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imagequant software version 5 2  (Molecular Dynamics Inc)

 
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    Molecular Dynamics Inc imagequant software version 5 2
    Imagequant Software Version 5 2, supplied by Molecular Dynamics Inc, used in various techniques. Bioz Stars score: 86/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/product/imagequant+software+version+5%C2%B72/imagequant+software/pmc11012841-164-36-40
    Average 86 stars, based on 1 article reviews
    imagequant software version 5 2 - by Bioz Stars, 2026-10
    86/100 stars

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    Article Title: Cardiac and kidney hormones cure up to 86% of human small-cell lung cancers in mice.
    Article Snippet: Background Four cardiac hormones synthesized by the same gene, i.e. atrial natriuretic peptide, vessel dilator, long acting natriuretic peptide and kaliuretic peptide, and the kidney hormone urodilatin have anticancer effects in vitro.. Materials and Methods These cardiac hormones and urodilatin were infused subcutaneously for 28 days with weekly fresh hormones since they lose biological effects at body temperature for more than a week at 0·3 nM kg body weight in athymic mice bearing human small-cell lung carcinomas.. Results Long acting natriuretic peptide, vessel dilator, kaliuretic peptide, atrial natriuretic peptide and urodilatin eliminated 86%, 71%, 57%, 43% (P < 0·001 for the cardiac hormones) and 25% (P < 0·05; urodilatin) of the human small-cell lung carcinomas.

    Software:

    Article Title: Cardiac and kidney hormones cure up to 86% of human small-cell lung cancers in mice.
    Article Snippet: Background Four cardiac hormones synthesized by the same gene, i.e. atrial natriuretic peptide, vessel dilator, long acting natriuretic peptide and kaliuretic peptide, and the kidney hormone urodilatin have anticancer effects in vitro.. Materials and Methods These cardiac hormones and urodilatin were infused subcutaneously for 28 days with weekly fresh hormones since they lose biological effects at body temperature for more than a week at 0·3 nM kg body weight in athymic mice bearing human small-cell lung carcinomas.. Results Long acting natriuretic peptide, vessel dilator, kaliuretic peptide, atrial natriuretic peptide and urodilatin eliminated 86%, 71%, 57%, 43% (P < 0·001 for the cardiac hormones) and 25% (P < 0·05; urodilatin) of the human small-cell lung carcinomas.



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    Image Search Results


    IL-2 promoter DNA binding of modified NF- κ Bs expressed in a cell-free E. coli protein biosynthesizing system following treatment with a cytoplasmic lysate from activated Jurkat cells in the presence of GTP. The relative intensities were determined using ImageQuant version 5.2 software (Molecular Dynamics) on the basis of the 32 P signal. The value of the band for wild-type NF- κ B in the presence of GTP was defined as 100%. (A) IL-2 promoter DNA binding with NF- κ Bs depends on the presence of GTP and cytoplasmic lysate. Lanes 1–3, wild-type NF- κ B; lanes 4–15, modified NF- κ Bs having p50 subunits with pTyr at respective positions 44, 60, 82, or 90. (B) Comparison of IL-2 promoter DNA binding ability to wild-type and modified NF- κ Bs. Controls included wild-type NF- κ B in the absence and presence of GTP (lanes 1 and 2), and NF κ Bs containing modified p50 subunits with pTyr at positions 44, 60, 82, or 90 (lanes 3, 4, 5, and 6, respectively). The statistical significance was determined using the Student’s t -test: wild-type vs pTyr44-p50, p > 0.05; wild-type vs pTyr60-p50, p < 0.001; wild-type vs pTyr82-p50, p < 0.001; and wild-type vs pTyr90-p50, p < 0.001.

    Journal: ACS chemical biology

    Article Title: Site-Selective Tyrosine Phosphorylation in the Activation of the p50 Subunit of NF- κ B for DNA Binding and Transcription

