Un scan it software

Manufactured by Silk Scientific

Sourced in United States

UN-SCAN-IT software is a data analysis tool designed for digitizing and analyzing graphical data. It provides the ability to extract numerical values from images, graphs, and charts. The software supports a variety of image formats and can be used to measure areas, lengths, and other parameters from the imported data.

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Lab products found in correlation

Blocking one, by Nacalai Tesque (4 mentions) Nitrocellulose membrane, by Bio-Rad (4 mentions) Las 3000 imaging system, by Fujifilm (4 mentions) β actin, by Merck Group (4 mentions) Bca protein assay kit, by Thermo Fisher Scientific (4 mentions) β actin, by Silk Scientific (3 mentions) Complete protease inhibitor cocktail, by Roche (3 mentions) Hp scanjet 550c, by Silk Scientific (3 mentions) Pvdf membrane, by Merck Group (3 mentions) Dc protein assay, by Bio-Rad (3 mentions) Trans blot turbo transfer system, by Bio-Rad (2 mentions) Hrp conjugated β actin, by Santa Cruz Biotechnology (2 mentions) Total stat3, by Cell Signaling Technology (2 mentions) P stat3 y705, by Cell Signaling Technology (2 mentions) Vegfr2, by Cell Signaling Technology (2 mentions) Protease inhibitor cocktail, by Roche (2 mentions) Immobilon western chemiluminescent hrp substrate, by Merck Group (2 mentions) Western blotting luminol reagent, by Santa Cruz Biotechnology (2 mentions) β actin, by Santa Cruz Biotechnology (2 mentions) Imagequant las 4000, by GE Healthcare (2 mentions)

Close spelling variants of this product

UN-SCAN-IT (35 citations) UN-SCAN-IT gel software (33 citations) UN-SCAN-IT gel analysis software (9 citations) Un-Scan-It gel version 6.1 scanning software (9 citations) UN-SCAN-IT software version 5.1 (8 citations) UN-SCAN-IT gels (version6.1) software (7 citations) UN-SCAN-IT Graph Digitizer software (6 citations) UN-SCAN-IT (version 6.1) software (4 citations) UN-SCAN-IT gel digitizing software (3 citations) UN-SCAN-IT densitometry software (3 citations)

82 protocols using un scan it software

Immunoprecipitation and Immunoblotting Protocol

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Tissues were lysed in lysis buffer A [50 mM Hepes-NaOH (pH 7.5), 3 mM MgCl₂, 150 mM NaCl, 1 mM dithiothreitol, 1 mM phenylmethane sulfonylfluoride, leupeptin (1 μg/ml), 1 mM EDTA, 1 mM Na₃VO₄, and 10 mM NaF] containing biochemical detergents (0.5% NP-40, 1% CHAPS, and 0.03% SDS). Unless otherwise indicated, all lysis steps were performed at 4°C (12 (link), 36 (link)). For immunoprecipitations, the supernatants cleared by centrifugation were mixed with an antibody-absorbed protein G resin (GE Healthcare) or ExtraCruz (Santa Cruz Biotechnology) according to the respective manufacturer’s instructions. The immunoprecipitates or proteins in the cell supernatants were denatured, subjected to SDS–polyacrylamide gel electrophoresis, and blotted to polyvinylidene difluoride membranes using the TransBlot TurboTransfer System (Bio-Rad). The membranes were blocked with Blocking One (Nacalai) and immunoblotted using a primary antibody followed by a peroxidase-conjugated secondary antibody. The bound antibodies were detected using Chemiluminescence One (standard and strong detection reagents; Nacalai). The bands were scanned using a C-DiGit Blot Scanner (MS Systems). They were densitometrically analyzed to identify their quantification using UN-SCAN-IT software (Silk Scientific).

Miyamoto Y., Torii T., Tago K., Tanoue A., Takashima S, & Yamauchi J. (2018). BIG1/Arfgef1 and Arf1 regulate the initiation of myelination by Schwann cells in mice. Science Advances, 4(4), eaar4471.

