Quantity one 1 d analysis software

Manufactured by Bio-Rad

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Quantity One 1-D analysis software is a comprehensive tool for analyzing and quantifying 1-dimensional electrophoresis data, such as DNA, RNA, and protein gels. The software provides essential functions for image capture, analysis, and data management.

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Lab products found in correlation

Pvdf membrane, by Merck Group (18 mentions) Gel doc xr system, by Bio-Rad (10 mentions) Pierce bca protein assay kit, by Thermo Fisher Scientific (10 mentions) Molecular imager chemidoc xrs system, by Bio-Rad (9 mentions) Ripa lysis buffer, by Beyotime (8 mentions) Chemidoc xrs system, by Bio-Rad (8 mentions) Chemidoc xr, by Bio-Rad (8 mentions) Ecl plus reagent, by Merck Group (7 mentions) Pvdf membrane, by Bio-Rad (6 mentions) Bovine serum albumin (bsa), by Merck Group (6 mentions) Protease inhibitor cocktail, by Merck Group (5 mentions) Ripa buffer, by Beyotime (5 mentions) Protease inhibitor cocktail, by Roche (5 mentions) Phosphatase inhibitor cocktail, by Roche (5 mentions) Gapdh, by Cell Signaling Technology (5 mentions) β actin, by Merck Group (5 mentions) Rb2 p130 r27020, by BD (5 mentions) P16ink4a ab54210, by Abcam (5 mentions) Gapdh g8795, by Merck Group (5 mentions) Gs 800 densitometer, by Bio-Rad (5 mentions)

Close spelling variants of this product

Quantity One 1-D analysis software package (4 citations) Quantity One 1-D Analysis Software, version 4.4 (13 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 1-D analysis software v4.52 (14 citations) Quantity One 4.6.5 1-D Analysis Software (5 citations) Quantity One 4.6.3 1-D Analysis Software (2 citations) Quantity One 1-D analysis (15 citations) Quantity One 1-D software (36 citations) Quantity 1-D Analysis Software (6 citations)

396 protocols using quantity one 1 d analysis software

Western Blot Analysis of Secretome Proteins

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The same secretome samples used for HPLC-MS analysis (CTRL, HF) were tested on a 10% SDS-PAGE; separated proteins transferred onto a nitrocellulose membrane (Amersham, GE Healthcare, USA) using a wet transfer system (Bio-Rad Laboratories, USA). Membranes were blocked with 3% BSA in TBST for 1 h at room temperature. Primary and secondary antibodies were diluted in 3% BSA in TBST. All primary antibodies were incubated overnight at 4°C. HRP-conjugated secondary antibodies (Santa Cruz Biotechnology, USA) were incubated for 1 h at room temperature.
The following antibodies were used: CATD (C20), goat polyclonal (Santa Cruz Biotechnology, USA), dilution 1 : 300, and CH3L1 goat polyclonal (R&D Systems), dilution 1 : 500.
Densitometric quantification of photographic films was performed using Quantity One 1-D Analysis Software (Bio-Rad Laboratories, USA). Photographic films were scanned and analysed by Quantity One 1-D Analysis Software (Bio-Rad Laboratories, USA).

Rocchiccioli S., Cecchettini A., Ucciferri N., Terreni M., Viglione F., Trivella M.G., Citti L., Parodi O, & Pelosi G. (2015). Site-Specific Secretome Map Evidences VSMC-Related Markers of Coronary Atherosclerosis Grade and Extent in the Hypercholesterolemic Swine. Disease Markers, 2015, 465242.

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Quantitative Protein Expression Analysis

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The protein levels of act1, total p38, ERK, JNK and phosphorylated p38, ERK and JNK (p-p38, p-ERK and p-JNK) were detected by western blot analysis. Briefly, the tissues or cells were collected, and total protein was extracted in 100 µL of RIPA lysis buffer at 4°C for 30 min. The protein concentration was determined by the Bradford method. Samples containing 10 µg of protein were boiled, subjected to SDS-PAGE in 10% Tris-glycine gels and transferred electrophoretically to a polyvinylidene fluoride membrane. The membrane was incubated with 5% fat-free milk in Tris-buffered solution (TBS) containing 0.05% Tween 20 (1 h, room temperature) and then incubated with primary antibodies (against total p38, ERK, JNK, p-p38, p-ERK, p-JNK and GAPDH, each diluted 1∶1000 to 2000; all were purchased from Cell Signaling, Danvers, MA, USA; anti-act1, 1∶1500; Genetex, Irvine, CA, USA) overnight at 4°C. The membrane was then incubated with horseradish peroxidase-linked secondary antibody and finally processed using the ECL chemiluminescence reaction kit (Cell Signaling), followed by exposure on medical film. The relative band density of the target protein compared with GAPDH was quantified with the Bio-Rad Quantity One 1-D Analysis Software (Bio-Rad, Hercules, CA, USA).

