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origin 7 itc software package  (Malvern Panalytical)


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    Structured Review

    Malvern Panalytical origin 7 itc software package
    Interaction of LYP with F-BAR dimers. A , B HEK293 cells were transfected with PSTPIP1 F-BAR dimers in 3xmyc plasmid, as indicated in the top of the panels, and with 3xFLAG-LYP. Lysates were immunoprecipitated with myc Ab and LYP bound to PSTPIP1 was detected by IB with Ab for LYP. Expression of the proteins was verified by IB in total lysates (TL) with the same Abs. C Determination of the interaction stoichiometry by titration of fluorescein-LYP-CTH (1 µM) with the F-BAR of PSTPIP1 (residues 1–289) using fluorescence anisotropy. The stoichiometry ( N ) was determined from the intersection of asymptotic lines in the linear ascending and saturation (i.e. plateau) regions. D <t>ITC</t> analysis of LYP binding to PSTPIP1. Upper panel, heat exchange of the dilution of the unlabeled LYP-CTH peptide in buffer 20 mM sodium phosphate (pH 7.5), 150 mM NaCl, 5% (v/v) DMSO (upper trace) and representative thermogram of the binding of LYP-CTH to the F-BAR of PSTPIP1 (lower trace). Lower panel, LYP binding isotherm to PSTPIP1. The red line is the fit of a one binding site model to the heat changes of the interaction after subtracting the heat change of the dilution of LYP in buffer. The reported values of N , k d , and binding enthalpy (Δ H ) are the means ± standard deviations of three independent experiments
    Origin 7 Itc Software Package, supplied by Malvern Panalytical, used in various techniques. Bioz Stars score: 99/100, based on 16279 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/product/origin+7+software+package/PEAQ-ITC/pmc08840930-94-5-10
    Average 99 stars, based on 16279 article reviews
    origin 7 itc software package - by Bioz Stars, 2026-11
    99/100 stars

    Images

    1) Product Images from "PSTPIP1-LYP phosphatase interaction: structural basis and implications for autoinflammatory disorders"

    Article Title: PSTPIP1-LYP phosphatase interaction: structural basis and implications for autoinflammatory disorders

    Journal: Cellular and Molecular Life Sciences

    doi: 10.1007/s00018-022-04173-w

    Interaction of LYP with F-BAR dimers. A , B HEK293 cells were transfected with PSTPIP1 F-BAR dimers in 3xmyc plasmid, as indicated in the top of the panels, and with 3xFLAG-LYP. Lysates were immunoprecipitated with myc Ab and LYP bound to PSTPIP1 was detected by IB with Ab for LYP. Expression of the proteins was verified by IB in total lysates (TL) with the same Abs. C Determination of the interaction stoichiometry by titration of fluorescein-LYP-CTH (1 µM) with the F-BAR of PSTPIP1 (residues 1–289) using fluorescence anisotropy. The stoichiometry ( N ) was determined from the intersection of asymptotic lines in the linear ascending and saturation (i.e. plateau) regions. D ITC analysis of LYP binding to PSTPIP1. Upper panel, heat exchange of the dilution of the unlabeled LYP-CTH peptide in buffer 20 mM sodium phosphate (pH 7.5), 150 mM NaCl, 5% (v/v) DMSO (upper trace) and representative thermogram of the binding of LYP-CTH to the F-BAR of PSTPIP1 (lower trace). Lower panel, LYP binding isotherm to PSTPIP1. The red line is the fit of a one binding site model to the heat changes of the interaction after subtracting the heat change of the dilution of LYP in buffer. The reported values of N , k d , and binding enthalpy (Δ H ) are the means ± standard deviations of three independent experiments
    Figure Legend Snippet: Interaction of LYP with F-BAR dimers. A , B HEK293 cells were transfected with PSTPIP1 F-BAR dimers in 3xmyc plasmid, as indicated in the top of the panels, and with 3xFLAG-LYP. Lysates were immunoprecipitated with myc Ab and LYP bound to PSTPIP1 was detected by IB with Ab for LYP. Expression of the proteins was verified by IB in total lysates (TL) with the same Abs. C Determination of the interaction stoichiometry by titration of fluorescein-LYP-CTH (1 µM) with the F-BAR of PSTPIP1 (residues 1–289) using fluorescence anisotropy. The stoichiometry ( N ) was determined from the intersection of asymptotic lines in the linear ascending and saturation (i.e. plateau) regions. D ITC analysis of LYP binding to PSTPIP1. Upper panel, heat exchange of the dilution of the unlabeled LYP-CTH peptide in buffer 20 mM sodium phosphate (pH 7.5), 150 mM NaCl, 5% (v/v) DMSO (upper trace) and representative thermogram of the binding of LYP-CTH to the F-BAR of PSTPIP1 (lower trace). Lower panel, LYP binding isotherm to PSTPIP1. The red line is the fit of a one binding site model to the heat changes of the interaction after subtracting the heat change of the dilution of LYP in buffer. The reported values of N , k d , and binding enthalpy (Δ H ) are the means ± standard deviations of three independent experiments

