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itc buffer containing 40–100 u -1 (rnasin, promega)  (Promega)

 
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    Promega itc buffer containing 40–100 u -1 (rnasin, promega)
    Itc Buffer Containing 40–100 U 1 (Rnasin, Promega), supplied by Promega, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/product/itc+buffer/itc+buffer+containing+40+100+u++1++rnasin++promega+/pmc06486635-70-19-20
    Average 90 stars, based on 1 article reviews
    itc buffer containing 40–100 u -1 (rnasin, promega) - by Bioz Stars, 2026-10
    90/100 stars

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    Related Articles

    Isothermal Titration Calorimetry:

    Article Title: IMP1 KH1 and KH2 domains create a structural platform with unique RNA recognition and re-modelling properties
    Article Snippet: The RNA was re-suspended in either nuclease-free water or ITC (isothermal titration calorimetry) buffer containing 40–100 u ml −1 (RNAsin, Promega) and the concentration determined by measuring absorbance at 260 nm and extinction coefficients calculated from the base composition of the sequence.

    Concentration Assay:

    Article Title: IMP1 KH1 and KH2 domains create a structural platform with unique RNA recognition and re-modelling properties
    Article Snippet: The RNA was re-suspended in either nuclease-free water or ITC (isothermal titration calorimetry) buffer containing 40–100 u ml −1 (RNAsin, Promega) and the concentration determined by measuring absorbance at 260 nm and extinction coefficients calculated from the base composition of the sequence.

    Sequencing:

    Article Title: IMP1 KH1 and KH2 domains create a structural platform with unique RNA recognition and re-modelling properties
    Article Snippet: The RNA was re-suspended in either nuclease-free water or ITC (isothermal titration calorimetry) buffer containing 40–100 u ml −1 (RNAsin, Promega) and the concentration determined by measuring absorbance at 260 nm and extinction coefficients calculated from the base composition of the sequence.

    Nuclear Magnetic Resonance:

    Article Title: IMP1 KH1 and KH2 domains create a structural platform with unique RNA recognition and re-modelling properties
    Article Snippet: The RNA was re-suspended in either nuclease-free water or ITC (isothermal titration calorimetry) buffer containing 40–100 u ml −1 (RNAsin, Promega) and the concentration determined by measuring absorbance at 260 nm and extinction coefficients calculated from the base composition of the sequence.



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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