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Western Blotting for Neuronal Calcium Sensor-1

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Cells were lysed in ice cold M-PER mammalian Protein Extraction Reagent (Thermo Scientific, Rockford, IL, USA) supplemented with protease inhibitors. To determine protein concentration a Bradford assay was conducted using the Bio-Rad protein assay reagent (Bio-Rad, San Diego, CA, USA). Proteins (30 μg) were subjected to sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE) and transferred to a nitrocellulose membrane (GE Healthcare, Arlington Heights, IL, USA). The resulting blots were blocked for 1 h at RT in 5% skimmed dry milk diluted in 1X Tris-buffered saline supplemented with Tween-20 (TBST). Blots were incubated at 4°C O/N in primary antibodies specific for NCS-1 (Abcam, Cambridge, MA, USA; diluted 1:1000) and β-tubulin (Cell Signaling, Boston, MA, USA; diluted 1:500). Following incubation, blots were washed with 5% milk/TBST before incubation with a horseradish peroxidase, labeled goat anti-rabbit IgG (Santa Cruz Biotechnology Inc., Paso Robles, CA, USA; diluted 1:1000) at RT for 1 h. Blots were washed with 5% milk/TBST and bands were visualized using electrochemiluminescence detection reagents (Thermo Scientific, Rockford, IL, USA). Immunoblots were then quantified by scanning densitometry using the Un-Scan-It software (Silk Scientific, Orem, UT, USA).

Moore L.M., England A., Ehrlich B.E, & Rimm D.L. (2017). Calcium Sensor, NCS-1, Promotes Tumor Aggressiveness and Predicts Patient Survival. Molecular cancer research : MCR, 15(7), 942-952.

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Zymographic Analysis of Gelatinases

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The zymographic analyses were performed on sera samples and the tissue sample (kidney) homogenates, using 1% gelatin in the gels, as described^{82 (link)–84 (link)}. Samples were prepared and were electrophoretically resolved on 7.5% SDS-PAGE containing 1.5% gelatin as a substrate. In the end, the gels were incubated in renaturation buffer (2.5% Triton X-100) for 30 min to remove SDS, rinsed in distilled water, and then incubated for 24 h at 37 °C in a water bath in an activation buffer (50 mmol/L Tris–HCl, pH 7.4, and 5 mmol/L CaCl₂). For reverse zymography, 10 μL of active collagenase was added to the active buffer. The gels were stained with the Coomassie R-250 brilliant blue dye for 1 h and then destained them with the destaining buffer (10% acetic acid, 10% methanol, and 80% distilled water). The clear digested regions representing MMPs activities as accessed by running the prestained molecular weight markers were quantified densitometrically using the Un-Scan-It software (Silk Scientific Inc., Orem, Utah, USA).

Singh M., Pushpakumar S., Zheng Y., Smolenkova I., Akinterinwa O.E., Luulay B, & Tyagi S.C. (2023). Novel mechanism of the COVID-19 associated coagulopathy (CAC) and vascular thromboembolism. Npj viruses, 1, 3.

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VEGFR2 and STAT3 Phosphorylation Assay

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Cells were lysed in RIPA buffer containing protease inhibitor cocktail (Roche Diagnostics, Indianapolis, IN) and orthovanadate (Thermo Scientifics, Rockford, IL), and clarified by centrifugation at 13,000×g rpm for 5 min at 4 °C. Protein concentration in the supernatant was quantified by bicinchoninic acid assay (BCA). 20 µg of protein from each treatment was loaded into NuPAGE 4–12% Bis-Tris Gels (Invitrogen, Carlsbad, CA), transferred to a PVDF membrane, and incubated with antibodies to phosphorylated VEGFR2 (p-VEGFR2, Y996) (1:500, Santa Cruz Biotechnology, Santa Cruz, CA), VEGFR2 (1:1000, Cell Signaling Technology, Danvers, MA), p-STAT3 (Y705) (1:1000, Cell Signaling Technology), or total STAT3 (1:1000, Cell Signaling Technology) at 4 °C overnight. After incubating with primary antibodies, membranes were then probed with HRP conjugated goat anti-rabbit secondary antibody or goat anti-mouse secondary antibody (1:3000–5000, ThermoFisher Scientific, Waltham, MA) at room temperature for 1 h. All the membranes were reprobed with HRP conjugated β-actin (1:3000, Santa Cruz Biotechnology) as loading controls. Densitometry analysis was performed on exposed films using UN-SCAN-IT software (Silk Scientific, Orem, UT) and normalized to β-actin.

Simmons A.B., Bretz C.A., Wang H., Kunz E., Hajj K., Kennedy C., Yang Z., Suwanmanee T., Kafri T, & Hartnett M.E. (2018). Gene therapy knockdown of VEGFR2 in retinal endothelial cells to treat retinopathy. Angiogenesis, 21(4), 751-764.