    Techniques Used: Transfection, Plasmid Preparation, Immunoprecipitation, Expressing, Titration, Fluorescence, Binding Assay

    Related Articles

    Isothermal Titration Calorimetry:

    Article Title: Molecular recognition of myosin L by the Toxoplasma gondii calmodulin.
    Article Snippet: .. Isothermal titration calorimetry (ITC) experiments were performed at 25 ◦C using a MicroCal PEAQ-ITC instrument (Malvern Ltd.,UK) as described [8]. ..

    Article Title: Differential recognition of β-catenin and TRIP6 by MAGI1 PDZ6 and allosteric modulation by DLL1.
    Article Snippet: .. Isothermal titration calorimetry Binding of DLL1 to MAGI1 was characterized by isothermal titration calorimetry (ITC) using a MicroCal PEAQ-ITC calorimeter (Malvern Panalytical). ..

    Article Title: Psyllid glycine-rich antimicrobial peptides oligomerize to directly cleave zinc transporter ZnuA on the membranes of citrus Huanglongbing pathogen.
    Article Snippet: .. 1670 Isothermal titration calorimetry (ITC) assay 1671 The binding affinity of DcGrAMP1 to CLas ZnuA and their mutants was quantified 1672 by ITC using a MicroCal PEAQ-ITC system (Malvern Panalytical). ..

    Article Title: Stk1 is required for BlaR1-mediated broad-spectrum β-lactam resistance in epidemic-causing strains of Staphylococcus aureus.
    Article Snippet: %Inhibition = 100× 1 Rate Background Rateð Þ Maximum Rate Background Rateð Þ ð1Þ IC50 values anderrorswerederived from thenon-linear regression analysis of these % inhibition curves using GraphPad Prism. .. Isothermal Titration Calorimetry binding data of Stk1 KD and GWX inhibitor Isothermal titration calorimetry (ITC) measurements were performed using a MicroCal PEAQ-ITC instrument (Malvern) at 25 °C in highfeedback mode with a stirring speed of 750 rpm for sixteen 2 μL injections. ..

    Binding Assay:

    Article Title: Differential recognition of β-catenin and TRIP6 by MAGI1 PDZ6 and allosteric modulation by DLL1.
    Article Snippet: .. Isothermal titration calorimetry Binding of DLL1 to MAGI1 was characterized by isothermal titration calorimetry (ITC) using a MicroCal PEAQ-ITC calorimeter (Malvern Panalytical). ..

    Article Title: Psyllid glycine-rich antimicrobial peptides oligomerize to directly cleave zinc transporter ZnuA on the membranes of citrus Huanglongbing pathogen.
    Article Snippet: .. 1670 Isothermal titration calorimetry (ITC) assay 1671 The binding affinity of DcGrAMP1 to CLas ZnuA and their mutants was quantified 1672 by ITC using a MicroCal PEAQ-ITC system (Malvern Panalytical). ..

    Article Title: Stk1 is required for BlaR1-mediated broad-spectrum β-lactam resistance in epidemic-causing strains of Staphylococcus aureus.
    Article Snippet: %Inhibition = 100× 1 Rate Background Rateð Þ Maximum Rate Background Rateð Þ ð1Þ IC50 values anderrorswerederived from thenon-linear regression analysis of these % inhibition curves using GraphPad Prism. .. Isothermal Titration Calorimetry binding data of Stk1 KD and GWX inhibitor Isothermal titration calorimetry (ITC) measurements were performed using a MicroCal PEAQ-ITC instrument (Malvern) at 25 °C in highfeedback mode with a stirring speed of 750 rpm for sixteen 2 μL injections. ..

    Titration:

    Article Title: Genome-directed discovery of an octalin-containing polyether ionophore improves diabetic skin wound healing.
    Article Snippet: .. ITC experiments were performed using a PEAQ-ITC titration calorimeter (MicroCal). ..