Xia W., Bai J., Wu X., Wei Y., Feng S., Li L., Zhang J., Xiong G., Fan Y., Shi J, & Li H. (2014). Interleukin-17A Promotes MUC5AC Expression and Goblet Cell Hyperplasia in Nasal Polyps via the Act1-Mediated Pathway. PLoS ONE, 9(6), e98915.

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Protein Expression Analysis by Western Blot

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The cells were harvested and lysed with RIPA lysis buffer. Equal amounts of protein were loaded and separated via 10% sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE). Separated proteins were transferred onto 0.4-µm polyvinylidene difluoride (PVDF) membranes. After blocking with 5% skim milk for 3 h, the PVDF membranes were incubated overnight with primary antibody against RUNX (H00000860-M06) or GAPDH (H00002597-M01) (1:1,000; Abnova, Taipei, China) diluted in blocking solution. Subsequently, the membranes were washed 3 times with Tris-buffered saline (TBS) with Tween-20 (TBST) [50 mM Tris-HCl (pH 7.5), 150 mM NaCl, and 0.05% Tween-20] and horseradish peroxidase-conjugated secondary antibodies (ZB-2305; ZSGB-BIO, Beijing, China) were incubated with the membranes for 1 h at room temperature. The membranes were washed twice with TBST and once with TBS, and soaked in enhanced chemiluminescence (ECL) reagent. Protein bands were visualized using the Western Blotting Systems ECL kit (Amersham, Piscataway, NJ, USA). Data obtained from western blot analysis were analyzed using Bio-Rad Quantity One 1-D Analysis software (Bio-Rad, Hercules, CA, USA).

Chen H., Ji X., She F., Gao Y, & Tang P. (2016). miR-628-3p regulates osteoblast differentiation by targeting RUNX2: Possible role in atrophic non-union. International Journal of Molecular Medicine, 39(2), 279-286.

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Protein Extraction and Western Blot Analysis

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Proteins were extracted from rat ovarian granulosa cells, ovaries and breast tissues, and MCF-7 breast cancer cells using RIPA buffer (Sigma-Aldrich) with complete protease inhibitor cocktail tablets (Roche Applied Science). Denatured proteins (20 μg per sample) were separated on SDS-PAGE and transferred to PVDF membranes. For proteins from ovarian granulosa cells and ovaries, immunoblotting was performed using specific anti-FSHR (sc-13935; Santa Cruz Biotechnology, Inc), anti-aromatase (sc-14245; Santa Cruz Biotechnology, Inc), anti-phospho-PKA (#04-404; Upstate, Millipore), anti-p-AKT1/2/3 (ser 473)-R (sc-7985-R; Santa Cruz Biotechnology, Inc) and anti-phospho-PKC (Thr555/Thr563; Upstate, Millipore) antibodies with anti-GAPDH antibody as the internal standard. After incubation with horseradish peroxidase-conjugated secondary antibody, the chemiluminescence (GE Bio-health) was detected with the Bio-Rad Chemi Doc™ EQ densitometer (Bio-Rad) and quantified by Bio-Rad Quantity One 1-D Analysis software (Bio-Rad).

Lok Wong K., Ming Lai Y., Li K.W., Fai Lee K., Ng T.B., Pan Cheung H., Bo Zhang Y., Lao L., Ngok-Shun Wong R., Chui Shaw P., Ho Wong J., Zhang Z.J., Lam J.K., Wencai Y, & Wing Sze S.C. (2015). A Novel, Stable, Estradiol-Stimulating, Osteogenic Yam Protein with Potential for the Treatment of Menopausal Syndrome. Scientific Reports, 5, 10179.

