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troponin  (R&D Systems)


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    Structured Review

    R&D Systems troponin
    Troponin, supplied by R&D Systems, used in various techniques. Bioz Stars score: 91/100, based on 6 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/product/peptide+substrate+ac+arg+gly/Ac-Arg-Gly-Lys(Ac)-AMC+Fluorogenic+Peptide+Substrate/ppr0660541-7-32-44
    Average 91 stars, based on 6 article reviews
    troponin - by Bioz Stars, 2026-09
    91/100 stars

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    Related Articles

    Incubation:

    Article Title: A ribose-functionalized NAD + with unexpected high activity and selectivity for protein poly-ADP-ribosylation
    Article Snippet: .. 0.5 mM NAD + or 6 was incubated with 0.25 mM acetylated peptide substrate Ac-Arg-Gly-Lys(Ac)-AMC (R&D System, MN) and 45.4 nM recombinant human SIRT2 (R&D System, MN) in buffer containing 25 mM Tris pH 8.0, 150 mM NaCl, 1 mM DTT for overnight at room temperature. ..

    Article Title: A ribose-functionalized NAD + with unexpected high activity and selectivity for protein poly-ADP-ribosylation.
    Article Snippet: .. 0.5mM NAD+ or 6 was incubated with 0.25 mM acetylated peptide substrate Ac-Arg-Gly-Lys(Ac)-AMC (R&D System, MN) and 45.4 nM recombinant human SIRT2 (R&D System, MN) in buffer containing 25mM Tris pH 8.0, 150mM NaCl, 1 mM DTT for overnight at room temperature. ..

    Recombinant:

    Article Title: A ribose-functionalized NAD + with unexpected high activity and selectivity for protein poly-ADP-ribosylation
    Article Snippet: .. 0.5 mM NAD + or 6 was incubated with 0.25 mM acetylated peptide substrate Ac-Arg-Gly-Lys(Ac)-AMC (R&D System, MN) and 45.4 nM recombinant human SIRT2 (R&D System, MN) in buffer containing 25 mM Tris pH 8.0, 150 mM NaCl, 1 mM DTT for overnight at room temperature. ..

    Article Title: A ribose-functionalized NAD + with unexpected high activity and selectivity for protein poly-ADP-ribosylation.
    Article Snippet: .. 0.5mM NAD+ or 6 was incubated with 0.25 mM acetylated peptide substrate Ac-Arg-Gly-Lys(Ac)-AMC (R&D System, MN) and 45.4 nM recombinant human SIRT2 (R&D System, MN) in buffer containing 25mM Tris pH 8.0, 150mM NaCl, 1 mM DTT for overnight at room temperature. ..



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    the fluorogenic peptide substrate for pseudo-cath-d (m2295: ac-glu-asp(edans)-lys-pro-ile-leu-phe-phe-arg-leu-gly-lys(dabcyl)-glu-nh2) - by Bioz Stars, 2026-09
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    (A) Superposition of human <t>HDAC(1-11)</t> structures showing conserved aromatic side chains in active site. Average distance between two side chain is labeled. PDB IDs are 4BKX, 4LXZ, 4A69, 2VQJ, 5EDU, 3C0Y, 1T64 for human HDAC 1-4, 6-8. HDAC5 and 9-11 are AlphaFold-predicted models. The representative SAHA (white) is from an HDAC2 co-crystal structure (PDB ID 4LXZ). (B) Superposition of the top poses of docked PTERi (yellow) in sPTER and docked SAHA in sPTER, and SAHA from an HDAC2 co-crystal structure (PDB ID 4LXZ). Superposition is based on the top-ranked SAHA pose in sPTER and SAHA pose in HDAC2. SAHA poses are not shown for simplicity. Side chains of sPTER are shown in purple, while side chains of HDAC2 are shown in white. (C) Chemical structure of PTERi. (D) Dose-response inhibition of PTER activity by PTERi. (E) Heat map of dose-response inhibition for PTERi against the indicated recombinant enzyme. (F, G) Lineweaver-Burke plot (F) and dose-response inhibition of PTERi (G) in PTER activity assays. For (D-G) , PTER activity (N-acetyltaurine hydrolysis) was measured by quantifying taurine production using 200 ng of purified recombinant mouse PTER (mPTER, panels D-G ) or purified recombinant PTER from the indicated species (G) and 100 µM N-acetyltaurine for 1 h at 37°C. N=3/data point for (D,G) and N=1/data point for (E,F) . (D,G) are shown as mean ± SEM. IC 50 values for were determined from the dose-response curves via nonlinear regression analysis using GraphPad Prism.
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    Image Search Results


