBIT-E 7 ; green). Failure to phosphorylate these serines also prevents binding. Responses were corrected by subtraction of a mock-coupled surface and expressed as a percentage of the maximal SPR response. These experiments are representative of at least three repeats. B. Biolayer interferometry (BLI) concentration/response measurements for soluble full-length IRBIT variants binding to GST/PLCδ 1 -PH immobilized on Octet anti-GST biosensors. IRBIT-WT (black), S66A/S70A/S77A-mutated IRBIT (magenta), S68A/S71A/S74A-mutated IRBIT (olive), and IRBIT-A 7 (gray) are compared. Immobilized GST/Dyn1-PH (maroon) provides a low-binding control. Individual points show the mean response during the final 20 s of association in the BLI experiment, after subtraction of the corresponding response for equivalent sensors on which GST-only had been immobilized. Responses were normalized to the mean fitted B max for IRBIT-WT and IRBIT S66A/S70A/S77A in the same experiment. The data shown are representative of three independent experiments. C. BLI association traces for binding of IRBIT-WT from a 5 μM solution to sensor-immobilized GST/PLCδ 1 -PH with no soluble competitor (in matched buffer; black/gray) or in the presence of 25 μM Ins(1,4,5) P 3 (red) as competitor. Traces were aligned at association onset, corrected by subtraction of signal from a matched GST-only sensor (and competitor-only signals), and normalized to the endpoint obtained with no competitor Fainter lines represent individual experiments; bold lines show means (no competitor, n = 4; Ins(1,4,5) P 3 , n = 3). One sensor was used per condition within each experiment.
Spodoptera Frugiperda Sf9 Cells, supplied by Expression Systems Inc, used in various techniques. Bioz Stars score: 99/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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sf9 spodoptera frugiperda cells  (Expression Systems Inc)
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Expression Systems Inc sf9 spodoptera frugiperda cells
IRBIT binding to PLCδ 1 -PH depends on its serine-rich region A. Surface plasmon resonance (SPR) measurements of GST/PLCδ 1 -PH binding to immobilized full-length His 6 -tagged IRBIT produced in <t>Sf9</t> cells. Wild-type IRBIT (IRBIT-WT; black) is compared with variants in which the seven serines highlighted in yellow and numbered in the IRBIT N-terminal sequence fragment shown at the top of the figure were replaced by alanines (IRBIT-A 7 ; gray) or glutamates (IRBIT-E 7 ; green). Failure to phosphorylate these serines also prevents binding. Responses were corrected by subtraction of a mock-coupled surface and expressed as a percentage of the maximal SPR response. These experiments are representative of at least three repeats. B. Biolayer interferometry (BLI) concentration/response measurements for soluble full-length IRBIT variants binding to GST/PLCδ 1 -PH immobilized on Octet anti-GST biosensors. IRBIT-WT (black), S66A/S70A/S77A-mutated IRBIT (magenta), S68A/S71A/S74A-mutated IRBIT (olive), and IRBIT-A 7 (gray) are compared. Immobilized GST/Dyn1-PH (maroon) provides a low-binding control. Individual points show the mean response during the final 20 s of association in the BLI experiment, after subtraction of the corresponding response for equivalent sensors on which GST-only had been immobilized. Responses were normalized to the mean fitted B max for IRBIT-WT and IRBIT S66A/S70A/S77A in the same experiment. The data shown are representative of three independent experiments. C. BLI association traces for binding of IRBIT-WT from a 5 μM solution to sensor-immobilized GST/PLCδ 1 -PH with no soluble competitor (in matched buffer; black/gray) or in the presence of 25 μM Ins(1,4,5) P 3 (red) as competitor. Traces were aligned at association onset, corrected by subtraction of signal from a matched GST-only sensor (and competitor-only signals), and normalized to the endpoint obtained with no competitor Fainter lines represent individual experiments; bold lines show means (no competitor, n = 4; Ins(1,4,5) P 3 , n = 3). One sensor was used per condition within each experiment.
