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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 16230 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 16230 article reviews
    physiological buffer - by Bioz Stars, 2026-10
    99/100 stars

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    Related Articles

    other:

    Article Title: Thermogel-gated field-effect transistor biosensors based on micellar self-assembly for glucose sensing.
    Article Snippet: Hypothesis: Real-time and accurate glucose detection is essential for healthcare management.. Conventional enzymatic sensors are often limited by instability and complex fabrication, while non-enzymatic alternatives often lack sufficient selectivity.. Experiments: We develop a novel field-effect transistor biosensor (bio-FET) integrated with a thermo-responsive hydrogel for enzyme-free glucose sensing.

    Article Title: A non-canonical redox family protein regulates bacterial interaction machineries.
    Article Snippet: REAGENT or RESOURCE SOURCE IDENTIFIER pRB31 (amyE::Phyper-spankydzFBacillus-anthracis-spec) This study N/A pRB32 (amyE::Phyper-spankydzFBacillus-cereus-spec) This study N/A pRB33 (amyE::Phyper-spankydzFListeria-monocytogenes-spec) This study N/A pRB34 (amyE::Phyper-spankydzFClostridium-botulinum-spec) This study N/A pET28a (+) N/A Dipankar Chatterji’s Laboratory stock pET28a-ydzF (C-terminal His6 tag - GSS linker) This study N/A pET28a-ydzFK22A (C-terminal His6 tag - GSS linker) This study N/A pET28a-ydzFW23A (C-terminal His6 tag - GSS linker) This study N/A pET28a-ydzFF48A (C-terminal His6 tag - GSS linker) This study N/A pET28a-ydzFK22A-W23A-F48A (C-terminal His6 tag - GSS linker) This study N/A pET28a-ymdB (N-terminal His6 tag - GSS linker) This study N/A pET28a-ymdBΔMFFE (N-terminal His6 tag - GSS linker) This study N/A Software and algorithms GraphPad Prism v8.0 Dotmatics https://www.graphpad.com/ SnapGene Viewer v8.0 Dotmatics https://www.snapgene.com/ Adobe Illustrator v2020 Adobe Inc. https://www.adobe.com/ Proteome Discoverer v2.5 Thermo Fisher Scientific RRID:SCR_014477 PANTHER v19.0 Mi et al.61 https://pantherdb.org/ ImageJ v1.54p NIH https://imagej.net/ij/ PyMOL v3.1 Schrodinger, LLC https://www.pymol.org/ MEGA11 Tamura et al.62 https://www.megasoftware.net/ iTOL v7 Letunic and Bork63 https://itol.embl.de/ Anaconda Navigator v2.6.3 (Python, including Jupyter Notebook v7.2.2) Anaconda, Inc. https://www.anaconda.com/ Pandas v2.2.3 NumFOCUS, Inc. https://pandas.pydata.org/ Plotly Express (in Python) Plotly https://plotly.com/python/plotly-express/ CFX Maestro v2.3 Bio-Rad Cat#12013758 MicroCal PEAQ-ITC Analysis v1.41 Malvern Panalytical RRID:SCR_023795 Olympus cellSens Dimension v3.2 Evident Scientific RRID:SCR_014551 ÄKTA UNICORN 6.3 Cytiva Cat#29020927 ZEN (blue edition) ZEISS RRID:SCR_013672 SEDFIT v16.1 LDMA/NIBIB, NIH RRID:SCR_018365 SEDNTERP v3 Philo64 RRID:SCR_016253 Spectra Manager v2.08 JASCO RRID:SCR_020145 iMOSFLM v7.4 (Data Processing) Battye et al.65 https://www.ccp4.ac.uk/ AIMLESS (Data scaling) Evans66 https://www.ccp4.ac.uk/ Phaser (Molecular Replacement) McCoy et al.67 https://www.ccp4.ac.uk/ Parrot (Density Modification) Cowtan68 https://www.ccp4.ac.uk/ Refmac v5.8 (Refinement) Murshudov et al.69 https://www.ccp4.ac.uk/ (Continued on next page) Cell Reports 45, 118071, October 27, 2026 19

    Automated:

    Article Title: Role of PER-WDR5 interactions in the mammalian circadian clock
    Article Snippet: .. To determine the K D values for the interactions of PER2 1132-1252 and PER1 1013-1291 with either WDR5 22-334 or CRY1 1-496, and of RbBP5 with WDR5, ITC experiments were performed and analysed using a MicroCal PEAQ-ITC 1.41 Automated system (Malvern Panalytical, Malvern, UK). ..

    Isothermal Titration Calorimetry:

    Article Title: A dual-action bacteriophage protein Ped1 degrades DNA and blocks replication in Pseudomonas aeruginosa.
    Article Snippet: The target protein signal was detected using the ECL Plus reagent kit (Cytiva) according to the manufacturer’s instructions by a Tanon 5200 Image analysis system (Tanon Technologies). .. Isothermal titration calorimetry assay (ITC) The binding of Ped1 to DnaB was characterized by isothermal titration calorimetry using a MicroCal PEAQ-ITC instrument (Malvern Panalytical) at 25 °C with a reference power of 5. ..

    Binding Assay:

    Article Title: A dual-action bacteriophage protein Ped1 degrades DNA and blocks replication in Pseudomonas aeruginosa.
    Article Snippet: The target protein signal was detected using the ECL Plus reagent kit (Cytiva) according to the manufacturer’s instructions by a Tanon 5200 Image analysis system (Tanon Technologies). .. Isothermal titration calorimetry assay (ITC) The binding of Ped1 to DnaB was characterized by isothermal titration calorimetry using a MicroCal PEAQ-ITC instrument (Malvern Panalytical) at 25 °C with a reference power of 5. ..

    Article Title: Protective effect of unsaturated fatty acids against glycation-induced structural and functional alteration of albumin: Perspectives on diabetic nephropathy.
    Article Snippet: Diabetic nephropathy (DN) is the leading cause of end-stage renal disease, and the protein glycation pathway has a major role in DN pathogenesis.. Accumulation of advanced glycation end products (AGEs) upregulates the Receptor for Advanced Glycation End products (RAGE)-NF-κB pathway, leading to elevated oxidative stress and inflammation.. The present study aims to shed light on the anti-glycation mechanism of unsaturated fatty acids (UFAs), such as oleic acid (OA), linoleic acid (LA), and docosahexaenoic acid (DHA), on glycated human serum albumin (G. HSA) in an in vitro setup using multispectroscopic techniques and renal cellular studies with HEK293 cells.

    Control:

    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: 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.



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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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    ( 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