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prometheusnt.48 dsf  (NanoTemper Technologies)

 
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    Structured Review

    NanoTemper Technologies prometheusnt.48 dsf
    (a) Left panel: A chromatogram showing streptactin-purified Huc separated via size exclusion chromatography on a Superose 6 10/300 column. The green highlighted region contains the Huc oligomer, while the pink region contains a low molecular weight Huc species. Right panel: A Coomassie-stained SDS-PAGE gel showing fractions from the coloured peak regions of the chromatogram. (b) A schematic of the Huc gene cluster showing the location of hucM (MSMEG_2261) compared to hucS and hucL . (c) A native-PAGE gel of the purified Huc oligomer (green) and low molecular species (pink), stained with Coomassie (left panel) and NBT (right panel). (d) <t>Differential</t> <t>scanning</t> <t>fluorimetry</t> analysis of the Huc oligomer showing a transition in tryptophan-derived fluorescence at 78.3 °C, indicating the melting temperature of the oligomer. (e) An NBT-stained native-PAGE gel of M. smegmatis cell lysate showing that Huc does not form an oligomer in the ΔhucM strain. (f) Gas chromatography analysis of the H 2 concentration of the headspace of sealed vials containing Huc, E. coli Hyd1 or no enzyme, showing Huc can oxidize H 2 from 100 ppm to the limit of detection for the gas chromatograph (40 ppbv) (green line). In contrast, Hyd1 does not oxidise H 2 < 8 ppmv. Data are presented as mean values +/− SD.
    Prometheusnt.48 Dsf, 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/prometheusnt%2E48+dsf/prometheusnt+48+dsf/pmc10017518-269-19-21
    Average 90 stars, based on 1 article reviews
    prometheusnt.48 dsf - by Bioz Stars, 2026-09
    90/100 stars

    Images

    1) Product Images from "Structural basis for bacterial energy extraction from atmospheric hydrogen"

    Article Title: Structural basis for bacterial energy extraction from atmospheric hydrogen

    Journal: Nature

    doi: 10.1038/s41586-023-05781-7

    (a) Left panel: A chromatogram showing streptactin-purified Huc separated via size exclusion chromatography on a Superose 6 10/300 column. The green highlighted region contains the Huc oligomer, while the pink region contains a low molecular weight Huc species. Right panel: A Coomassie-stained SDS-PAGE gel showing fractions from the coloured peak regions of the chromatogram. (b) A schematic of the Huc gene cluster showing the location of hucM (MSMEG_2261) compared to hucS and hucL . (c) A native-PAGE gel of the purified Huc oligomer (green) and low molecular species (pink), stained with Coomassie (left panel) and NBT (right panel). (d) Differential scanning fluorimetry analysis of the Huc oligomer showing a transition in tryptophan-derived fluorescence at 78.3 °C, indicating the melting temperature of the oligomer. (e) An NBT-stained native-PAGE gel of M. smegmatis cell lysate showing that Huc does not form an oligomer in the ΔhucM strain. (f) Gas chromatography analysis of the H 2 concentration of the headspace of sealed vials containing Huc, E. coli Hyd1 or no enzyme, showing Huc can oxidize H 2 from 100 ppm to the limit of detection for the gas chromatograph (40 ppbv) (green line). In contrast, Hyd1 does not oxidise H 2 < 8 ppmv. Data are presented as mean values +/− SD.
    Figure Legend Snippet: (a) Left panel: A chromatogram showing streptactin-purified Huc separated via size exclusion chromatography on a Superose 6 10/300 column. The green highlighted region contains the Huc oligomer, while the pink region contains a low molecular weight Huc species. Right panel: A Coomassie-stained SDS-PAGE gel showing fractions from the coloured peak regions of the chromatogram. (b) A schematic of the Huc gene cluster showing the location of hucM (MSMEG_2261) compared to hucS and hucL . (c) A native-PAGE gel of the purified Huc oligomer (green) and low molecular species (pink), stained with Coomassie (left panel) and NBT (right panel). (d) Differential scanning fluorimetry analysis of the Huc oligomer showing a transition in tryptophan-derived fluorescence at 78.3 °C, indicating the melting temperature of the oligomer. (e) An NBT-stained native-PAGE gel of M. smegmatis cell lysate showing that Huc does not form an oligomer in the ΔhucM strain. (f) Gas chromatography analysis of the H 2 concentration of the headspace of sealed vials containing Huc, E. coli Hyd1 or no enzyme, showing Huc can oxidize H 2 from 100 ppm to the limit of detection for the gas chromatograph (40 ppbv) (green line). In contrast, Hyd1 does not oxidise H 2 < 8 ppmv. Data are presented as mean values +/− SD.

