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imagequant software  (Molecular Dynamics Inc)
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Molecular Dynamics Inc imagequant software
A, Relative transcript levels for genes encoding mitochondrial ATP-dependent proteases in ftsh4-1 and ftsh4-2 mutants grown in LD at 22°C and LD at 30°C compared with wild-type (WT) plants. The relative abundance of transcripts is expressed as log2 ratios. Mean values ± sd from at least three independent experiments are shown. The dotted lines indicate cutoff values ± 0.5 (log2) of the ratio corresponding to the threshold levels for significant up- and down-regulation of the transcripts in ftsh4. B, Representative images of the immunodetection of selected mitochondrial proteases in the ftsh4-1 mutant compared with wild-type plants growing in LD at 22°C, LD at 30°C, or SD at 22°C. C, Densitometric quantification of immunoblots presented in B. The intensity of bands was estimated using <t>ImageQuant</t> software (Molecular Dynamics). Data for ftsh4-1 are expressed as percentages of the value for wild-type plants. Mean values ± sd from at least three experiments are shown. Significant differences in abundance between the wild type and the ftsh4-1 mutant are indicated by asterisks (one-sample Student’s t test; *, P < 0.05).
Imagequant 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
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A, Relative transcript levels for genes encoding mitochondrial ATP-dependent proteases in ftsh4-1 and ftsh4-2 mutants grown in LD at 22°C and LD at 30°C compared with wild-type (WT) plants. The relative abundance of transcripts is expressed as log2 ratios. Mean values ± sd from at least three independent experiments are shown. The dotted lines indicate cutoff values ± 0.5 (log2) of the ratio corresponding to the threshold levels for significant up- and down-regulation of the transcripts in ftsh4. B, Representative images of the immunodetection of selected mitochondrial proteases in the ftsh4-1 mutant compared with wild-type plants growing in LD at 22°C, LD at 30°C, or SD at 22°C. C, Densitometric quantification of immunoblots presented in B. The intensity of bands was estimated using ImageQuant software (Molecular Dynamics). Data for ftsh4-1 are expressed as percentages of the value for wild-type plants. Mean values ± sd from at least three experiments are shown. Significant differences in abundance between the wild type and the ftsh4-1 mutant are indicated by asterisks (one-sample Student’s t test; *, P < 0.05).

Journal: Plant Physiology

Article Title: Lack of FTSH4 Protease Affects Protein Carbonylation, Mitochondrial Morphology, and Phospholipid Content in Mitochondria of Arabidopsis: New Insights into a Complex Interplay 1

doi: 10.1104/pp.16.00370

Figure Lengend Snippet: A, Relative transcript levels for genes encoding mitochondrial ATP-dependent proteases in ftsh4-1 and ftsh4-2 mutants grown in LD at 22°C and LD at 30°C compared with wild-type (WT) plants. The relative abundance of transcripts is expressed as log2 ratios. Mean values ± sd from at least three independent experiments are shown. The dotted lines indicate cutoff values ± 0.5 (log2) of the ratio corresponding to the threshold levels for significant up- and down-regulation of the transcripts in ftsh4. B, Representative images of the immunodetection of selected mitochondrial proteases in the ftsh4-1 mutant compared with wild-type plants growing in LD at 22°C, LD at 30°C, or SD at 22°C. C, Densitometric quantification of immunoblots presented in B. The intensity of bands was estimated using ImageQuant software (Molecular Dynamics). Data for ftsh4-1 are expressed as percentages of the value for wild-type plants. Mean values ± sd from at least three experiments are shown. Significant differences in abundance between the wild type and the ftsh4-1 mutant are indicated by asterisks (one-sample Student’s t test; *, P < 0.05).

Article Snippet: The membranes were documented using a chemiluminescence imager (G-BOX ChemiXR5; Syngene), and the optical density of the bands was quantified using ImageQuant software (Molecular Dynamics).

Techniques: Immunodetection, Mutagenesis, Western Blot, Software

Amounts and activities of respiratory complexes (A–C) and the level of ATP (D) in ftsh4 and wild-type (WT) plants. Mitochondria were isolated from 3-week-old wild-type and mutant plants (ftsh4-1 and ftsh4-2) growing hydroponically in LD at 22°C and LD at 30°C. A and B, Coomassie Brilliant Blue (CBB) and in-gel activity staining of complex I (C I) and complex V (C V) after BN-PAGE. C, Quantification of the activities of complexes I and V. The intensity of bands was estimated by densitometric analysis using ImageQuant software (Molecular Dynamics). Relative complex activity from mutant mitochondria was calculated as a percentage of that in wild-type plants. Differences in activity between the wild type and mutants are in all cases statistically significant (one-sample Student’s t test; P < 0.05). Mean values ± sd from three experiments are shown. D, ATP contents in wild-type and ftsh4 mitochondria. Mitochondria were isolated from 3-week-old wild-type, ftsh4-1, and ftsh4-2 seedlings grown under LD at 30°C. The ATP concentration was determined as described in “Materials and Methods.” An unpaired Student’s t test was used to estimate the P values: *, P < 0.05. Error bars correspond to sd (n = 6).

Journal: Plant Physiology

Article Title: Lack of FTSH4 Protease Affects Protein Carbonylation, Mitochondrial Morphology, and Phospholipid Content in Mitochondria of Arabidopsis: New Insights into a Complex Interplay 1

doi: 10.1104/pp.16.00370

Figure Lengend Snippet: Amounts and activities of respiratory complexes (A–C) and the level of ATP (D) in ftsh4 and wild-type (WT) plants. Mitochondria were isolated from 3-week-old wild-type and mutant plants (ftsh4-1 and ftsh4-2) growing hydroponically in LD at 22°C and LD at 30°C. A and B, Coomassie Brilliant Blue (CBB) and in-gel activity staining of complex I (C I) and complex V (C V) after BN-PAGE. C, Quantification of the activities of complexes I and V. The intensity of bands was estimated by densitometric analysis using ImageQuant software (Molecular Dynamics). Relative complex activity from mutant mitochondria was calculated as a percentage of that in wild-type plants. Differences in activity between the wild type and mutants are in all cases statistically significant (one-sample Student’s t test; P < 0.05). Mean values ± sd from three experiments are shown. D, ATP contents in wild-type and ftsh4 mitochondria. Mitochondria were isolated from 3-week-old wild-type, ftsh4-1, and ftsh4-2 seedlings grown under LD at 30°C. The ATP concentration was determined as described in “Materials and Methods.” An unpaired Student’s t test was used to estimate the P values: *, P < 0.05. Error bars correspond to sd (n = 6).

Article Snippet: The membranes were documented using a chemiluminescence imager (G-BOX ChemiXR5; Syngene), and the optical density of the bands was quantified using ImageQuant software (Molecular Dynamics).

Techniques: Isolation, Mutagenesis, Activity Assay, Staining, Software, Concentration Assay