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    Malvern Panalytical origin 7 itc software package
    Interaction of LYP with F-BAR dimers. A , B HEK293 cells were transfected with PSTPIP1 F-BAR dimers in 3xmyc plasmid, as indicated in the top of the panels, and with 3xFLAG-LYP. Lysates were immunoprecipitated with myc Ab and LYP bound to PSTPIP1 was detected by IB with Ab for LYP. Expression of the proteins was verified by IB in total lysates (TL) with the same Abs. C Determination of the interaction stoichiometry by titration of fluorescein-LYP-CTH (1 µM) with the F-BAR of PSTPIP1 (residues 1–289) using fluorescence anisotropy. The stoichiometry ( N ) was determined from the intersection of asymptotic lines in the linear ascending and saturation (i.e. plateau) regions. D <t>ITC</t> analysis of LYP binding to PSTPIP1. Upper panel, heat exchange of the dilution of the unlabeled LYP-CTH peptide in buffer 20 mM sodium phosphate (pH 7.5), 150 mM NaCl, 5% (v/v) DMSO (upper trace) and representative thermogram of the binding of LYP-CTH to the F-BAR of PSTPIP1 (lower trace). Lower panel, LYP binding isotherm to PSTPIP1. The red line is the fit of a one binding site model to the heat changes of the interaction after subtracting the heat change of the dilution of LYP in buffer. The reported values of N , k d , and binding enthalpy (Δ H ) are the means ± standard deviations of three independent experiments
    Origin 7 Itc Software Package, supplied by Malvern Panalytical, 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/origin+7+software+package/PEAQ-ITC/pmc08840930-94-5-10
    Average 99 stars, based on 1 article reviews
    origin 7 itc software package - by Bioz Stars, 2026-11
    99/100 stars
      Buy from Supplier

    Image Search Results


    Interaction of LYP with F-BAR dimers. A , B HEK293 cells were transfected with PSTPIP1 F-BAR dimers in 3xmyc plasmid, as indicated in the top of the panels, and with 3xFLAG-LYP. Lysates were immunoprecipitated with myc Ab and LYP bound to PSTPIP1 was detected by IB with Ab for LYP. Expression of the proteins was verified by IB in total lysates (TL) with the same Abs. C Determination of the interaction stoichiometry by titration of fluorescein-LYP-CTH (1 µM) with the F-BAR of PSTPIP1 (residues 1–289) using fluorescence anisotropy. The stoichiometry ( N ) was determined from the intersection of asymptotic lines in the linear ascending and saturation (i.e. plateau) regions. D ITC analysis of LYP binding to PSTPIP1. Upper panel, heat exchange of the dilution of the unlabeled LYP-CTH peptide in buffer 20 mM sodium phosphate (pH 7.5), 150 mM NaCl, 5% (v/v) DMSO (upper trace) and representative thermogram of the binding of LYP-CTH to the F-BAR of PSTPIP1 (lower trace). Lower panel, LYP binding isotherm to PSTPIP1. The red line is the fit of a one binding site model to the heat changes of the interaction after subtracting the heat change of the dilution of LYP in buffer. The reported values of N , k d , and binding enthalpy (Δ H ) are the means ± standard deviations of three independent experiments

    Journal: Cellular and Molecular Life Sciences

    Article Title: PSTPIP1-LYP phosphatase interaction: structural basis and implications for autoinflammatory disorders

    doi: 10.1007/s00018-022-04173-w

    Figure Lengend Snippet: Interaction of LYP with F-BAR dimers. A , B HEK293 cells were transfected with PSTPIP1 F-BAR dimers in 3xmyc plasmid, as indicated in the top of the panels, and with 3xFLAG-LYP. Lysates were immunoprecipitated with myc Ab and LYP bound to PSTPIP1 was detected by IB with Ab for LYP. Expression of the proteins was verified by IB in total lysates (TL) with the same Abs. C Determination of the interaction stoichiometry by titration of fluorescein-LYP-CTH (1 µM) with the F-BAR of PSTPIP1 (residues 1–289) using fluorescence anisotropy. The stoichiometry ( N ) was determined from the intersection of asymptotic lines in the linear ascending and saturation (i.e. plateau) regions. D ITC analysis of LYP binding to PSTPIP1. Upper panel, heat exchange of the dilution of the unlabeled LYP-CTH peptide in buffer 20 mM sodium phosphate (pH 7.5), 150 mM NaCl, 5% (v/v) DMSO (upper trace) and representative thermogram of the binding of LYP-CTH to the F-BAR of PSTPIP1 (lower trace). Lower panel, LYP binding isotherm to PSTPIP1. The red line is the fit of a one binding site model to the heat changes of the interaction after subtracting the heat change of the dilution of LYP in buffer. The reported values of N , k d , and binding enthalpy (Δ H ) are the means ± standard deviations of three independent experiments

    Article Snippet: Data were analyzed using the Origin 7 ITC software package (MicroCal Software, Northampton, MA, USA), corrected by the heat of injection calculated from the basal heat remaining after saturation and confirmed by titration into buffer only as control.

    Techniques: Transfection, Plasmid Preparation, Immunoprecipitation, Expressing, Titration, Fluorescence, Binding Assay