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differential scanning fluorimetry instrument prometheus nt.48 nanodsf  (NanoTemper Technologies)

 
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    NanoTemper Technologies differential scanning fluorimetry instrument prometheus nt.48 nanodsf
    Differential Scanning Fluorimetry Instrument Prometheus Nt.48 Nanodsf, supplied by NanoTemper Technologies, 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/dsf+buffer/prometheus+nt+48/pm28383125-324-23-30
    Average 90 stars, based on 1 article reviews
    differential scanning fluorimetry instrument prometheus nt.48 nanodsf - by Bioz Stars, 2026-11
    90/100 stars

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    other:

    Article Title: Discovery of Small Molecules Against Foot-and-Mouth Disease Virus Replication by Targeting 2C Helicase Activity.
    Article Snippet: Purified 2C protein (2 mg/mL in 50 mM HEPES pH 7.5, 50 mM NaCl) was analyzed with a Prometheus NT.48 instrument (NanoTemper, Munich, Germany).

    Article Title: Molecular recording of cellular protein kinase activity with chemical labeling.
    Article Snippet: The protein thermostability was measured at 0.5 mg ml−1 in activity buffer using a nanoscale differential scanning fluorimeter (NanoDSF) Prometheus NT 48 device (NanoTemper Technologies).

    Article Title: Low nanomolar affinity to major grass pollen allergen Phl p 5 as achieved in an unmutated human antibody-lineage ancestor
    Article Snippet: Antibody thermal stability was assessed using Nano Differential Scanning Fluorimetry (NanoDSF, Prometheus (Nanotemper, Munich, Germany)).

    Article Title: The mechanistic basis for interprotomer deglycosylation of antibodies by corynebacterial IgG-specific endoglycosidases.
    Article Snippet: The sample was loaded into standard treated capillaries and measured in the Prometheus NT.48 instrument (NanoTemper, Munich, Germany).

    Article Title: Modifying recombinant purple acid phosphatase using computational design.
    Article Snippet: Thermal unfolding profiles were measured using a Nano-DSF (Prometheus NT.48, NanoTemper Technologies, Munich, Germany).

    Fluorescence:

    Article Title: Supporting Information Substrate Induced Movement of the Metal Cofactor between Active and Resting State
    Article Snippet: .. All experiments were done with Prometheus NT.48 (Nanotemper Technologies), between 15 and 95oC, with a temperature increase rate of 1oC/minute and at a fluorescence intensity of 50%. ..

    Article Title: Mechanistic insights into the allosteric regulation of cell wall hydrolase RipA in Mycobacterium tuberculosis
    Article Snippet: Two or three independent experiments were performed for Mt SteB and Mt RipA CAT , respectively; and Kd values were obtained from steady-state signal versus concentration curves fitted with GraphPad Prism 9 assuming a one-site binding model. .. Fluorescence measurements were carried out on the Prometheus NT.48 (NanoTemper Technologies) using standard-grade glass capillaries filled with 10–12 μl of Mt SteA or Cg SteA at 40 μM in 25 mM HEPES, pH 8, 500 mM NaCl and 5% glycerol. ..



