Quantity 1 d analysis software

Manufactured by Bio-Rad

Quantity 1-D Analysis Software is a data analysis tool designed for handling one-dimensional electrophoresis gel data. The software provides functionality for image analysis, band detection, and quantification of protein or nucleic acid samples.

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Lab products found in correlation

Chemidoc xrs system, by Bio-Rad (2 mentions) γ 32p adenosine triphosphate, by PerkinElmer (2 mentions) Gs 360, by Bio-Rad (2 mentions) T4 polynucleotide kinase, by New England Biolabs (2 mentions) Ripa buffer, by Merck Group (1 mentions) Nupage lds sample buffer, by Thermo Fisher Scientific (1 mentions) Immobilon p pvdf membrane, by Merck Group (1 mentions) Zymogram renaturation buffer, by Bio-Rad (1 mentions) Zymogram development buffer, by Bio-Rad (1 mentions) Zymogram sample buffer, by Bio-Rad (1 mentions) Mini protean tetra cell system, by Bio-Rad (1 mentions) Gel doc xr system, by Bio-Rad (1 mentions) Gelatin, by Merck Group (1 mentions) Hybond c membrane, by Cytiva (1 mentions) Horseradish peroxidase conjugated anti goat igg, by Abcam (1 mentions) Fluor s multiimager, by Bio-Rad (1 mentions)

Spelling variants of this product

Quantity One 1-D analysis software (396 citations) Quantity 1 software (16 citations) Quantity One 1-D analysis software v4.52 (14 citations) Quantity One 1-D Analysis Software, version 4.4 (13 citations) 1-D Analysis Software (5 citations) Quantity One 4.6.5 1-D Analysis Software (5 citations) Quantity I software (2 citations) Quantity One (Quantity One 1-D Analysis Software 170-9600, (2 citations) Discovery Series Quantity One 1-D Analysis Software (2 citations) Quantity One 4.6.3 1-D Analysis Software (2 citations)

6 protocols using quantity 1 d analysis software

Western Blot Analysis of Histone Proteins

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Protein was obtained by lysis of cells in ice-cold RIPA buffer (EMD-Millipore) containing 1X HALT protease and phosphatase inhibitor cocktail (Pierce, Rockford, IL) for 15 min. Protein concentrations were determined with the Bradford assay for equilibration prior to loading for SDS-PAGE. Proteins were transferred to nitrocellulose for immunoblotting. The following dilutions of primary antibodies were used: 1:500 rabbit anti-H1 (GeneTex, Irvine, TX, GTX102924), 1:500 rabbit anti-H2 (GeneTex, Irvine, TX, GTX108152), 1:500 rabbit anti-H3 (GeneTex, GTX100187) and 1:500 rabbit anti-H4 (GeneTex, GTX100387). After application of 1:1000 donkey anti-rabbit-HRP secondary antibodies (Abcam, Cambridge, MA, cat. no. ab97064), bands were visualized by chemiluminescence (WestPico Supersignal kit, Thermo-Fisher, Waltham, MA) alongside a Bionexus BNPM50 prestained protein marker (Bionexus, Oakland, CA) to determine relative mobility, using a Bio-Rad Chemi Doc XRS+ System with Quantity 1-D Analysis Software (Bio-Rad, Hercules, CA).

Adderley S.P., Zhang X.E, & Breslin J.W. (2015). Involvement of the H1 histamine receptor, p38 MAP kinase, MLCK, and Rho/ROCK in histamine-induced endothelial barrier dysfunction. Microcirculation (New York, N.Y. : 1994), 22(4), 237-248.

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Immunoblot Analysis of Lymphangion Proteins

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Approximately 10 lymphangions, freshly isolated from rat mesentery, were placed in 200 μl 1X RIPA (4 °C) containing HALT Protease and Phosphatase Inhibitor Cocktail (Pierce, Rockford, IL). The mixture was sonicated at 4 °C for 5 s twice using a Fisher Sonic Dismembranator, model FB-120 (Fisher Scientific, Asheville, NC). Protein concentrations were determined using the BCA protein assay (Pierce) to equilibrate samples. Lysate was mixed with 4X NuPage LDS sample buffer containing reducing agent (Invitrogen, Grand Island, NY). Samples containing 40 μg of protein were loaded into 4–20% Novex Bis-Tris gels (Invitrogen) for SDS-PAGE to separate proteins. The NexusPointer prestained protein ladder (BioNexus, Oakland, CA) was used to determine molecular weight vs. mobility. The proteins were transferred from the gels to Immobilon-P PVDF membranes (Millipore) by wet transfer. Membranes were blocked with 5% BSA in TBST. Primary antibodies were 1:200 rabbit anti-H1 (GTX70501) or 1:200 rabbit anti-H2 (GTX108152). The secondary antibody was 1:3000 donkey anti-rabbit IgG-HRP (ab97064). Bands were visualized using WestPico Supersignal reagent (Pierce; 5 min incubation) and a BioRad Chemi Doc XRS+ System with Quantity 1-D Analysis Software (5 min exposure).

Kurtz K.H., Moor A.N., Souza-Smith F.M, & Breslin J.W. (2014). Involvement of H1 and H2 receptors and soluble guanylate cyclase in histamine-induced relaxation of rat mesenteric collecting lymphatics. Microcirculation (New York, N.Y. : 1994), 21(7), 593-605.

