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gel analysis program imagequant  (Molecular Dynamics Inc)

 
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    Molecular Dynamics Inc gel analysis program imagequant
    Fluorescence intensities of the N157C, E19C, and V309C proteins on the SDS-PAGE gel described in the legend to Fig. ​Fig.2.2. Intensity traces of the N157C and E19C protein lanes of the gel in Fig. ​Fig.22 were created with the gel analysis program <t>ImageQuant</t> from Molecular Dynamics. Fluorescence intensity is plotted versus distance from an arbitrary point near the leading edge of the gel; thus, bands on the gel moved from right to left. RbsC is at about 340 pixels.
    Gel Analysis Program Imagequant, supplied by Molecular Dynamics Inc, 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/gel+analysis+program+imagequant/pmc00181013-203-18-23?v=Molecular+Dynamics+Inc
    Average 90 stars, based on 1 article reviews
    gel analysis program imagequant - by Bioz Stars, 2026-07
    90/100 stars

    Images

    1) Product Images from "Topology of RbsC, the Membrane Component of the Escherichia coli Ribose Transporter † "

    Article Title: Topology of RbsC, the Membrane Component of the Escherichia coli Ribose Transporter †

    Journal:

    doi: 10.1128/JB.185.17.5234-5239.2003

    Fluorescence intensities of the N157C, E19C, and V309C proteins on the SDS-PAGE gel described in the legend to Fig. ​Fig.2.2. Intensity traces of the N157C and E19C protein lanes of the gel in Fig. ​Fig.22 were created with the gel analysis program ImageQuant from Molecular Dynamics. Fluorescence intensity is plotted versus distance from an arbitrary point near the leading edge of the gel; thus, bands on the gel moved from right to left. RbsC is at about 340 pixels.
    Figure Legend Snippet: Fluorescence intensities of the N157C, E19C, and V309C proteins on the SDS-PAGE gel described in the legend to Fig. ​Fig.2.2. Intensity traces of the N157C and E19C protein lanes of the gel in Fig. ​Fig.22 were created with the gel analysis program ImageQuant from Molecular Dynamics. Fluorescence intensity is plotted versus distance from an arbitrary point near the leading edge of the gel; thus, bands on the gel moved from right to left. RbsC is at about 340 pixels.

    Techniques Used: Fluorescence, SDS Page



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    Fluorescence intensities of the N157C, E19C, and V309C proteins on the SDS-PAGE gel described in the legend to Fig. ​Fig.2.2. Intensity traces of the N157C and E19C protein lanes of the gel in Fig. ​Fig.22 were created with the gel analysis program <t>ImageQuant</t> from Molecular Dynamics. Fluorescence intensity is plotted versus distance from an arbitrary point near the leading edge of the gel; thus, bands on the gel moved from right to left. RbsC is at about 340 pixels.
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    Average 90 stars, based on 1 article reviews
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    Image Search Results


    Fluorescence intensities of the N157C, E19C, and V309C proteins on the SDS-PAGE gel described in the legend to Fig. ​Fig.2.2. Intensity traces of the N157C and E19C protein lanes of the gel in Fig. ​Fig.22 were created with the gel analysis program ImageQuant from Molecular Dynamics. Fluorescence intensity is plotted versus distance from an arbitrary point near the leading edge of the gel; thus, bands on the gel moved from right to left. RbsC is at about 340 pixels.

    Journal:

    Article Title: Topology of RbsC, the Membrane Component of the Escherichia coli Ribose Transporter †

    doi: 10.1128/JB.185.17.5234-5239.2003

    Figure Lengend Snippet: Fluorescence intensities of the N157C, E19C, and V309C proteins on the SDS-PAGE gel described in the legend to Fig. ​Fig.2.2. Intensity traces of the N157C and E19C protein lanes of the gel in Fig. ​Fig.22 were created with the gel analysis program ImageQuant from Molecular Dynamics. Fluorescence intensity is plotted versus distance from an arbitrary point near the leading edge of the gel; thus, bands on the gel moved from right to left. RbsC is at about 340 pixels.

    Article Snippet: Intensity traces of the N157C and E19C protein lanes of the gel in Fig. were created with the gel analysis program ImageQuant from Molecular Dynamics.

    Techniques: Fluorescence, SDS Page