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buffer a itc  (Malvern Panalytical)


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    Malvern Panalytical buffer a itc
    Buffer A Itc, supplied by Malvern Panalytical, used in various techniques. Bioz Stars score: 99/100, based on 16191 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/product/buffer+a+itc/PEAQ-ITC/pm41211845-263-27-37
    Average 99 stars, based on 16191 article reviews
    buffer a itc - by Bioz Stars, 2026-09
    99/100 stars

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    Related Articles

    Injection:

    Article Title: Nerol as an anti-quorum sensing and therapeutic agent against Acinetobacter baumannii pneumonia
    Article Snippet: .. Injection intervals were set at 150 s, with equilibrium periods of 300 s. The standard Microcal pEAQ-ITC control software package outputs standard interaction enthalpy (ΔH) and Gibbs free energy (ΔG), while also providing the reaction stoichiometry (n) and binding affinity constant (Ka). ..

    Control:

    Article Title: Nerol as an anti-quorum sensing and therapeutic agent against Acinetobacter baumannii pneumonia
    Article Snippet: .. Injection intervals were set at 150 s, with equilibrium periods of 300 s. The standard Microcal pEAQ-ITC control software package outputs standard interaction enthalpy (ΔH) and Gibbs free energy (ΔG), while also providing the reaction stoichiometry (n) and binding affinity constant (Ka). ..

    Article Title: Nerol as an anti-quorum sensing and therapeutic agent against Acinetobacter baumannii pneumonia
    Article Snippet: The mass spectrometry proteomics data have been deposited to the ProteomeXchange Consortium ( https://proteomecentral.proteomexchange.org ) via the iProX partner repository , with the dataset identifier PXD073438. .. The interaction between Nerol and BfmS was determined at 25°C using a Malvern ITC system equipped with MicroCal PEAQ-ITC control software. .. The pET22b (+) plasmid containing the BfmS gene was transformed into E. coli BL21(DE3), with the target protein being overexpressed and purified by BGI Shenzhen.

    Software:

    Article Title: Nerol as an anti-quorum sensing and therapeutic agent against Acinetobacter baumannii pneumonia
    Article Snippet: .. Injection intervals were set at 150 s, with equilibrium periods of 300 s. The standard Microcal pEAQ-ITC control software package outputs standard interaction enthalpy (ΔH) and Gibbs free energy (ΔG), while also providing the reaction stoichiometry (n) and binding affinity constant (Ka). ..

    Article Title: Targeting Undruggable Protein Interactions with DNA Aptamers: Inhibition of the Interaction Between Yersinia Outer Protein M and Human DEAD-Box Helicase 3.
    Article Snippet: .. The data were analyzed using the PEAQ-ITC analysis software, version 1.41 (MicroCal–Malvern Panalytical) with the one-binding-site model. ..

    Article Title: Nerol as an anti-quorum sensing and therapeutic agent against Acinetobacter baumannii pneumonia
    Article Snippet: The mass spectrometry proteomics data have been deposited to the ProteomeXchange Consortium ( https://proteomecentral.proteomexchange.org ) via the iProX partner repository , with the dataset identifier PXD073438. .. The interaction between Nerol and BfmS was determined at 25°C using a Malvern ITC system equipped with MicroCal PEAQ-ITC control software. .. The pET22b (+) plasmid containing the BfmS gene was transformed into E. coli BL21(DE3), with the target protein being overexpressed and purified by BGI Shenzhen.

    Binding Assay:

    Article Title: Nerol as an anti-quorum sensing and therapeutic agent against Acinetobacter baumannii pneumonia
    Article Snippet: .. Injection intervals were set at 150 s, with equilibrium periods of 300 s. The standard Microcal pEAQ-ITC control software package outputs standard interaction enthalpy (ΔH) and Gibbs free energy (ΔG), while also providing the reaction stoichiometry (n) and binding affinity constant (Ka). ..

    Isothermal Titration Calorimetry:

    Article Title: Photothermal-Activated Antibacterial Amyloid-Polyphenol-Iron Hydrogels for Synergistic Wound Healing.
    Article Snippet: The ,2-Diphenyl-1-picrylhydrazyl (DPPH) scavenging activity was ested by Ultraviolet–visible absorption spectrum (UV–vis, Agient Technologies, USA) and calculated according to a previous rotocol [29]. .. Isothermal titration calorimetry (ITC) determiation was obtained using a MicroCal PEAQ-ITC instrument Malvern, UK). ..



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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 ) <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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    Image Search Results


    ( 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