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COL4A1 Protein Expression Analysis by Western Blot

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The protein level of COL4A1 was determined by using Western blot. After the cells were transfected with ASO-miR-214-5p, ASO-NC, miR-214-5p mimic and its control, and pcDNA3.1 (+)-COL4A1 and its control, for 48 hours, the cells were homogenised in radioimmunoprecipitation assay (RIPA) buffer (Beyotime, Shanghai, China) and additionally, protease inhibitors. Protein concentrations were determined by a bicinchoninic acid (BCA) assay kit (Thermo Fisher Scientific Inc., Rockford, Illinois). Equivalent amounts of protein (10 μg) were separated by sodium dodecyl sulfate (SDS)-polyacrylamide gel electrophoresis (PAGE), and were then transferred to nitrocellulose membranes (Sigma-Aldrich). After blocking with 5% non-fat milk, the membranes were incubated with anti-COL4A1 antibody (ab6586; 1:1000; Abcam, Cambridge, Massachusetts) at 4°C overnight. GAPDH was used as a loading control. Subsequently, the membranes were washed with Tris-buffered saline with Tween 20 (TBST) and incubated with horseradish peroxidase (HRP)-conjugated anti-goat IgG (ab181658; 1:5000; Abcam) at room temperature for two hours. An enhanced chemiluminescence (ECL) system was used to visualise the bands. Quantitative analysis was conducted by Bio-Rad Quantity One 1-D Analysis Software (Bio-Rad Laboratories, Hercules, California).

Li Q.S., Meng F.Y., Zhao Y.H., Jin C.L., Tian J, & Yi X.J. (2017). Inhibition of microRNA-214-5p promotes cell survival and extracellular matrix formation by targeting collagen type IV alpha 1 in osteoblastic MC3T3-E1 cells. Bone & Joint Research, 6(8), 464-471.

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BDNF Protein Quantification in Rat Brain

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The protein levels of BDNF in rat prefrontal cortex and hippocampus were measured using a BDNF Sandwich ELISA Kit (#CYT306; Millipore) following the manufacturer’s instructions. The protein expression levels of BDNF were normalized using the total protein concentration of the individual samples. Immunoblotting was performed using anti-TrkB receptor antibody (sc-8316; Santa Cruz Biotechnology, Inc) for proteins from the prefrontal cortex with anti-GAPDH antibody as the internal standard. After incubation with horseradish peroxidase-conjugated secondary antibody, the chemiluminescence (GE Bio-health) was detected using a Bio-Rad Chemi Doc™ EQ densitometer (Bio-Rad) and quantified by the Bio-Rad Quantity One 1-D Analysis software (Bio-Rad).

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Quantifying Hrd1 Protein Levels

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The Hrd1 protein level was determined by using Western blot analysis as previously described.21 (link) Briefly, the tissues or cells were dissociated on ice and homogenized in a radioimmunoprecipitation assay (RIPA) lysis buffer (Beyotime, Shanghai, China) containing 50 μL/mL protease inhibitor cocktail (Sigma-Aldrich, St. Louis, MO, USA) and 1 mM phenylmethylsulfonyl fluoride (PMSF) (Beyotime). The protein concentration in the supernatants was determined by the BCA method. Samples containing 20 µg of protein were boiled and subjected to sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE) on 10% Tris-glycine gels and electrophoretically transferred onto a polyvinylidene fluoride membrane. The membrane was blocked with 5% fat-free milk in Tris-buffered solution containing 0.05% Tween-20 for 1 hour at room temperature and then incubated with rabbit anti-human Hrd1 (1:5,000; Santa Cruz Biotechnology) overnight at 4°C. The membrane was washed and incubated with a horseradish peroxidase-linked secondary antibody (1:2,000, Beyotime) and finally processed by using an ECL chemiluminescence reaction kit (Millipore, Billerica, MA, USA), followed by exposure to medical film. The band density of the target protein relative to that of β-actin was quantified with Bio-Rad Quantity One 1-D Analysis Software (Bio-Rad Laboratories, Hercules, CA, USA).

Chen K., Han M., Tang M., Xie Y., Lai Y., Hu X., Zhang J., Yang J, & Li H. (2018). Differential Hrd1 Expression and B-Cell Accumulation in Eosinophilic and Non-eosinophilic Chronic Rhinosinusitis With Nasal Polyps. Allergy, Asthma & Immunology Research, 10(6), 698-715.