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Myosin Heavy Chain Isoform Analysis

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Digastric muscles (chosen due to previously reported adaptations to
weaning [14 (link), 15 (link)]) and limb muscles (used as controls) were
isolated from euthanized mice. Protein was analyzed with a 6% acrylamide, 30%
glycerol separation gel and a 4% acrylamide, 30% glycerol stacking gel [29 (link), 30 (link)]. Protein (400 ng) from each muscle was separated through sodium
dodecyl sulphate polyacrylamide gel electrophoresis (SDS-PAGE) for 29–32
hours, using a SE900 gel system(Hoefer, Inc), then silver stained (SilverQuest
Staining Kit, Thermo Fisher Scientific). Band optical density (average pixel
value), obtained using UN-SCAN-IT software (Silk Scientific), was used to
determine relative percentage of MyHC isoform composition of each muscle.

Glass T.J., Twadell S.L., Valmadrid L.C, & Connor N.P. (2018). Early impacts of modified food consistency on oromotor outcomes in mouse models of Down syndrome. Physiology & behavior, 199, 273-281.

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Expression and Purification of Chimera Proteins

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Chimera proteins, CaM(1TnC), CaM(2TnC), CaM(3TnC), and CaM(4TnC), were obtained as a generous gift from Dr. George [39 (link)]. CaM and the chimera proteins were expressed and purified as described previously [14 (link)]. In general, bacterial cells carrying the plasmid containing gene inserts of CaM(1TnC), CaM(2TnC), and CaM(4TnC) were induced for protein expression by heat shock at 42°C at an OD₆₀₀ = ~1.0. The culture was continuously incubated for an additional 4–6 hrs at 42°C. CaM(3TnC) was sub-cloned to a pLW-His₆ vector and was expressed as described previously for NOX5 [40 (link)]. All proteins except CaM(3TnC) were purified through a phenyl-sepharose column [41 (link)]. CaM(3TnC) was purified through a Ni-NTA column by elution with 40 mM imidazole. The purified proteins were stored at −80°C until further use. Protein purity was checked on SDS-PAGE electrophoresis and its purity was estimated to be > 95% based on density profiles measured using UN-SCAN-IT software (Silk Scientific, Inc., Utah). The concentrations of CaM and chimera proteins were determined as reported previously [20 (link)]. Dansylation of CaM and chimeras was performed in the presence of 2 mM Ca²⁺ as described previously [30 (link)].

Jensen D., Reynolds N., Yang Y.P., Shakya S., Wang Z.Q., Stuehr D.J, & Wei C.C. (2015). The exchanged EF-hands in calmodulin and troponin C chimeras impair the Ca2+-induced hydrophobicity and alter the interaction with Orai1: a spectroscopic, thermodynamic and kinetic study. BMC Biochemistry, 16, 6.

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ACE2 Protein Detection in Tissue Homogenates

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ACE2 protein in tissue homogenates was detected by Western blotting. Briefly, frozen tissue was homogenized on ice in N-Per Total Protein Extraction reagent (Thermo Scientific) with addition of protease and phosphatase inhibitor cocktails (Sigma-Aldrich). Homogenates were centrifuged at 20,000 g at 4°C and supernatants were collected. Protein content was measured by BCA method (Thermo Scientific). Equal amounts of total proteins were mixed with 4x Laemmli sample buffer and boiled for 10 min at 80°C. Protein extracts were separated on 8% SDS-PAGE denaturing acrylamide gels using approximately 35 μg of total protein per lane and then blotted to nitrocellulose membrane (0.45 μm, Amersham) using standard Tris-glycine wet method. Membranes were blocked with 5% dry milk (Bio-Rad), incubated with anti-ACE2 (Proteintech #21115-1-AP or R&D Systems, #AF3437) at 1/1000 or anti-GAPDH (Proteintech #10494-1-AP) at 1/5000 dilution rabbit polyclonal antibodies overnight at 4°C, washed several times in TBST buffer (pH 8.0) and incubated 60 min with secondary anti-rabbit-HRP antibody (Pierce). Signal was detected using Clarity chemiluminescence substrate (Bio-Rad). Blots were repeated at least three times with comparable results. Densitometric band analysis was performed by Un-scan-it software (Silk Scientific, Inc) on 3 independent blots using GAPDH band for relative comparisons.

Bilinska K., Jakubowska P., von Bartheld C.S, & Butowt R. (2020). Expression of the SARS-CoV-2 Entry Proteins, ACE2 and TMPRSS2, in Cells of the Olfactory Epithelium: Identification of Cell Types and Trends with Age. ACS chemical neuroscience, 11(11), 1555-1562.

