Liteablot extend

Manufactured by Euroclone

Sourced in Italy, United States

The LiteAblot EXTEND is a compact and versatile laboratory equipment designed for various applications. It is a multi-functional device that can perform tasks such as Western blotting, dot blotting, and slot blotting. The LiteAblot EXTEND is a reliable and efficient tool for researchers and scientists working in the field of molecular biology and biochemistry.

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Lab products found in correlation

Chemidoc xrs system, by Bio-Rad (3 mentions) Protein assay, by Bio-Rad (2 mentions) Polyvinylidene difluoride membrane, by Bio-Rad (2 mentions) Biospectrum imaging system, by Analytik Jena (2 mentions) Halt protease inhibitor cocktail, by Thermo Fisher Scientific (2 mentions) Visionworks ls image acquisition and analysis software, by Analytik Jena (2 mentions) Mouse anti β actin, by Merck Group (2 mentions) Image lab software, by Bio-Rad (1 mentions) Rabbit anti gapdh, by Cell Signaling Technology (1 mentions) Protease and phosphatase inhibitor, by Thermo Fisher Scientific (1 mentions) Ni nta agarose resin, by Qiagen (1 mentions) T5168, by Merck Group (1 mentions) Nupage novex 4 12 bis tris gel, by Thermo Fisher Scientific (1 mentions) Protein assay system, by Bio-Rad (1 mentions) Anti β actin 20 33, by Merck Group (1 mentions) Non fat dry milk, by Bio-Rad (1 mentions) Protease inhibitor, by Roche (1 mentions) Polyvinylidene difluoride membrane, by Merck Group (1 mentions) Phosphatase inhibitor, by Roche (1 mentions) Imagequantlas 4000 digital imager, by GE Healthcare (1 mentions)

Spelling variants of this product

LiteAblot (8 citations) LiteAblot EXTEND chemiluminescent substrate (5 citations) LiteAblot extend substrate (3 citations) ECL LiteAblot Extend (2 citations)

8 protocols using liteablot extend

Western Blot Analysis of TFEB Protein

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Proteins were extracted by sonicating the tissues in RIPA buffer, containing protease and phosphatase inhibitors (Thermo Scientific) and centrifuged for 10 min at 13 000 rpm at 4°C.
Protein concentrations were measured using the Bio-Rad Protein Assay (Bio-Rad Laboratories, Inc., Hercules, CA) according to the manufacturer’s instructions. Proteins were separated under reducing condition by electrophoresis on 8% gels (NuSep, Köln, Germany) and immunoblotted onto polyvinylidene difluoride membranes. The membranes were blocked with 5% BSA diluted in Tris-buffered saline, 0.1% Tween 20 and incubated overnight with rabbit anti-TFEB (1:1000) (#A303-673A Bethyl laboratories Inc., Montgomery, Texas) or rabbit anti-GAPDH (1:1000) (#5174 Cell Signalling, Danvers, Massachusetts). Following the incubation with horseradish peroxidase (HRP), secondary antibody conjugates IgG (Jackson ImmunoResearch Europe Ltd, Cambridge House, UK). Immunoblots were developed with LiteAblot EXTEND (EuroClone, Milan, Italy) and acquired with the ChemiDoc XRS System (Bio-Rad). Density of the bands was quantified by Image Lab software (Bio-Rad).

De Leo E., Taranta A., Raso R., Polishchuk E., D’Oria V., Pezzullo M., Goffredo B.M., Cairoli S., Bellomo F., Battafarano G., Camassei F.D., Del Fattore A., Polishchuk R., Emma F, & Rega L.R. (2022). Genistein improves renal disease in a mouse model of nephropathic cystinosis: a comparison study with cysteamine. Human Molecular Genetics, 32(7), 1090-1101.