    Techniques Used: Purification, Size-exclusion Chromatography, Molecular Weight, Staining, SDS Page, Clear Native PAGE, Derivative Assay, Fluorescence, Gas Chromatography, Concentration Assay

    Related Articles

    Purification:

    Article Title: Structural basis for bacterial energy extraction from atmospheric hydrogen
    Article Snippet: To determine the stability of the Huc complex, thermal melting was performed from 20 to 90 °C using a PrometheusNT.48 DSF (Nanotemper) using high sensitivity capillaries.

    Size-exclusion Chromatography:

    Article Title: Structural basis for bacterial energy extraction from atmospheric hydrogen
    Article Snippet: To determine the stability of the Huc complex, thermal melting was performed from 20 to 90 °C using a PrometheusNT.48 DSF (Nanotemper) using high sensitivity capillaries.

    Molecular Weight:

    Article Title: Structural basis for bacterial energy extraction from atmospheric hydrogen
    Article Snippet: To determine the stability of the Huc complex, thermal melting was performed from 20 to 90 °C using a PrometheusNT.48 DSF (Nanotemper) using high sensitivity capillaries.

    Staining:

    Article Title: Structural basis for bacterial energy extraction from atmospheric hydrogen
    Article Snippet: To determine the stability of the Huc complex, thermal melting was performed from 20 to 90 °C using a PrometheusNT.48 DSF (Nanotemper) using high sensitivity capillaries.

    SDS Page:

    Article Title: Structural basis for bacterial energy extraction from atmospheric hydrogen
    Article Snippet: To determine the stability of the Huc complex, thermal melting was performed from 20 to 90 °C using a PrometheusNT.48 DSF (Nanotemper) using high sensitivity capillaries.

    Clear Native PAGE:

    Article Title: Structural basis for bacterial energy extraction from atmospheric hydrogen
    Article Snippet: To determine the stability of the Huc complex, thermal melting was performed from 20 to 90 °C using a PrometheusNT.48 DSF (Nanotemper) using high sensitivity capillaries.

    Derivative Assay:

    Article Title: Structural basis for bacterial energy extraction from atmospheric hydrogen
    Article Snippet: To determine the stability of the Huc complex, thermal melting was performed from 20 to 90 °C using a PrometheusNT.48 DSF (Nanotemper) using high sensitivity capillaries.

    Fluorescence:

    Article Title: Structural basis for bacterial energy extraction from atmospheric hydrogen
    Article Snippet: To determine the stability of the Huc complex, thermal melting was performed from 20 to 90 °C using a PrometheusNT.48 DSF (Nanotemper) using high sensitivity capillaries.

    Gas Chromatography:

    Article Title: Structural basis for bacterial energy extraction from atmospheric hydrogen
    Article Snippet: To determine the stability of the Huc complex, thermal melting was performed from 20 to 90 °C using a PrometheusNT.48 DSF (Nanotemper) using high sensitivity capillaries.

    Concentration Assay:

    Article Title: Structural basis for bacterial energy extraction from atmospheric hydrogen
    Article Snippet: To determine the stability of the Huc complex, thermal melting was performed from 20 to 90 °C using a PrometheusNT.48 DSF (Nanotemper) using high sensitivity capillaries.