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Western Blot Analysis of Protein Lysates

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Cells were washed in cold PBS and subjected to lysis at 4°C in lysis buffer (50 mM Tris-HCl pH 7.4, 150 mM NaCl, 1 mM EDTA, 1% Triton X-100) supplemented with a cocktail of protease inhibitors (Sigma-Aldrich). Lysates were cleared by centrifugation at 16,000 x g for 20 min, and protein concentration determined with a protein assay solution (Bio-Rad Laboratories, Hercules, CA, USA). Samples with equivalent amount of protein were boiled for 5 min with Laemmli SDS-PAGE sample buffer, and analyzed by SDS-PAGE. Proteins were electroblotted onto nitrocellulose membranes, and membranes were incubated sequentially with primary and secondary antibodies for 1 h at room temperature, or overnight at 4°C. Chemiluminescence protein detection was performed using Pierce Western Blotting Substrate (Thermo Scientific). As an internal loading control, β-actin levels were examined on the same nitrocellulose membranes. Quantification of chemiluminiscence signal was carried out using UN-SCAN-IT software (Silk Scientific Corporation, Orem, UT, USA).

Cavieres V.A., González A., Muñoz V.C., Yefi C.P., Bustamante H.A., Barraza R.R., Tapia-Rojas C., Otth C., Barrera M.J., González C., Mardones G.A., Inestrosa N.C, & Burgos P.V. (2015). Tetrahydrohyperforin Inhibits the Proteolytic Processing of Amyloid Precursor Protein and Enhances Its Degradation by Atg5-Dependent Autophagy. PLoS ONE, 10(8), e0136313.

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Investigating Cold Plasma-Induced Protein Expression

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HaCaT cells (3 × 10⁵) were plated in 6-cm dishes and incubated with complete cell culture media which were pretreated with various conditions of He/Ar-CAPJ for 24 h. The treated cells were lysed with 100 μL RIPA reagent containing with protease and phosphatase inhibitors (Roch, Indianapolis, IN, United States). The cell lysates resolved by 10% SDS-PAGE and then performed the Western blot assay. The samples were transferred onto a polyvinylidene difluoride (PVDF) membrane (Millipore, Billerica, MA, United States) and immersed with 5% dehydrated skim milk to block non-specific protein binding. The membranes were incubated with primary antibodies as indicated in each experiment. The blots were then probed with the HRP-conjugated secondary antibody. The proteins of interest were detected using ECL Western blotting detection reagents (GE Healthcare, Piscataway, NJ, United States) and visualized by using Azure c400 system and AzureSpot Analysis Software (Azure Biosystems, Dublin, CA, United States). The signal intensity of each protein was quantified with UN-SCAN-IT software (Silk Scientific Corporation, Orem, UT, United States) as described previously (Lin et al., 2019 (link)). These data were expressed as the mean ± standard deviation determined from three independent experiments.

Lou B.S., Hsieh J.H., Chen C.M., Hou C.W., Wu H.Y., Chou P.Y., Lai C.H, & Lee J.W. (2020). Helium/Argon-Generated Cold Atmospheric Plasma Facilitates Cutaneous Wound Healing. Frontiers in Bioengineering and Biotechnology, 8, 683.

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Western Blotting of Protein Extracts

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Cells (5 × 10⁵/ml) were exposed to drugs or solvent for 48 hrs, collected by centrifugation, washed with cold PBS, and lysed with cell lysis buffer (Cell Signaling Technology, Danvers, MA). The protein concentrations were determined using a BCA Protein Assay kit (Thermo Fisher Scientific, Rockford, IL). Proteins were resolved on polyacrylamide-SDS gels and blotted onto nitrocellulose membranes (Bio-Rad, Hercules, CA). Western blot analyses were done by chemiluminescence using the Immobilon Western Chemiluminescent HRP Substrate (EMD Millipore). The antibodies, their sources, and other relevant information are shown in Supplementary Table 2. X-ray films were scanned with the EPSON Perfection V750 PRO and analyzed with UN-SCAN-IT software (Silk Scientific, Orem, UT).

Valdez B.C., Li Y., Murray D., Liu Y., Nieto Y., Champlin R.E, & Andersson B.S. (2017). Combination of a hypomethylating agent and inhibitors of PARP and HDAC traps PARP1 and DNMT1 to chromatin, acetylates DNA repair proteins, down-regulates NuRD and induces apoptosis in human leukemia and lymphoma cells. Oncotarget, 9(3), 3908-3921.

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