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Purification and Detection of 6His-Ubiquitin Conjugates

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Cells transformed with a plasmid encoding 6His-ubiquitin under the CUP1 promoter [YEp96-6His-Ub, (Iglesias et al. 2010 (link))] were grown on selective media and stimulated overnight with 0.1 mM CuSO₄. Growth was stopped in the morning at an OD₆₀₀ of 0.8–1. Cells were lysed in guanidinium buffer (6 M guanidinium-HCl, 0.1 M Na₂HPO₄/NaH₂PO₄, 0.01 M Tris-HCl, pH 8.0, 0.1% Triton X-100, 5 mM imidazole, 10 mM β-mercaptoethanol, 0.1 mM MG132 and protease inhibitors), 1/20^th of the lysate was kept aside as input material and TCA (5.5%) precipitated; the rest was incubated on a Ni-NTA agarose resin (QIAGEN) at 4° with rotation. The resin was washed three times with urea buffer (8 M urea, 0.1 M Na₂HPO₄/Na₂HPO₄, 0.01 M Tris-HCl, pH 6.4, 3.5 mM β-mercaptoethanol, and 0.1% Triton X-100) before elution in 2X sample buffer (0.125 M Tris-HCl, pH 6.8, 4% SDS, 0.285 M β-mercaptoethanol, 20% SDS, 2% bromophenol blue). Eluates and inputs were loaded on 7.5% and 10% SDS-PAGE gels, respectively. Western blots were hybridized with anti-myc, Anti-6X His tag, and anti-Ada2 antibodies. Signals were detected by chemiluminescence using LiteAblot Extend (EuroClone) and the ChemiDoc XRS+ System (Biorad).

Canzonetta C., Vernarecci S., Iuliani M., Marracino C., Belloni C., Ballario P, & Filetici P. (2015). SAGA DUB-Ubp8 Deubiquitylates Centromeric Histone Variant Cse4. G3: Genes|Genomes|Genetics, 6(2), 287-298.

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Saquinavir Induces Protein Ubiquitination in HeLa Cells

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After 2 h of treatment with 40, 60 and 80 µM saquinavir, whole HeLa cell protein extracts were prepared in 150 mM NaCl, 1% Nonidet-40, 50 mM Tris-HCl (pH 7.5) and Halt Protease Inhibitor Cocktail (Thermo Fisher Scientific, Inc.). Cell extracts (20 µg) were resolved by sodium dodecyl sulfate-polyacrylamide gel electrophoresis (NuPAGE^® Novex^® 4–12% Bis-Tris gels; Thermo Fisher Scientific, Inc.) and blotted onto polyvinylidene difluoride membranes (Bio-Rad Laboratories, Inc., Hercules, CA, USA). α-Tubulin was used as a protein loading control. Following blocking in Tris-buffered saline containing 5% non-fat milk, the blots were incubated with primary antibodies against α-tubulin (dilution, 1:20,000; T5168; Sigma-Aldrich; Merck Millipore) or ubiquitin (dilution, 1:200; P4D1; Santa Cruz Biotechnology, Inc., Dallas, TX, USA) at 4°C for 12 hours, followed by incubation with horseradish peroxidase-conjugated secondary rabbit anti-mouse IgG (dilution, 1:10,000; catalog no., A9044; Sigma-Aldrich; Merck Millipore) at room temperature for 1 h. Signals were detected on a BioSpectrum Imaging System (UVP, Inc., Upland, CA, USA) with the LiteAblot^® EXTEND (Euroclone SpA). Images were processed with VisionWorks^® LS Image Acquisition and Analysis software version 7.0.1 (UVP, Inc.).

Bandiera E., Todeschini P., Romani C., Zanotti L., Erba E., Colmegna B., Bignotti E., Santin A.D., Sartori E., Odicino F.E., Pecorelli S., Tassi R.A, & Ravaggi A. (2016). The HIV-protease inhibitor saquinavir reduces proliferation, invasion and clonogenicity in cervical cancer cell lines. Oncology Letters, 12(4), 2493-2500.

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Western Blot Analysis of FOXM1 Protein

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Whole protein extracts from cells at 24 h following siRNA transfection or untransfection were lysed in NaCl, 1% Nonidet‑40, 50 mM Tris‑HCl (pH 7.5) and Halt Protease Inhibitor Cocktail (Thermo Fisher Scientific), and protein concentrations were determined using a Bio-Rad protein assay system (Bio-Rad). Equivalent amounts of proteins were separated by SDS-PAGE, and then transferred to polyvinylidene difluoride membranes (Bio-Rad). After being blocked in Tris-buffered saline (TBS) containing 5% non-fat milk, the blots were incubated with the following primary antibodies: anti-FOXM1 (clone sc-502, 1:200 dilution, Santa Cruz Biotechnology, Santa Cruz, CA), and anti-β-actin ((20–33), 1:200 dilution) (Sigma-Aldrich, Saint Louis, Missouri, USA), at 4 °C for 12 h, followed by incubation with horseradish peroxidase-conjugated secondary (anti-mouse or anti-rabbit) IgGs at room temperature for 1 h. Signals were detected on BioSpectrum® Imaging System (UVP, LLC, Upland, CA, USA) with the LiteAblot® EXTEND (EuroClone). Images were processed with VisionWorks® LS Image Acquisition and Analysis software (version 7.0.1, UVP, LLC).