    Similar Products

    prometheusnt.48 dsf  (NanoTemper Technologies)
    90
    NanoTemper Technologies prometheusnt.48 dsf
    (a) Left panel: A chromatogram showing streptactin-purified Huc separated via size exclusion chromatography on a Superose 6 10/300 column. The green highlighted region contains the Huc oligomer, while the pink region contains a low molecular weight Huc species. Right panel: A Coomassie-stained SDS-PAGE gel showing fractions from the coloured peak regions of the chromatogram. (b) A schematic of the Huc gene cluster showing the location of hucM (MSMEG_2261) compared to hucS and hucL . (c) A native-PAGE gel of the purified Huc oligomer (green) and low molecular species (pink), stained with Coomassie (left panel) and NBT (right panel). (d) <t>Differential</t> <t>scanning</t> <t>fluorimetry</t> analysis of the Huc oligomer showing a transition in tryptophan-derived fluorescence at 78.3 °C, indicating the melting temperature of the oligomer. (e) An NBT-stained native-PAGE gel of M. smegmatis cell lysate showing that Huc does not form an oligomer in the ΔhucM strain. (f) Gas chromatography analysis of the H 2 concentration of the headspace of sealed vials containing Huc, E. coli Hyd1 or no enzyme, showing Huc can oxidize H 2 from 100 ppm to the limit of detection for the gas chromatograph (40 ppbv) (green line). In contrast, Hyd1 does not oxidise H 2 < 8 ppmv. Data are presented as mean values +/− SD.
    Prometheusnt.48 Dsf, 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/prometheusnt%2E48+dsf/prometheusnt+48+dsf/pmc10017518-269-19-21
    Average 90 stars, based on 1 article reviews
    prometheusnt.48 dsf - by Bioz Stars, 2026-09
    90/100 stars
    		  Buy from Supplier

    Image Search Results


    (a) Left panel: A chromatogram showing streptactin-purified Huc separated via size exclusion chromatography on a Superose 6 10/300 column. The green highlighted region contains the Huc oligomer, while the pink region contains a low molecular weight Huc species. Right panel: A Coomassie-stained SDS-PAGE gel showing fractions from the coloured peak regions of the chromatogram. (b) A schematic of the Huc gene cluster showing the location of hucM (MSMEG_2261) compared to hucS and hucL . (c) A native-PAGE gel of the purified Huc oligomer (green) and low molecular species (pink), stained with Coomassie (left panel) and NBT (right panel). (d) Differential scanning fluorimetry analysis of the Huc oligomer showing a transition in tryptophan-derived fluorescence at 78.3 °C, indicating the melting temperature of the oligomer. (e) An NBT-stained native-PAGE gel of M. smegmatis cell lysate showing that Huc does not form an oligomer in the ΔhucM strain. (f) Gas chromatography analysis of the H 2 concentration of the headspace of sealed vials containing Huc, E. coli Hyd1 or no enzyme, showing Huc can oxidize H 2 from 100 ppm to the limit of detection for the gas chromatograph (40 ppbv) (green line). In contrast, Hyd1 does not oxidise H 2 < 8 ppmv. Data are presented as mean values +/− SD.

    Journal: Nature

    Article Title: Structural basis for bacterial energy extraction from atmospheric hydrogen

    doi: 10.1038/s41586-023-05781-7

    Figure Lengend Snippet: (a) Left panel: A chromatogram showing streptactin-purified Huc separated via size exclusion chromatography on a Superose 6 10/300 column. The green highlighted region contains the Huc oligomer, while the pink region contains a low molecular weight Huc species. Right panel: A Coomassie-stained SDS-PAGE gel showing fractions from the coloured peak regions of the chromatogram. (b) A schematic of the Huc gene cluster showing the location of hucM (MSMEG_2261) compared to hucS and hucL . (c) A native-PAGE gel of the purified Huc oligomer (green) and low molecular species (pink), stained with Coomassie (left panel) and NBT (right panel). (d) Differential scanning fluorimetry analysis of the Huc oligomer showing a transition in tryptophan-derived fluorescence at 78.3 °C, indicating the melting temperature of the oligomer. (e) An NBT-stained native-PAGE gel of M. smegmatis cell lysate showing that Huc does not form an oligomer in the ΔhucM strain. (f) Gas chromatography analysis of the H 2 concentration of the headspace of sealed vials containing Huc, E. coli Hyd1 or no enzyme, showing Huc can oxidize H 2 from 100 ppm to the limit of detection for the gas chromatograph (40 ppbv) (green line). In contrast, Hyd1 does not oxidise H 2 < 8 ppmv. Data are presented as mean values +/− SD.

    Article Snippet: To determine the stability of the Huc complex, thermal melting was performed from 20 to 90 °C using a PrometheusNT.48 DSF (Nanotemper) using high sensitivity capillaries.

    Techniques: Purification, Size-exclusion Chromatography, Molecular Weight, Staining, SDS Page, Clear Native PAGE, Derivative Assay, Fluorescence, Gas Chromatography, Concentration Assay