Sf9 Spodoptera Frugiperda Cells, supplied by Expression Systems Inc, used in various techniques. Bioz Stars score: 99/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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spodoptera frugiperda 9 sf9 cells  (Expression Systems Inc)
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IRBIT binding to PLCδ 1 -PH depends on its serine-rich region A. Surface plasmon resonance (SPR) measurements of GST/PLCδ 1 -PH binding to immobilized full-length His 6 -tagged IRBIT produced in <t>Sf9</t> cells. Wild-type IRBIT (IRBIT-WT; black) is compared with variants in which the seven serines highlighted in yellow and numbered in the IRBIT N-terminal sequence fragment shown at the top of the figure were replaced by alanines (IRBIT-A 7 ; gray) or glutamates (IRBIT-E 7 ; green). Failure to phosphorylate these serines also prevents binding. Responses were corrected by subtraction of a mock-coupled surface and expressed as a percentage of the maximal SPR response. These experiments are representative of at least three repeats. B. Biolayer interferometry (BLI) concentration/response measurements for soluble full-length IRBIT variants binding to GST/PLCδ 1 -PH immobilized on Octet anti-GST biosensors. IRBIT-WT (black), S66A/S70A/S77A-mutated IRBIT (magenta), S68A/S71A/S74A-mutated IRBIT (olive), and IRBIT-A 7 (gray) are compared. Immobilized GST/Dyn1-PH (maroon) provides a low-binding control. Individual points show the mean response during the final 20 s of association in the BLI experiment, after subtraction of the corresponding response for equivalent sensors on which GST-only had been immobilized. Responses were normalized to the mean fitted B max for IRBIT-WT and IRBIT S66A/S70A/S77A in the same experiment. The data shown are representative of three independent experiments. C. BLI association traces for binding of IRBIT-WT from a 5 μM solution to sensor-immobilized GST/PLCδ 1 -PH with no soluble competitor (in matched buffer; black/gray) or in the presence of 25 μM Ins(1,4,5) P 3 (red) as competitor. Traces were aligned at association onset, corrected by subtraction of signal from a matched GST-only sensor (and competitor-only signals), and normalized to the endpoint obtained with no competitor Fainter lines represent individual experiments; bold lines show means (no competitor, n = 4; Ins(1,4,5) P 3 , n = 3). One sensor was used per condition within each experiment.
Spodoptera Frugiperda 9 Sf9 Cells, supplied by Expression Systems Inc, used in various techniques. Bioz Stars score: 99/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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spodoptera frugiperda sf 9 insect cells  (Expression Systems Inc)
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Expression Systems Inc spodoptera frugiperda sf 9 insect cells
IRBIT binding to PLCδ 1 -PH depends on its serine-rich region A. Surface plasmon resonance (SPR) measurements of GST/PLCδ 1 -PH binding to immobilized full-length His 6 -tagged IRBIT produced in <t>Sf9</t> cells. Wild-type IRBIT (IRBIT-WT; black) is compared with variants in which the seven serines highlighted in yellow and numbered in the IRBIT N-terminal sequence fragment shown at the top of the figure were replaced by alanines (IRBIT-A 7 ; gray) or glutamates (IRBIT-E 7 ; green). Failure to phosphorylate these serines also prevents binding. Responses were corrected by subtraction of a mock-coupled surface and expressed as a percentage of the maximal SPR response. These experiments are representative of at least three repeats. B. Biolayer interferometry (BLI) concentration/response measurements for soluble full-length IRBIT variants binding to GST/PLCδ 1 -PH immobilized on Octet anti-GST biosensors. IRBIT-WT (black), S66A/S70A/S77A-mutated IRBIT (magenta), S68A/S71A/S74A-mutated IRBIT (olive), and IRBIT-A 7 (gray) are compared. Immobilized GST/Dyn1-PH (maroon) provides a low-binding control. Individual points show the mean response during the final 20 s of association in the BLI experiment, after subtraction of the corresponding response for equivalent sensors on which GST-only had been immobilized. Responses were normalized to the mean fitted B max for IRBIT-WT and IRBIT S66A/S70A/S77A in the same experiment. The data shown are representative of three independent experiments. C. BLI association traces for binding of IRBIT-WT from a 5 μM solution to sensor-immobilized GST/PLCδ 1 -PH with no soluble competitor (in matched buffer; black/gray) or in the presence of 25 μM Ins(1,4,5) P 3 (red) as competitor. Traces were aligned at association onset, corrected by subtraction of signal from a matched GST-only sensor (and competitor-only signals), and normalized to the endpoint obtained with no competitor Fainter lines represent individual experiments; bold lines show means (no competitor, n = 4; Ins(1,4,5) P 3 , n = 3). One sensor was used per condition within each experiment.