Tassi R.A., Todeschini P., Siegel E.R., Calza S., Cappella P., Ardighieri L., Cadei M., Bugatti M., Romani C., Bandiera E., Zanotti L., Tassone L., Guarino D., Santonocito C., Capoluongo E.D., Beltrame L., Erba E., Marchini S., D’Incalci M., Donzelli C., Santin A.D., Pecorelli S., Sartori E., Bignotti E., Odicino F, & Ravaggi A. (2017). FOXM1 expression is significantly associated with chemotherapy resistance and adverse prognosis in non-serous epithelial ovarian cancer patients. Journal of Experimental & Clinical Cancer Research : CR, 36, 63.

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Western Blot Analysis of Adipocyte Proteins

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Cells and tissues were collected and lysed in 40 μl RIPA buffer (20 mM Tris-HCl, pH 7.5, 150 mM NaCl, 1 mM EGTA, 1% NP-40, 1% sodium deoxycholate) supplemented with protease inhibitors (Roche) and phosphatase inhibitors (Sigma). Protein concentration was determined with the BCA Protein Assay (ThermoFisher). Protein extracts (30–40 μg) were mixed with Novex Sample Buffer and Reducing Agent (Life Technologies), resolved by SDS-PAGE in 12%, 10% or 4–12% gradient gels and blotted onto polyvinylidene difluoride membranes (Millipore). Membranes were blocked for 1 h with 5% non-fat dry milk (Bio-Rad) or 5% BSA in Tris-buffered saline containing 0.1% Tween 20 (TBS-T), and then incubated overnight at 4 °C with the following primary antibodies: mouse anti-β-actin (1:3000; Sigma-Aldrich); mouse anti-FABP4 (1:500, Santa Cruz Biotechnology); rabbit anti-adiponectin (1:1000; Thermo-Fisher Scientific); rabbit anti-Emilin-2 (1:1000 [45 (link)], antibody specificity shown in Additional file 1: Fig. S2F). After three washes for 10 min in TBS-T, membranes were incubated for 1 h with goat anti-mouse or anti-rabbit horseradish peroxidase-conjugated secondary antibodies (1:1000; Bethyl). After three further washes for 10 min in TBS-T, bands were detected with LiteAblot Extend chemiluminescent substrate (Euroclone), using a ImageQuantLAS 4000 digital imager (GE Healthcare).

Da Ros F., Persano L., Bizzotto D., Michieli M., Braghetta P., Mazzucato M, & Bonaldo P. (2022). Emilin-2 is a component of bone marrow extracellular matrix regulating mesenchymal stem cell differentiation and hematopoietic progenitors. Stem Cell Research & Therapy, 13, 2.

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Western Blot Analysis of E-cadherin and Vimentin

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Frozen tissue fragments from normal and tumor tissues were ground using a mortar and pestle in liquid nitrogen, then lysed in a RIPA buffer with an added fresh protease inhibitor cocktail, sonicated, and centrifuged at 13,000 rpm for 20 min. The protein concentrations were determined by the Bradford assay. Protein aliquots of 30 μg were separated by SDS-PAGE and transferred onto nitrocellulose membranes, which were washed with TBS-T (50-mM Tris-HCl, pH 7.4, 150-mM NaCl, and 0.05% Tween-20); saturated with 5% low fat milk in TBS-T; and then incubated at +4 °C overnight with antibodies against E-cadherin 1:1000 (#3195 Cell Signaling Technology, Danvers, MA, USA), vimentin 1:1000 (#5741 Cell Signaling Technology), or GAPDH 1:10,000 (ab8245 Abcam, Cambridge, UK) in TBS-T. After washing, the membranes were incubated with the appropriate horseradish peroxidase-conjugated secondary antibodies against mouse or rabbit IgG (1:20,000) in TBS-T and developed using the LiteAblot EXTEND chemiluminescent substrate (Euroclone, Milan, Italy). Densitometric analyses were carried out using ImageJ software from the National Institutes of Health (Bethesda, MD, USA).