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Western Blot Analysis of Osteopontin Knockdown

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TPC-1 cells transfected with OPN-siRNA or the scr-siRNA were lysed in RIPA lysis buffer supplemented with phosphatase and protease inhibitors. Proteins were quantified using DCTM Protein Assay (Bio-RAD, Hercules, CA, USA) and then resolved by SDS-PAGE and transferred onto nitrocellulose membranes (GE Healthcare, Little Chalfont, UK). The primary antibodies were anti-tOPN (O-17 #18625) (1:500) from IBL Immuno-Biological Laboratories; anti-collagen type I—sc-8784 (1:400), and anti-osteocalcin sc-30044 (1:800) from Santa Cruz Biotechnology, Santa Cruz, CA, USA. Protein was detected using a horseradish peroxidase-conjugated antibody (Santa Cruz Biotechnology, Santa Cruz, CA, USA) and a luminescence system (Perkin-Elmer, Waltham, MA, USA). For protein loading control, membranes were incubated with an anti-GAPDH antibody from Santa Cruz Biotechnology (Santa Cruz, CA, USA). Protein expression was quantified using the Bio-Rad Quantity One 1-D Analysis software (Bio-Rad Laboratories, Inc., Hercules, CA, USA). All proteins were normalized by GAPDH loading control.

Ferreira L.B., Lima R.T., Bastos A.C., Silva A.M., Tavares C., Pestana A., Rios E., Eloy C., Sobrinho-Simões M., Gimba E.R, & Soares P. (2018). OPNa Overexpression Is Associated with Matrix Calcification in Thyroid Cancer Cell Lines. International Journal of Molecular Sciences, 19(10), 2990.

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Agarose Gel Electrophoresis of Genomic DNA

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A 1% agarose gel was prepared by dissolving agarose (Cat# A9539-10G, Thermo Scientific, Dallas, USA) in 1× TAE (40 mM Tris-acetate and 1 mM EDTA, pH 8.3) buffer (Cat# 15558042, Thermo Fisher Scientific, Chicago, USA) and boiled in a microwave. After cooling to room temperature, 0.5 µg/mL of ethidium bromide (Invitrogen, Chicago, USA) was added and poured on a gel cast apparatus (Biorad, USA) set with a 10 well comb. DNA samples were prepared by adding 50 to 100 ng of extracted genomic DNA, 1 µL of 10× Blue Juice Gel loading buffer (Life Technologies, Chicago, USA) and 1× TAE buffer to make up the total volume to 10 µL. DNA samples and 0.5 µg of Lambda DNA Hind III digest (New England Biolabs, Boston, USA) were loaded in separate wells of the 1% agarose gel and was run at 80 V in mini-sub cell GT cell mini agarose gel apparatus (Cat#1704467EDU, Biorad, Los Angeles, USA) containing 1× TAE running buffer. Images of the agarose gels were analyzed in Biorad Quantity One 1-D Analysis Software (Biorad, Los Angeles, USA) as previously described^{37 (link)}.

Dyavar S.R., Ye Z., Byrareddy S.N., Scarsi K.K., Winchester L.C., Weinhold J.A., Fletcher C.V, & Podany A.T. (2018). Normalization of cell associated antiretroviral drug concentrations with a novel RPP30 droplet digital PCR assay. Scientific Reports, 8, 3626.

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Protein Extraction and Western Blot Analysis of SGK1 Signaling

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The tissues or cells were dissociated on ice and homogenized in radioimmunoprecipitation assay lysis buffer (Beyotime, Shanghai, China) containing 1 mM phenylmethylsulfonyl fluoride (PMSF; Sigma-Aldrich), 10 μL/mL sodium fluoride (NaF; Sangon Biotech, Shanghai, China), 2 µL/mL protease inhibitor cocktail (Merck-Millipore, Bedford, MA, USA), and 1 µL/mL sodium orthovanadate (Na₂VO₃; Sangon Biotech). The supernatant protein concentration was determined using the BCA method. Samples containing 30 µg of protein were separated by 10% sodium dodecyl sulfate–polyacrylamide gel electrophoresis and electrophoretically transferred onto a nitrocellulose filter membrane. The membrane was blocked with 5% fat-free milk for 1 hour at room temperature and incubated with rabbit anti-human SGK1 (1:1,000; Cell Signaling Technology, Danvers, MA, USA), and rabbit anti-human p-SGK1 (1:1,000; Cell Signaling Technology) overnight at 4°C. The membrane was then washed and incubated with a corresponding secondary antibody, and processed using an electrochemiluminescence reaction kit (Merck-Millipore), followed by exposure to medical film. The density of the target protein band relative to that of β-actin (1:10,000; Beyotime) was quantified using Bio-Rad Quantity One 1-D Analysis Software (Bio-Rad Laboratories, Hercules, CA, USA).

Lai Y., Hu L., Yang L., Hu X., Song X., Yang J., Li H., Chen K., Li H, & Wang D. (2021). Interaction Between Serum/Glucocorticoid-Regulated Kinase 1 and Interleukin-6 in Chronic Rhinosinusitis. Allergy, Asthma & Immunology Research, 13(5), 776-790.

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