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Gelatin Zymography for MMP2 and MMP9 Detection

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gelatin zymography was used for the detection of MMP2 and MMP9 on a protein level and the corresponding activity. Supernatant fluids were mixed 1:2 with non-reducing Zymogram sample buffer (BioRad, Munich, Germany). Samples were loaded onto 0.75 mm thick, 7.5% polyacrylamide gels (all components Carl Roth, Karlsruhe, Germany) containing 2 mg/ml gelatin (Merck, Darmstadt, Deutschland). Electrophoresis was carried out on the Mini-PROTEAN Tetra Cell System (Bio-Rad). Afterwards, gels were washed twice for 15 min in Zymogram renaturation buffer and incubated over night in Zymogram development buffer at 37°C (both Bio-Rad). Staining with Coomassie solution and subsequent destaining revealed clear bands originating from MMP activity. Pictures of gels were taken and analyzed with the Gel Doc XR+ System and the Quantity 1D Analysis Software (both Bio-Rad).

Hengartner N.E., Fiedler J., Schrezenmeier H., Huber-Lang M, & Brenner R.E. (2015). Crucial Role of IL1beta and C3a in the In Vitro-Response of Multipotent Mesenchymal Stromal Cells to Inflammatory Mediators of Polytrauma. PLoS ONE, 10(1), e0116772.

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Electrophoretic Mobility Shift Assay for Transcription Factor Binding

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Complementary pairs of ∼40bp non-risk and risk probes were chemically synthesized by Integrated DNA Technologies, annealed, and end-labeled with (γ-³²P) adenosine triphosphate (Perkin Elmer) using T4 polynucleotide kinase (New England Biolabs (NEB); #M0291S) (Supplementary Table S1). Ten micrograms of nuclear proteins, extracted from Jurkat, EBV B, and THP-1 cells stimulated with or without P/I, were incubated with labelled 50,000 cpm probes in binding buffer (1 μg poly dI-dC, 20 mM HEPES, 1mM MgCl₂, 100 mM Tris-HCl, pH 7.4, and 0.5 mM EDTA) for 30min at room temperature. DNA-protein complexes were resolved on non-denaturing 5% acrylamide gels in 0.5X Tris borate/EDTA. Dried gels were exposed overnight on a phosphor screen, visualized on a phophor-imager (BioRad; GS-360), and quantified using BioRad Quantity 1D Analysis software. For competition assays, 10, 50, and 100-fold excess of unlabeled non-risk and risk probes were added to the binding reactions. For the EMSA-SS, anti-p65 antibody (GeneTex, Inc.; #GTX107678) was added to the binding reaction and incubated for 15 min at room temperature prior to adding labeled probe.

Pasula S., Gopalakrishnan J., Fu Y., Tessneer K.L., Wiley M.M., Pelikan R.C., Kelly J.A, & Gaffney P.M. (2022). Systemic lupus erythematosus variants modulate the function of an enhancer upstream of TNFAIP3. Frontiers in Genetics, 13, 1011965.

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Electrophoretic Mobility Shift Assay of Genetic Variants

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Complementary pairs of 41 bp non-risk and risk probes of individual variants were chemically synthesized by Integrated DNA Technologies (Supplemental Table 1), annealed and end-labeled with (γ-³²P) adenosine triphosphate (Perkin Elmer) using T4 polynucleotide kinase (New England Biolabs (NEB); #M0201S). Nuclear proteins were extracted from Jurkat, EBV B, and THP1 cells with or without P/I stimulation for 2 h. Ten micrograms of nuclear protein were incubated with labelled 50,000 cpm non-risk or risk probes in binding buffer (1 μg poly dI-dC, 20 mM HEPES, 1 mM MgCl₂, 100 mM Tris-HCl, pH 7.4, and 0.5 mM EDTA) for 30 min at room temperature. DNA-protein complexes were resolved on a non-denaturing 5% acrylamide gel in 0.5X Tris borate/EDTA. Gels were dried and exposed overnight on a phosphor screen. DNA-protein complexes were visualized on a phosphor-imager (Bio-Rad; GS-360) and quantified using Bio-Rad Quantity 1D Analysis software. For competition assays, 10, 50, and 100-fold excess of unlabeled non-risk or risk probes were added to the EMSA binding reactions.

Gopalakrishnan J., Tessneer K.L., Fu Y., Pasula S., Pelikan R.C., Kelly J.A., Wiley G.B, & Gaffney P.M. (2021). Variants on the UBE2L3-YDJC autoimmune disease risk haplotype increase UBE2L3 gene expression by modulating CTCF and YY1 binding.. Arthritis & rheumatology (Hoboken, N.J.), 74(1), 163-173.

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Immunoblotting Analysis of Protein Levels

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Immunoblotting was carried out with 50 μg protein on 12.5% SDS-PAGE. The electrophoresis was performed at room temperature and the proteins were electroblotted onto Hybond-C membrane (Amersham Biosciences, U.K.) at 150 mA for 2 h. The membranes were blocked with 5% (w/v) nonfat milk in TBST buffer (0.1 M Tris pH 7.9, 0.15 M NaCl and 0.1% Tween 20) and probed with primary polyclonal anti-MSR (ab16803) and anti-DnaK (ab80161) (Abcam Ltd., U.K.) at varying dilutions (1:1000–1:15000) in TBS buffer. Immunodetection was performed with horse radish peroxidase conjugated anti-goat IgG (Abcam Ltd., U.K.) as secondary antibody at a concentration of 1:20000 for detection using enhanced chemiluminescence (Pierce). X-ray film from immunoblotting was scanned using Bio-Rad FlourS system equipped with a 12-bit camera and exported in tiff format. Protein quantification was performed using the Fluor S MultiImager (Bio-Rad) and Quantity 1-D Analysis software (Bio-Rad) using the volume analysis function, and the relative signals were calculated.

Ghosh S., Narula K., Sinha A., Ghosh R., Jawa P., Chakraborty N, & Chakraborty S. (2016). Proteometabolomic Study of Compatible Interaction in Tomato Fruit Challenged with Sclerotinia rolfsii Illustrates Novel Protein Network during Disease Progression. Frontiers in Plant Science, 7, 1034.

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