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    (a) UNC10088 C -induced conformational change of the loop adjacent to C326. Structural overlay of the SCF FBXO22 -UNC10088 C -NSD2 PWWP1 model (dark gray) and the SCF FBXO22 -BACH1 BTB complex (light gray, PDB: 8UA3) , revealing the displacement of FBXO22 residues Y390. (b) Chemical structures of UNC8732 analogs that contain an aromatic aldehyde in place of the aliphatic amine of UNC8732. (c) Benzaldehyde derivatives UNC10415667 and UNC10415668 promote FBXO22-dependent ubiquitination of *NSD2 PWWP1 when added at 0.5 µM, based on fluorescent scanning of an SDS-PAGE gel. (d) Treatment of U2OS NSD2-HiBit cells with UNC10415667 (1 µM) for 6 hours resulted in a potent reduction of NSD2 levels by about 75%. A more modest effect was observed upon treatment with UNC10415668, and all other compounds had no significant effect. n ≥ 3 independent experiments. Error bars: standard error of the mean. (e) Treatment of U2OS NSD2 HiBit cells with UNC10415667 in a dose response fashion revealed a DC 50 value of 0.46 µM, which is about 2-fold more potent than UNC8732 and UNC10088. n = 3 independent experiments. Error bars: standard error of the mean. (f) UNC10415667 uses C326 to recruit NSD2 to the FBXO22 FIST domain as monitored by size-exclusion chromatography. Chromatograms of different elution profiles between mixtures of WT FBXO22 FIST or a C326A mutant with NSD2 and UNC10415667 (top). Representative Coomassie-stained SDS-PAGE gels of collected fractions. (g) <t>Differential</t> <t>scanning</t> <t>fluorimetry</t> <t>(DSF)</t> was used to monitor the stability of FBXO22 FIST wild type and variants in the presence of UNC10088 or UNC10415667 compared to DMSO, revealing that both compounds stabilize WT FBXO22 FIST and the C326 single cysteine variant (C326 only) as evidenced by an increase in melting temperature (ΔT m ), but not the C326A mutant. n = 3 independent experiments. Error bars: standard error of the mean.
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    (a) UNC10088 C -induced conformational change of the loop adjacent to C326. Structural overlay of the SCF FBXO22 -UNC10088 C -NSD2 PWWP1 model (dark gray) and the SCF FBXO22 -BACH1 BTB complex (light gray, PDB: 8UA3) , revealing the displacement of FBXO22 residues Y390. (b) Chemical structures of UNC8732 analogs that contain an aromatic aldehyde in place of the aliphatic amine of UNC8732. (c) Benzaldehyde derivatives UNC10415667 and UNC10415668 promote FBXO22-dependent ubiquitination of *NSD2 PWWP1 when added at 0.5 µM, based on fluorescent scanning of an SDS-PAGE gel. (d) Treatment of U2OS NSD2-HiBit cells with UNC10415667 (1 µM) for 6 hours resulted in a potent reduction of NSD2 levels by about 75%. A more modest effect was observed upon treatment with UNC10415668, and all other compounds had no significant effect. n ≥ 3 independent experiments. Error bars: standard error of the mean. (e) Treatment of U2OS NSD2 HiBit cells with UNC10415667 in a dose response fashion revealed a DC 50 value of 0.46 µM, which is about 2-fold more potent than UNC8732 and UNC10088. n = 3 independent experiments. Error bars: standard error of the mean. (f) UNC10415667 uses C326 to recruit NSD2 to the FBXO22 FIST domain as monitored by size-exclusion chromatography. Chromatograms of different elution profiles between mixtures of WT FBXO22 FIST or a C326A mutant with NSD2 and UNC10415667 (top). Representative Coomassie-stained SDS-PAGE gels of collected fractions. (g) <t>Differential</t> <t>scanning</t> <t>fluorimetry</t> <t>(DSF)</t> was used to monitor the stability of FBXO22 FIST wild type and variants in the presence of UNC10088 or UNC10415667 compared to DMSO, revealing that both compounds stabilize WT FBXO22 FIST and the C326 single cysteine variant (C326 only) as evidenced by an increase in melting temperature (ΔT m ), but not the C326A mutant. n = 3 independent experiments. Error bars: standard error of the mean.
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    Image Search Results