Spodoptera Frugiperda Sf 9 Insect Cells, supplied by Expression Systems Inc, used in various techniques. Bioz Stars score: 95/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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spodoptera frugiperda sf9 insect  (Expression Systems Inc)
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Expression Systems Inc spodoptera frugiperda sf9 insect
IRBIT binding to PLCδ 1 -PH depends on its serine-rich region A. Surface plasmon resonance (SPR) measurements of GST/PLCδ 1 -PH binding to immobilized full-length His 6 -tagged IRBIT produced in <t>Sf9</t> cells. Wild-type IRBIT (IRBIT-WT; black) is compared with variants in which the seven serines highlighted in yellow and numbered in the IRBIT N-terminal sequence fragment shown at the top of the figure were replaced by alanines (IRBIT-A 7 ; gray) or glutamates (IRBIT-E 7 ; green). Failure to phosphorylate these serines also prevents binding. Responses were corrected by subtraction of a mock-coupled surface and expressed as a percentage of the maximal SPR response. These experiments are representative of at least three repeats. B. Biolayer interferometry (BLI) concentration/response measurements for soluble full-length IRBIT variants binding to GST/PLCδ 1 -PH immobilized on Octet anti-GST biosensors. IRBIT-WT (black), S66A/S70A/S77A-mutated IRBIT (magenta), S68A/S71A/S74A-mutated IRBIT (olive), and IRBIT-A 7 (gray) are compared. Immobilized GST/Dyn1-PH (maroon) provides a low-binding control. Individual points show the mean response during the final 20 s of association in the BLI experiment, after subtraction of the corresponding response for equivalent sensors on which GST-only had been immobilized. Responses were normalized to the mean fitted B max for IRBIT-WT and IRBIT S66A/S70A/S77A in the same experiment. The data shown are representative of three independent experiments. C. BLI association traces for binding of IRBIT-WT from a 5 μM solution to sensor-immobilized GST/PLCδ 1 -PH with no soluble competitor (in matched buffer; black/gray) or in the presence of 25 μM Ins(1,4,5) P 3 (red) as competitor. Traces were aligned at association onset, corrected by subtraction of signal from a matched GST-only sensor (and competitor-only signals), and normalized to the endpoint obtained with no competitor Fainter lines represent individual experiments; bold lines show means (no competitor, n = 4; Ins(1,4,5) P 3 , n = 3). One sensor was used per condition within each experiment.
Spodoptera Frugiperda Sf9 Insect, supplied by Expression Systems Inc, used in various techniques. Bioz Stars score: 95/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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spodoptera frugiperda  (Expression Systems Inc)
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Expression Systems Inc spodoptera frugiperda
IRBIT binding to PLCδ 1 -PH depends on its serine-rich region A. Surface plasmon resonance (SPR) measurements of GST/PLCδ 1 -PH binding to immobilized full-length His 6 -tagged IRBIT produced in <t>Sf9</t> cells. Wild-type IRBIT (IRBIT-WT; black) is compared with variants in which the seven serines highlighted in yellow and numbered in the IRBIT N-terminal sequence fragment shown at the top of the figure were replaced by alanines (IRBIT-A 7 ; gray) or glutamates (IRBIT-E 7 ; green). Failure to phosphorylate these serines also prevents binding. Responses were corrected by subtraction of a mock-coupled surface and expressed as a percentage of the maximal SPR response. These experiments are representative of at least three repeats. B. Biolayer interferometry (BLI) concentration/response measurements for soluble full-length IRBIT variants binding to GST/PLCδ 1 -PH immobilized on Octet anti-GST biosensors. IRBIT-WT (black), S66A/S70A/S77A-mutated IRBIT (magenta), S68A/S71A/S74A-mutated IRBIT (olive), and IRBIT-A 7 (gray) are compared. Immobilized GST/Dyn1-PH (maroon) provides a low-binding control. Individual points show the mean response during the final 20 s of association in the BLI experiment, after subtraction of the corresponding response for equivalent sensors on which GST-only had been immobilized. Responses were normalized to the mean fitted B max for IRBIT-WT and IRBIT S66A/S70A/S77A in the same experiment. The data shown are representative of three independent experiments. C. BLI association traces for binding of IRBIT-WT from a 5 μM solution to sensor-immobilized GST/PLCδ 1 -PH with no soluble competitor (in matched buffer; black/gray) or in the presence of 25 μM Ins(1,4,5) P 3 (red) as competitor. Traces were aligned at association onset, corrected by subtraction of signal from a matched GST-only sensor (and competitor-only signals), and normalized to the endpoint obtained with no competitor Fainter lines represent individual experiments; bold lines show means (no competitor, n = 4; Ins(1,4,5) P 3 , n = 3). One sensor was used per condition within each experiment.