    (A) Superposition of human HDAC(1-11) structures showing conserved aromatic side chains in active site. Average distance between two side chain is labeled. PDB IDs are 4BKX, 4LXZ, 4A69, 2VQJ, 5EDU, 3C0Y, 1T64 for human HDAC 1-4, 6-8. HDAC5 and 9-11 are AlphaFold-predicted models. The representative SAHA (white) is from an HDAC2 co-crystal structure (PDB ID 4LXZ). (B) Superposition of the top poses of docked PTERi (yellow) in sPTER and docked SAHA in sPTER, and SAHA from an HDAC2 co-crystal structure (PDB ID 4LXZ). Superposition is based on the top-ranked SAHA pose in sPTER and SAHA pose in HDAC2. SAHA poses are not shown for simplicity. Side chains of sPTER are shown in purple, while side chains of HDAC2 are shown in white. (C) Chemical structure of PTERi. (D) Dose-response inhibition of PTER activity by PTERi. (E) Heat map of dose-response inhibition for PTERi against the indicated recombinant enzyme. (F, G) Lineweaver-Burke plot (F) and dose-response inhibition of PTERi (G) in PTER activity assays. For (D-G) , PTER activity (N-acetyltaurine hydrolysis) was measured by quantifying taurine production using 200 ng of purified recombinant mouse PTER (mPTER, panels D-G ) or purified recombinant PTER from the indicated species (G) and 100 µM N-acetyltaurine for 1 h at 37°C. N=3/data point for (D,G) and N=1/data point for (E,F) . (D,G) are shown as mean ± SEM. IC 50 values for were determined from the dose-response curves via nonlinear regression analysis using GraphPad Prism.

    Journal: bioRxiv

    Article Title: A small molecule PTER-selective inhibitor reduces food intake and body weight

    doi: 10.64898/2026.01.26.701829

    Figure Lengend Snippet: (A) Superposition of human HDAC(1-11) structures showing conserved aromatic side chains in active site. Average distance between two side chain is labeled. PDB IDs are 4BKX, 4LXZ, 4A69, 2VQJ, 5EDU, 3C0Y, 1T64 for human HDAC 1-4, 6-8. HDAC5 and 9-11 are AlphaFold-predicted models. The representative SAHA (white) is from an HDAC2 co-crystal structure (PDB ID 4LXZ). (B) Superposition of the top poses of docked PTERi (yellow) in sPTER and docked SAHA in sPTER, and SAHA from an HDAC2 co-crystal structure (PDB ID 4LXZ). Superposition is based on the top-ranked SAHA pose in sPTER and SAHA pose in HDAC2. SAHA poses are not shown for simplicity. Side chains of sPTER are shown in purple, while side chains of HDAC2 are shown in white. (C) Chemical structure of PTERi. (D) Dose-response inhibition of PTER activity by PTERi. (E) Heat map of dose-response inhibition for PTERi against the indicated recombinant enzyme. (F, G) Lineweaver-Burke plot (F) and dose-response inhibition of PTERi (G) in PTER activity assays. For (D-G) , PTER activity (N-acetyltaurine hydrolysis) was measured by quantifying taurine production using 200 ng of purified recombinant mouse PTER (mPTER, panels D-G ) or purified recombinant PTER from the indicated species (G) and 100 µM N-acetyltaurine for 1 h at 37°C. N=3/data point for (D,G) and N=1/data point for (E,F) . (D,G) are shown as mean ± SEM. IC 50 values for were determined from the dose-response curves via nonlinear regression analysis using GraphPad Prism.

    Article Snippet: The HDAC assay was performed in 50 μl reaction volume containing the HDAC reaction assay buffer, 600 μg of the liver lysate, 100 μM HDAC substrate peptide Ac-Arg-Gly-Lys-Ac-Glu-AMC (custom synthesized by Elim Biopharm), and 10 μM of indicated inhibitors.

    Techniques: Labeling, Inhibition, Activity Assay, Recombinant, Purification