    (a) UNC10088 C -induced conformational change of the loop adjacent to C326. Structural overlay of the SCF FBXO22 -UNC10088 C -NSD2 PWWP1 model (dark gray) and the SCF FBXO22 -BACH1 BTB complex (light gray, PDB: 8UA3) , revealing the displacement of FBXO22 residues Y390. (b) Chemical structures of UNC8732 analogs that contain an aromatic aldehyde in place of the aliphatic amine of UNC8732. (c) Benzaldehyde derivatives UNC10415667 and UNC10415668 promote FBXO22-dependent ubiquitination of *NSD2 PWWP1 when added at 0.5 µM, based on fluorescent scanning of an SDS-PAGE gel. (d) Treatment of U2OS NSD2-HiBit cells with UNC10415667 (1 µM) for 6 hours resulted in a potent reduction of NSD2 levels by about 75%. A more modest effect was observed upon treatment with UNC10415668, and all other compounds had no significant effect. n ≥ 3 independent experiments. Error bars: standard error of the mean. (e) Treatment of U2OS NSD2 HiBit cells with UNC10415667 in a dose response fashion revealed a DC 50 value of 0.46 µM, which is about 2-fold more potent than UNC8732 and UNC10088. n = 3 independent experiments. Error bars: standard error of the mean. (f) UNC10415667 uses C326 to recruit NSD2 to the FBXO22 FIST domain as monitored by size-exclusion chromatography. Chromatograms of different elution profiles between mixtures of WT FBXO22 FIST or a C326A mutant with NSD2 and UNC10415667 (top). Representative Coomassie-stained SDS-PAGE gels of collected fractions. (g) Differential scanning fluorimetry (DSF) was used to monitor the stability of FBXO22 FIST wild type and variants in the presence of UNC10088 or UNC10415667 compared to DMSO, revealing that both compounds stabilize WT FBXO22 FIST and the C326 single cysteine variant (C326 only) as evidenced by an increase in melting temperature (ΔT m ), but not the C326A mutant. n = 3 independent experiments. Error bars: standard error of the mean.

    Journal: bioRxiv

    Article Title: Structural basis of NSD2 degradation via targeted recruitment of SCF-FBXO22

    doi: 10.1101/2025.08.29.673087

    Figure Lengend Snippet: (a) UNC10088 C -induced conformational change of the loop adjacent to C326. Structural overlay of the SCF FBXO22 -UNC10088 C -NSD2 PWWP1 model (dark gray) and the SCF FBXO22 -BACH1 BTB complex (light gray, PDB: 8UA3) , revealing the displacement of FBXO22 residues Y390. (b) Chemical structures of UNC8732 analogs that contain an aromatic aldehyde in place of the aliphatic amine of UNC8732. (c) Benzaldehyde derivatives UNC10415667 and UNC10415668 promote FBXO22-dependent ubiquitination of *NSD2 PWWP1 when added at 0.5 µM, based on fluorescent scanning of an SDS-PAGE gel. (d) Treatment of U2OS NSD2-HiBit cells with UNC10415667 (1 µM) for 6 hours resulted in a potent reduction of NSD2 levels by about 75%. A more modest effect was observed upon treatment with UNC10415668, and all other compounds had no significant effect. n ≥ 3 independent experiments. Error bars: standard error of the mean. (e) Treatment of U2OS NSD2 HiBit cells with UNC10415667 in a dose response fashion revealed a DC 50 value of 0.46 µM, which is about 2-fold more potent than UNC8732 and UNC10088. n = 3 independent experiments. Error bars: standard error of the mean. (f) UNC10415667 uses C326 to recruit NSD2 to the FBXO22 FIST domain as monitored by size-exclusion chromatography. Chromatograms of different elution profiles between mixtures of WT FBXO22 FIST or a C326A mutant with NSD2 and UNC10415667 (top). Representative Coomassie-stained SDS-PAGE gels of collected fractions. (g) Differential scanning fluorimetry (DSF) was used to monitor the stability of FBXO22 FIST wild type and variants in the presence of UNC10088 or UNC10415667 compared to DMSO, revealing that both compounds stabilize WT FBXO22 FIST and the C326 single cysteine variant (C326 only) as evidenced by an increase in melting temperature (ΔT m ), but not the C326A mutant. n = 3 independent experiments. Error bars: standard error of the mean.

    Article Snippet: 9.5 μL of the master mix containing FBXO22 FIST WT or variants, SYPRO Orange Dye (Invitrogen), and DSF buffer (20 mM Tris 7.5, 150 mM NaCl, and 1 mM TCEP) were added to a 384-well qPCR plate (Genesee Scientific).

    Techniques: Ubiquitin Proteomics, SDS Page, Size-exclusion Chromatography, Mutagenesis, Staining, Variant Assay