    doi: 10.1021/acschembio.2c00678

    Figure Lengend Snippet: IL-2 promoter DNA binding of modified NF- κ Bs expressed in a cell-free E. coli protein biosynthesizing system following treatment with a cytoplasmic lysate from activated Jurkat cells in the presence of GTP. The relative intensities were determined using ImageQuant version 5.2 software (Molecular Dynamics) on the basis of the 32 P signal. The value of the band for wild-type NF- κ B in the presence of GTP was defined as 100%. (A) IL-2 promoter DNA binding with NF- κ Bs depends on the presence of GTP and cytoplasmic lysate. Lanes 1–3, wild-type NF- κ B; lanes 4–15, modified NF- κ Bs having p50 subunits with pTyr at respective positions 44, 60, 82, or 90. (B) Comparison of IL-2 promoter DNA binding ability to wild-type and modified NF- κ Bs. Controls included wild-type NF- κ B in the absence and presence of GTP (lanes 1 and 2), and NF κ Bs containing modified p50 subunits with pTyr at positions 44, 60, 82, or 90 (lanes 3, 4, 5, and 6, respectively). The statistical significance was determined using the Student’s t -test: wild-type vs pTyr44-p50, p > 0.05; wild-type vs pTyr60-p50, p < 0.001; wild-type vs pTyr82-p50, p < 0.001; and wild-type vs pTyr90-p50, p < 0.001.

    Article Snippet: The relative intensities were determined using ImageQuant version 5.2 software (Molecular Dynamics) on the basis of the 32 P signal.

    Techniques: Binding Assay, Modification, Software, Comparison

    IL-2 promoter DNA binding of modified p50s expressed in a cell-free E. coli protein biosynthesizing system following treatment with a cytoplasmic lysate from activated Jurkat cells in the presence of GTP. Sample analysis was achieved by 5% native polyacrylamide gel electrophoresis (PAGE, 100 V for 1 h). Relative intensities were determined using ImageQuant software (version 5.2, Molecular Dynamics) on the basis of the 32 P signal. The band for wild-type NF- κ B in the presence of GTP was defined as 100%. Lane 1, wild-type p50; lanes 2–5, altered p50 subunits with pTyr at respective positions 44, 60, 82, or 90. Statistical significance was calculated with the Student’s t -test: p > 0.05 for all proteins.

    Journal: ACS chemical biology

    Article Title: Site-Selective Tyrosine Phosphorylation in the Activation of the p50 Subunit of NF- κ B for DNA Binding and Transcription

    doi: 10.1021/acschembio.2c00678

    Figure Lengend Snippet: IL-2 promoter DNA binding of modified p50s expressed in a cell-free E. coli protein biosynthesizing system following treatment with a cytoplasmic lysate from activated Jurkat cells in the presence of GTP. Sample analysis was achieved by 5% native polyacrylamide gel electrophoresis (PAGE, 100 V for 1 h). Relative intensities were determined using ImageQuant software (version 5.2, Molecular Dynamics) on the basis of the 32 P signal. The band for wild-type NF- κ B in the presence of GTP was defined as 100%. Lane 1, wild-type p50; lanes 2–5, altered p50 subunits with pTyr at respective positions 44, 60, 82, or 90. Statistical significance was calculated with the Student’s t -test: p > 0.05 for all proteins.

    Article Snippet: The relative intensities were determined using ImageQuant version 5.2 software (Molecular Dynamics) on the basis of the 32 P signal.

    Techniques: Binding Assay, Modification, Polyacrylamide Gel Electrophoresis, Software

    Phosphorylation of wild-type p50 (A) and modified p50 (containing pTyr60) (B) in the presence of Jurkat cell lysate. The results were analyzed by 15% sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE). The relative intensities were determined using ImageQuant software (version 5.2, Molecular Dynamics) based on the 32 P signal. 0 min: no Jurkat cell lysate was added; 0.5–60 min after Jurkat cell lysate addition. (C) Time-dependent phosphorylation of the wild-type and modified p50s in the presence of cell lysate from activated Jurkat cells. The band at 30 or 60 min was defined as 100%.

    Journal: ACS chemical biology

    Article Title: Site-Selective Tyrosine Phosphorylation in the Activation of the p50 Subunit of NF- κ B for DNA Binding and Transcription

    doi: 10.1021/acschembio.2c00678

    Figure Lengend Snippet: Phosphorylation of wild-type p50 (A) and modified p50 (containing pTyr60) (B) in the presence of Jurkat cell lysate. The results were analyzed by 15% sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE). The relative intensities were determined using ImageQuant software (version 5.2, Molecular Dynamics) based on the 32 P signal. 0 min: no Jurkat cell lysate was added; 0.5–60 min after Jurkat cell lysate addition. (C) Time-dependent phosphorylation of the wild-type and modified p50s in the presence of cell lysate from activated Jurkat cells. The band at 30 or 60 min was defined as 100%.

    Article Snippet: The relative intensities were determined using ImageQuant version 5.2 software (Molecular Dynamics) on the basis of the 32 P signal.

    Techniques: Phospho-proteomics, Modification, Polyacrylamide Gel Electrophoresis, SDS Page, Software