sigma plot 5·0 Search Results


99
SYSTAT sigma plot 14 5 software
Sigma Plot 14 5 Software, supplied by SYSTAT, 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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Valiant Co Ltd beating buffer
Beating Buffer, supplied by Valiant Co Ltd, used in various techniques. Bioz Stars score: 96/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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Shimadzu Corporation gas chromatograph
Gas Chromatograph, supplied by Shimadzu Corporation, 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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96
Croda International Plc phosphatidylserine
(A-B) Protein-lipid overlay assay. The recombinant GST-tagged N-terminal LRT domain (LRT) and full-length BteA (BteA/BtcA) protein of B. pertussis were incubated at 5 μg/ml with commercial (A) or home-made (B) lipid arrays. The binding was detected using an anti-GST antibody followed by chemiluminescence detection. Recombinant GST was used as a control. Triglyceride (GT); diacylglycerol (DAG); phosphatidic acid (PA); <t>phosphatidylserine</t> (PS); phosphatidylethanolamine (PE); phosphatidylcholine (PC); phosphatidylglycerol (PG); cardiolipin (CL); phosphatidylinositol (PI), and phosphatidylinositol phosphates (PIP, PIP2, PIP3). (C) SPR real-time kinetics of LRT binding to lipid membranes. Serially diluted LRT protein (at 500, 250, 125, 62.5 and 31.25 nM concentrations) was injected in parallel over the neutravidin sensor chip coated with the immobilized liposomes (100 nm in diameter) containing PC, PC/PS (80:20) or PC/PIP2 (95:5), and left to associate (120 s) and dissociate (380 s) at constant flow rate of 30 μl/min. The sensograms show the representative binding curves from five independent “one-shot kinetic” experiments. (D) SPR steady-state analysis of LRT binding to lipid vesicles. Serially diluted LRT protein was injected over the immobilized lipid vesicles to reach the SPR binding equilibrium, and the near-equilibrium values (R eq ) were plotted against LRT concentrations (P 0 ). Solid lines represent binding isotherms determined by a nonlinear fitting of the data using the equation R eq = R max /(1 + K D /P 0 ). The calculated K D values represent the mean ± SD from three independent experiments.
Phosphatidylserine, supplied by Croda International Plc, used in various techniques. Bioz Stars score: 96/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/product/sigma+plot+5%C2%B70/16%3A0-18%3A1+PS/bio_rxiv__2020__11__17__386359-196-43-47
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99
Thermo Fisher mebc buffer
(A-B) Protein-lipid overlay assay. The recombinant GST-tagged N-terminal LRT domain (LRT) and full-length BteA (BteA/BtcA) protein of B. pertussis were incubated at 5 μg/ml with commercial (A) or home-made (B) lipid arrays. The binding was detected using an anti-GST antibody followed by chemiluminescence detection. Recombinant GST was used as a control. Triglyceride (GT); diacylglycerol (DAG); phosphatidic acid (PA); <t>phosphatidylserine</t> (PS); phosphatidylethanolamine (PE); phosphatidylcholine (PC); phosphatidylglycerol (PG); cardiolipin (CL); phosphatidylinositol (PI), and phosphatidylinositol phosphates (PIP, PIP2, PIP3). (C) SPR real-time kinetics of LRT binding to lipid membranes. Serially diluted LRT protein (at 500, 250, 125, 62.5 and 31.25 nM concentrations) was injected in parallel over the neutravidin sensor chip coated with the immobilized liposomes (100 nm in diameter) containing PC, PC/PS (80:20) or PC/PIP2 (95:5), and left to associate (120 s) and dissociate (380 s) at constant flow rate of 30 μl/min. The sensograms show the representative binding curves from five independent “one-shot kinetic” experiments. (D) SPR steady-state analysis of LRT binding to lipid vesicles. Serially diluted LRT protein was injected over the immobilized lipid vesicles to reach the SPR binding equilibrium, and the near-equilibrium values (R eq ) were plotted against LRT concentrations (P 0 ). Solid lines represent binding isotherms determined by a nonlinear fitting of the data using the equation R eq = R max /(1 + K D /P 0 ). The calculated K D values represent the mean ± SD from three independent experiments.
Mebc Buffer, supplied by Thermo Fisher, used in various techniques. Bioz Stars score: 99/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/product/sigma+plot+5%C2%B70/Phosphate/pm22719865-223-15-59
Average 99 stars, based on 1 article reviews
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96
SYSTAT plot v 13
(A-B) Protein-lipid overlay assay. The recombinant GST-tagged N-terminal LRT domain (LRT) and full-length BteA (BteA/BtcA) protein of B. pertussis were incubated at 5 μg/ml with commercial (A) or home-made (B) lipid arrays. The binding was detected using an anti-GST antibody followed by chemiluminescence detection. Recombinant GST was used as a control. Triglyceride (GT); diacylglycerol (DAG); phosphatidic acid (PA); <t>phosphatidylserine</t> (PS); phosphatidylethanolamine (PE); phosphatidylcholine (PC); phosphatidylglycerol (PG); cardiolipin (CL); phosphatidylinositol (PI), and phosphatidylinositol phosphates (PIP, PIP2, PIP3). (C) SPR real-time kinetics of LRT binding to lipid membranes. Serially diluted LRT protein (at 500, 250, 125, 62.5 and 31.25 nM concentrations) was injected in parallel over the neutravidin sensor chip coated with the immobilized liposomes (100 nm in diameter) containing PC, PC/PS (80:20) or PC/PIP2 (95:5), and left to associate (120 s) and dissociate (380 s) at constant flow rate of 30 μl/min. The sensograms show the representative binding curves from five independent “one-shot kinetic” experiments. (D) SPR steady-state analysis of LRT binding to lipid vesicles. Serially diluted LRT protein was injected over the immobilized lipid vesicles to reach the SPR binding equilibrium, and the near-equilibrium values (R eq ) were plotted against LRT concentrations (P 0 ). Solid lines represent binding isotherms determined by a nonlinear fitting of the data using the equation R eq = R max /(1 + K D /P 0 ). The calculated K D values represent the mean ± SD from three independent experiments.
Plot V 13, supplied by SYSTAT, used in various techniques. Bioz Stars score: 96/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/product/sigma+plot+5%C2%B70/SYSTAT+v13%2E1/pmc08536682-247-10-12
Average 96 stars, based on 1 article reviews
plot v 13 - by Bioz Stars, 2026-11
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Image Search Results