Spodoptera Frugiperda, supplied by Expression Systems Inc, used in various techniques. Bioz Stars score: 99/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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IRBIT binding to PLCδ 1 -PH depends on its serine-rich region A. Surface plasmon resonance (SPR) measurements of GST/PLCδ 1 -PH binding to immobilized full-length His 6 -tagged IRBIT produced in Sf9 cells. Wild-type IRBIT (IRBIT-WT; black) is compared with variants in which the seven serines highlighted in yellow and numbered in the IRBIT N-terminal sequence fragment shown at the top of the figure were replaced by alanines (IRBIT-A 7 ; gray) or glutamates (IRBIT-E 7 ; green). Failure to phosphorylate these serines also prevents binding. Responses were corrected by subtraction of a mock-coupled surface and expressed as a percentage of the maximal SPR response. These experiments are representative of at least three repeats. B. Biolayer interferometry (BLI) concentration/response measurements for soluble full-length IRBIT variants binding to GST/PLCδ 1 -PH immobilized on Octet anti-GST biosensors. IRBIT-WT (black), S66A/S70A/S77A-mutated IRBIT (magenta), S68A/S71A/S74A-mutated IRBIT (olive), and IRBIT-A 7 (gray) are compared. Immobilized GST/Dyn1-PH (maroon) provides a low-binding control. Individual points show the mean response during the final 20 s of association in the BLI experiment, after subtraction of the corresponding response for equivalent sensors on which GST-only had been immobilized. Responses were normalized to the mean fitted B max for IRBIT-WT and IRBIT S66A/S70A/S77A in the same experiment. The data shown are representative of three independent experiments. C. BLI association traces for binding of IRBIT-WT from a 5 μM solution to sensor-immobilized GST/PLCδ 1 -PH with no soluble competitor (in matched buffer; black/gray) or in the presence of 25 μM Ins(1,4,5) P 3 (red) as competitor. Traces were aligned at association onset, corrected by subtraction of signal from a matched GST-only sensor (and competitor-only signals), and normalized to the endpoint obtained with no competitor Fainter lines represent individual experiments; bold lines show means (no competitor, n = 4; Ins(1,4,5) P 3 , n = 3). One sensor was used per condition within each experiment.

Journal: bioRxiv

Article Title: Recognition of negative charge arrays by pleckstrin homology (PH) domains

doi: 10.64898/2026.09.21.753330

Figure Lengend Snippet: IRBIT binding to PLCδ 1 -PH depends on its serine-rich region A. Surface plasmon resonance (SPR) measurements of GST/PLCδ 1 -PH binding to immobilized full-length His 6 -tagged IRBIT produced in Sf9 cells. Wild-type IRBIT (IRBIT-WT; black) is compared with variants in which the seven serines highlighted in yellow and numbered in the IRBIT N-terminal sequence fragment shown at the top of the figure were replaced by alanines (IRBIT-A 7 ; gray) or glutamates (IRBIT-E 7 ; green). Failure to phosphorylate these serines also prevents binding. Responses were corrected by subtraction of a mock-coupled surface and expressed as a percentage of the maximal SPR response. These experiments are representative of at least three repeats. B. Biolayer interferometry (BLI) concentration/response measurements for soluble full-length IRBIT variants binding to GST/PLCδ 1 -PH immobilized on Octet anti-GST biosensors. IRBIT-WT (black), S66A/S70A/S77A-mutated IRBIT (magenta), S68A/S71A/S74A-mutated IRBIT (olive), and IRBIT-A 7 (gray) are compared. Immobilized GST/Dyn1-PH (maroon) provides a low-binding control. Individual points show the mean response during the final 20 s of association in the BLI experiment, after subtraction of the corresponding response for equivalent sensors on which GST-only had been immobilized. Responses were normalized to the mean fitted B max for IRBIT-WT and IRBIT S66A/S70A/S77A in the same experiment. The data shown are representative of three independent experiments. C. BLI association traces for binding of IRBIT-WT from a 5 μM solution to sensor-immobilized GST/PLCδ 1 -PH with no soluble competitor (in matched buffer; black/gray) or in the presence of 25 μM Ins(1,4,5) P 3 (red) as competitor. Traces were aligned at association onset, corrected by subtraction of signal from a matched GST-only sensor (and competitor-only signals), and normalized to the endpoint obtained with no competitor Fainter lines represent individual experiments; bold lines show means (no competitor, n = 4; Ins(1,4,5) P 3 , n = 3). One sensor was used per condition within each experiment.

Article Snippet: Spodoptera frugiperda Sf9 cells (Expression Systems), originally established from immature ovaries of female S. frugiperda pupae, were propagated at 27°C with constant shaking at 120 rpm in either serum-free ESF 921 Insect Cell Culture Medium (Expression Systems) containing 50 U/mL penicillin/streptomycin or Insect-XPRESS medium (Lonza), and were used for production of all proteins.

Techniques: Binding Assay, SPR Assay, Produced, Sequencing, Concentration Assay, Control