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physiological buffer  (Malvern Panalytical)


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    Malvern Panalytical physiological buffer
    Physiological Buffer, supplied by Malvern Panalytical, used in various techniques. Bioz Stars score: 99/100, based on 16247 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/product/itc+buffer/PEAQ-ITC/pmc11849797-159-9-13
    Average 99 stars, based on 16247 article reviews
    physiological buffer - by Bioz Stars, 2026-10
    99/100 stars

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    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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    ( a ) Characterisation of BRD4 mutants that disrupt binding to CDK9-cyclin T1. Mutation of residues Gln1350, Leu1354 and Phe1357, highlighted by the FragLite map and AlphaFold3 model disrupt BRD4 binding to CDK9-Cyclin T1. ( b ) Mutation of BRD4 residues Leu1354 and Phe1357, leads to a loss of BRD4 binding to CDK9-cyclin T2 in a fluorescence polarisation (FP) assay. ( c ) The cyclin T1 Tyr175Ala mutation reduces the Homogenous Time-Resolved Fluorescence (HTRF) signal, whereas the Trp210Ala mutation, previously identified as important for AFF4 interaction and adjacent to Tyr175, shows signals comparable to wild-type. ( d-g ) <t>Isothermal</t> <t>Titration</t> <t>Calorimetry</t> <t>(ITC)</t> plots of CDK9-cyclin T2 complexes with BRD4. Representative titration plots for (d) CDK9-cyclin T2 (e) CDK9-cyclin T2 Tyr174Ala, (f) CDK9-cyclin T2 Phe175Ala (negative control), and (g) CDK9-cyclin T2 Trp206Ala vs the BRD4 P-TEFb Interaction Domain (PID). The top panels show the raw heat signal, and the bottom panels show the integrated heat per injection fitted to a single-site binding model. HTRF experiments were carried out in triplicate and repeated on three separate days. The error bars indicate SD. FP experiments were carried out in triplicate and repeated on three separate days. ITC thermodynamic parameters (K d ) were derived from three independent biological replicates. Derived K d values are compiled in . Related to and Supplementary Figure 11.
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    ( a ) Characterisation of BRD4 mutants that disrupt binding to CDK9-cyclin T1. Mutation of residues Gln1350, Leu1354 and Phe1357, highlighted by the FragLite map and AlphaFold3 model disrupt BRD4 binding to CDK9-Cyclin T1. ( b ) Mutation of BRD4 residues Leu1354 and Phe1357, leads to a loss of BRD4 binding to CDK9-cyclin T2 in a fluorescence polarisation (FP) assay. ( c ) The cyclin T1 Tyr175Ala mutation reduces the Homogenous Time-Resolved Fluorescence (HTRF) signal, whereas the Trp210Ala mutation, previously identified as important for AFF4 interaction and adjacent to Tyr175, shows signals comparable to wild-type. ( d-g ) <t>Isothermal</t> <t>Titration</t> <t>Calorimetry</t> <t>(ITC)</t> plots of CDK9-cyclin T2 complexes with BRD4. Representative titration plots for (d) CDK9-cyclin T2 (e) CDK9-cyclin T2 Tyr174Ala, (f) CDK9-cyclin T2 Phe175Ala (negative control), and (g) CDK9-cyclin T2 Trp206Ala vs the BRD4 P-TEFb Interaction Domain (PID). The top panels show the raw heat signal, and the bottom panels show the integrated heat per injection fitted to a single-site binding model. HTRF experiments were carried out in triplicate and repeated on three separate days. The error bars indicate SD. FP experiments were carried out in triplicate and repeated on three separate days. ITC thermodynamic parameters (K d ) were derived from three independent biological replicates. Derived K d values are compiled in . Related to and Supplementary Figure 11.
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    ( a ) Characterisation of BRD4 mutants that disrupt binding to CDK9-cyclin T1. Mutation of residues Gln1350, Leu1354 and Phe1357, highlighted by the FragLite map and AlphaFold3 model disrupt BRD4 binding to CDK9-Cyclin T1. ( b ) Mutation of BRD4 residues Leu1354 and Phe1357, leads to a loss of BRD4 binding to CDK9-cyclin T2 in a fluorescence polarisation (FP) assay. ( c ) The cyclin T1 Tyr175Ala mutation reduces the Homogenous Time-Resolved Fluorescence (HTRF) signal, whereas the Trp210Ala mutation, previously identified as important for AFF4 interaction and adjacent to Tyr175, shows signals comparable to wild-type. ( d-g ) Isothermal Titration Calorimetry (ITC) plots of CDK9-cyclin T2 complexes with BRD4. Representative titration plots for (d) CDK9-cyclin T2 (e) CDK9-cyclin T2 Tyr174Ala, (f) CDK9-cyclin T2 Phe175Ala (negative control), and (g) CDK9-cyclin T2 Trp206Ala vs the BRD4 P-TEFb Interaction Domain (PID). The top panels show the raw heat signal, and the bottom panels show the integrated heat per injection fitted to a single-site binding model. HTRF experiments were carried out in triplicate and repeated on three separate days. The error bars indicate SD. FP experiments were carried out in triplicate and repeated on three separate days. ITC thermodynamic parameters (K d ) were derived from three independent biological replicates. Derived K d values are compiled in . Related to and Supplementary Figure 11.

    Journal: bioRxiv

    Article Title: FragLite mapping to identify the BRD4 recruitment site of P-TEFb

    doi: 10.64898/2026.04.09.717428

    Figure Lengend Snippet: ( a ) Characterisation of BRD4 mutants that disrupt binding to CDK9-cyclin T1. Mutation of residues Gln1350, Leu1354 and Phe1357, highlighted by the FragLite map and AlphaFold3 model disrupt BRD4 binding to CDK9-Cyclin T1. ( b ) Mutation of BRD4 residues Leu1354 and Phe1357, leads to a loss of BRD4 binding to CDK9-cyclin T2 in a fluorescence polarisation (FP) assay. ( c ) The cyclin T1 Tyr175Ala mutation reduces the Homogenous Time-Resolved Fluorescence (HTRF) signal, whereas the Trp210Ala mutation, previously identified as important for AFF4 interaction and adjacent to Tyr175, shows signals comparable to wild-type. ( d-g ) Isothermal Titration Calorimetry (ITC) plots of CDK9-cyclin T2 complexes with BRD4. Representative titration plots for (d) CDK9-cyclin T2 (e) CDK9-cyclin T2 Tyr174Ala, (f) CDK9-cyclin T2 Phe175Ala (negative control), and (g) CDK9-cyclin T2 Trp206Ala vs the BRD4 P-TEFb Interaction Domain (PID). The top panels show the raw heat signal, and the bottom panels show the integrated heat per injection fitted to a single-site binding model. HTRF experiments were carried out in triplicate and repeated on three separate days. The error bars indicate SD. FP experiments were carried out in triplicate and repeated on three separate days. ITC thermodynamic parameters (K d ) were derived from three independent biological replicates. Derived K d values are compiled in . Related to and Supplementary Figure 11.

    Article Snippet: CDK9-cyclin T2 was buffer exchanged using a HiTrap desalting column (5 mL) (Cytiva) into ITC buffer (50 mM HEPES, 300 mM NaCl, 0.5 mM TCEP, pH 7.4) and protein concentration was then determined using a Nanodrop 2000 at an absorbance of 280 nm with sequence derived extinction coefficients ( http://web.expasy.org/ protparam/).

    Techniques: Binding Assay, Mutagenesis, Fluorescence, FP Assay, Isothermal Titration Calorimetry, Titration, Negative Control, Injection, Derivative Assay