Baldini E., Tuccilli C., Pironi D., Catania A., Tartaglia F., Di Matteo F.M., Palumbo P., Arcieri S., Mascagni D., Palazzini G., Tripodi D., Maturo A., Vergine M., Tarroni D., Lori E., Ferent I.C., De Vito C., Fallahi P., Antonelli A., Censi S., D’Armiento M., Barollo S., Mian C., Morrone A., D’Andrea V., Sorrenti S, & Ulisse S. (2021). Expression and Clinical Utility of Transcription Factors Involved in Epithelial–Mesenchymal Transition during Thyroid Cancer Progression. Journal of Clinical Medicine, 10(18), 4076.

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Protein Extraction and Western Blot Analysis of Aortic Tissues

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Proteins were extracted from aortas using the ''Total protein extraction kit'' (Merck Millipore) as indicated by the manufacturer, supplemented with protease and phosphatase inhibitors (Roche). Protein samples were quantified with Pierce BCA Protein Assay Kit (23227, ThermoScientific), loaded and separated in pre-cast NuPAGE 10% Bis-Tris Gel (Novex, ThermoScientific) and blotted into PVDF membranes (ThermoScientific). The filters were blocked and incubated with primary and secondary antibodies. Reactive bands were revealed by LiteAblot EXTEND or LiteAblot PLUS (Euroclone), and quantified using the ImageJ software.
Primary antibodies used were: mouse anti-Smad4 (1:200; Santa Cruz); mouse anti-b-actin (1:4000; Sigma Aldrich); rabbit anti-P-Smad2 (1:1,000; Cell Signaling); rabbit anti-P-Smad1/5/8 (1:1,000; Millipore); rabbit anti-P-JNK (1:500; Cell Signaling); rabbit anti-P-p38 (1:1,000 Cell Signaling); rabbit anti-P-ERK1/2 (1:500; Santa Cruz); rabbit anti-P-TAK1 (1:500, Cell Signaling); rabbit anti-TAK1 (1:1000, Bethyl); rabbit anti-RelA/p65 (1:1000; Santa Cruz); rabbit anti-P-(S536)RelA/p65 (1:1,000; Cell Signaling). Secondary antibodies (Bethyl) were used 1:1,000.

Da Ros F., Carnevale R., Cifelli G., Bizzotto D., Casaburo M., Perrotta M., Carnevale L., Vinciguerra I., Fardella S., Iacobucci R., Bressan G.M., Braghetta P., Lembo G, & Carnevale D. (2017). Targeting Interleukin-1β Protects from Aortic Aneurysms Induced by Disrupted Transforming Growth Factor β Signaling. Immunity, 47(5).

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Quantitative Protein Analysis Protocol

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For total cell extracts, cells were lysed in radioimmunoprecipitation assay buffer, sonicated, and centrifuged for 10 minutes at 13,000 rpm at 4 C. Alternatively, nuclear and cytosolic fractions were obtained as described in Martina and Puertollano. 38 Protein concentrations were measured using the Bio-Rad Protein Assay (Bio-Rad Laboratories, Inc., Hercules, CA). Proteins were separated by 12% sodium dodecylsulfate-polyacrylamide gel electrophoresis and immunoblotted onto a nitrocellulose membrane (Whatman Bioscience Ltd., Maidstone, UK). The membrane was blocked with 5% bovine serum albumin in Tris-buffered saline, 0.1% Tween 20 and incubated with primary antibodies anti-Actin (Ambion), anticystinosin (Abnova, Taipei City, Taiwan), anti-glyceraldehyde-3-phosphate dehydrogenase, anti-TFEB, or antihistone H3 (Cell Signaling, Danvers, MA), and with horseradish peroxidase secondary antibody conjugate IgG (Santa Cruz Biotechnology, Inc., Santa Cruz, CA). Immunoblots were developed with LiteAblot EXTEND (EuroClone, Milan, Italy) and acquired with the ChemiDoc XRS System (Bio-Rad).

Rega L.R., Polishchuk E., Montefusco S., Napolitano G., Tozzi G., Zhang J., Bellomo F., Taranta A., Pastore A., Polishchuk R., Piemonte F., Medina D.L., Catz S.D., Ballabio A, & Emma F. (2016). Activation of the transcription factor EB rescues lysosomal abnormalities in cystinotic kidney cells. Kidney international, 89(4).

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