(A-B) Protein-lipid overlay assay. The recombinant GST-tagged N-terminal LRT domain (LRT) and full-length BteA (BteA/BtcA) protein of B. pertussis were incubated at 5 μg/ml with commercial (A) or home-made (B) lipid arrays. The binding was detected using an anti-GST antibody followed by chemiluminescence detection. Recombinant GST was used as a control. Triglyceride (GT); diacylglycerol (DAG); phosphatidic acid (PA); phosphatidylserine (PS); phosphatidylethanolamine (PE); phosphatidylcholine (PC); phosphatidylglycerol (PG); cardiolipin (CL); phosphatidylinositol (PI), and phosphatidylinositol phosphates (PIP, PIP2, PIP3). (C) SPR real-time kinetics of LRT binding to lipid membranes. Serially diluted LRT protein (at 500, 250, 125, 62.5 and 31.25 nM concentrations) was injected in parallel over the neutravidin sensor chip coated with the immobilized liposomes (100 nm in diameter) containing PC, PC/PS (80:20) or PC/PIP2 (95:5), and left to associate (120 s) and dissociate (380 s) at constant flow rate of 30 μl/min. The sensograms show the representative binding curves from five independent “one-shot kinetic” experiments. (D) SPR steady-state analysis of LRT binding to lipid vesicles. Serially diluted LRT protein was injected over the immobilized lipid vesicles to reach the SPR binding equilibrium, and the near-equilibrium values (R eq ) were plotted against LRT concentrations (P 0 ). Solid lines represent binding isotherms determined by a nonlinear fitting of the data using the equation R eq = R max /(1 + K D /P 0 ). The calculated K D values represent the mean ± SD from three independent experiments.

Journal: bioRxiv

Article Title: Lipid binding by N-terminal motif mediates plasma membrane localization of Bordetella effector protein BteA

doi: 10.1101/2020.11.17.386359

Figure Lengend Snippet: (A-B) Protein-lipid overlay assay. The recombinant GST-tagged N-terminal LRT domain (LRT) and full-length BteA (BteA/BtcA) protein of B. pertussis were incubated at 5 μg/ml with commercial (A) or home-made (B) lipid arrays. The binding was detected using an anti-GST antibody followed by chemiluminescence detection. Recombinant GST was used as a control. Triglyceride (GT); diacylglycerol (DAG); phosphatidic acid (PA); phosphatidylserine (PS); phosphatidylethanolamine (PE); phosphatidylcholine (PC); phosphatidylglycerol (PG); cardiolipin (CL); phosphatidylinositol (PI), and phosphatidylinositol phosphates (PIP, PIP2, PIP3). (C) SPR real-time kinetics of LRT binding to lipid membranes. Serially diluted LRT protein (at 500, 250, 125, 62.5 and 31.25 nM concentrations) was injected in parallel over the neutravidin sensor chip coated with the immobilized liposomes (100 nm in diameter) containing PC, PC/PS (80:20) or PC/PIP2 (95:5), and left to associate (120 s) and dissociate (380 s) at constant flow rate of 30 μl/min. The sensograms show the representative binding curves from five independent “one-shot kinetic” experiments. (D) SPR steady-state analysis of LRT binding to lipid vesicles. Serially diluted LRT protein was injected over the immobilized lipid vesicles to reach the SPR binding equilibrium, and the near-equilibrium values (R eq ) were plotted against LRT concentrations (P 0 ). Solid lines represent binding isotherms determined by a nonlinear fitting of the data using the equation R eq = R max /(1 + K D /P 0 ). The calculated K D values represent the mean ± SD from three independent experiments.

Article Snippet: To prepare home-made lipid arrays, solutions of 5 μM, 50 μM and 500 μM of cholesterol (cat.no.C8667, Sigma Aldrich, USA), phosphatidic acid (PA 16:0-18:1; cat.no.840857P, Avanti Polar Lipids, USA,), phosphatidylethanolamine (PE 16:0-18:1; cat.no.01991, Sigma Aldrich, USA), phosphatidylcholine (PC 16:0-18:1; cat.no.42773, Sigma Aldrich, USA), phosphatidylserine (PS 16:0-18:1; cat.no.840034P, Avanti Polar Lipids, USA), phosphatidylinositol (PI 16:0-18:1; cat.no.850142P, Avanti Polar Lipids, USA) or phosphatidylinositol 4,5-bisphosphate (PI(4,5)P2 18:1-18:1; cat.no.850155P, Avanti Polar Lipids, USA) were prepared in chloroform or in a 20:9:1 mixture of chloroform / methanol / H 2 O in the case of PIP2.

Techniques: Protein-lipid Overlay Assay (PLOA), Recombinant, Incubation, Binding Assay, Injection