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imagequant version 5 2 software  (Molecular Dynamics Inc)

 
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    Molecular Dynamics Inc imagequant version 5 2 software
    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.
    Imagequant Version 5 2 Software, 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+version+5+2+software/imagequant+software/pmc10026595-54-6-10
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    imagequant version 5 2 software - by Bioz Stars, 2026-10
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    Images

    1) Product Images from "Site-Selective Tyrosine Phosphorylation in the Activation of the p50 Subunit of NF- κ B for DNA Binding and Transcription"

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

    Journal: ACS chemical biology

    doi: 10.1021/acschembio.2c00678

    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.
    Figure Legend 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.

    Techniques Used: 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.
    Figure Legend 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.

    Techniques Used: 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%.
    Figure Legend 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%.

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

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    TUNEL Assay:

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    Staining:

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    Microscopy:

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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