Kaleidoscope

Manufactured by Bio-Rad

Sourced in United States

The Kaleidoscope is a versatile laboratory instrument used for the analysis and visualization of various biological and chemical samples. It is designed to provide high-quality images and data related to the properties and characteristics of the samples under investigation.

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Lab products found in correlation

Nupage novex 4 12 bis tris gel, by Thermo Fisher Scientific (2 mentions) Nitrocellulose membrane, by Thermo Fisher Scientific (2 mentions) Ecl western blot detection kit, by Cytiva (1 mentions) Mini trans blot, by Bio-Rad (1 mentions) Horseradish peroxidase, by Merck Group (1 mentions) Bca kit, by Merck Group (1 mentions) Enhanced chemiluminescence kit, by Merck Group (1 mentions) Image studio lite, by LI COR (1 mentions) Glycerol, by Bio-Rad (1 mentions) Glycine, by Bio-Rad (1 mentions) Bis ans, by Thermo Fisher Scientific (1 mentions) Acrylamide, by Bio-Rad (1 mentions) Chelex 100, by Merck Group (1 mentions) Direct q 3 system, by Merck Group (1 mentions) Amicon ultra centrifugal filter, by Merck Group (1 mentions) Ripa buffer, by Merck Group (1 mentions) Odyssey blocking buffer, by LI COR (1 mentions) Odyssey scanner, by LI COR (1 mentions) Complete mini edta free protease inhibitor cocktail, by Roche (1 mentions) Amersham hyperfilm ecl, by GE Healthcare (1 mentions)

12 protocols using kaleidoscope

Identification of Fungal Laccase Isoenzymes

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To identify the number of isoenzymes involved in Cu²⁺ induction, the crude enzyme was subjected to native polyacrylamide gel electrophoresis (ND-PAGE) and denaturing polyacrylamide gel electrophoresis (SDS-PAGE) in 7.5% gels. After resolving the proteins using ND-PAGE, the gel was incubated in 0.1 M sodium acetate buffer containing 5 mM DMP before detecting laccase activity.¹⁸ After incubating the gel for 5 min, the dye solution was discarded; the gel was immediately scanned using a scanner (HP Deskjet F300 All-in-One series).
The molecular weight of the isoenzymes was evaluated using 7.5% SDS-PAGE including a molecular weight marker (Kaleidoscope, BioRad). SDS was removed by incubating the gel in 50 mM sodium acetate containing 0.2% Triton X-100 and then staining with 5 mM DMP to detect laccase activity.¹⁹

Fonseca M.I., Tejerina M.R., Sawostjanik-Afanasiuk S.S., Giorgio E.M., Barchuk M.L., Zapata P.D, & Villalba L.L. (2016). Preliminary studies of new strains of Trametes sp. from Argentina for laccase production ability. Brazilian Journal of Microbiology, 47(2), 287-297.

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Quantitative Western Blot Analysis of PAFR and PKA-Cα

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Proteins were subjected to Coomassie blue quantification before use in western blotting with some modification of published methods (Ibe et al. 2000, 2002, 2007). Proteins were suspended in sodium dodecyl sulfate (SDS) sample buffer, pH 6.8, containing: 125 mmol/L Tris‐base, 4% SDS, 0.006% bromophenol blue, 36 mmol/L EDTA, 90 mmol/L DTT, 10% glycerol, 10% beta‐mercaptoethanol. Proteins were loaded on each sample per lane and subjected to SDS‐PAGE gel electrophoresis for 1 h at 200V on 4–12% Tris‐glycine gradient gels (Lonza, Rockland, ME), along with Bio‐Rad kaleidoscope prestained molecular weight markers and protein standards. After 1 h of SDS‐PAGE, proteins were transferred to nitrocellulose membrane by means of mini Trans‐Blot, (Bio‐Rad, Irvine, CA) at 70V and then blocked with 5% nonfat dry milk in 1% T‐TBS overnight. Blots were then incubated for 2–4 with the specific antibody, for instance, 1:500 of PAFR antibody; then, each antibody was washed with 1% T‐TBS, incubated for 1 h with an anti‐rabbit Ig HRP‐linked secondary antibody (Amersham), followed by three more washes with 1% T‐TBS. The signals were developed for 1 min using Amersham ECL Western Blot detection kit and then exposed to X‐ray film. Bands corresponding to PAFR and PKA‐Cα proteins were scanned and quantified.

Hanouni M., Bernal G., McBride S., Narvaez V.R, & Ibe B.O. (2016). Hypoxia and hyperoxia potentiate PAF receptor‐mediated effects in newborn ovine pulmonary arterial smooth muscle cells: significance in oxygen therapy of PPHN. Physiological Reports, 4(12), e12840.

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Western Blotting of Protein Markers

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A previously described protocol was used for the western blotting[22 (link)] of selected proteins for validation. Briefly, 15μl of each effusion sample was separated by electrophoresis on NuPAGE Novex 4–12% Bis-Tris gels (Life technologies, Carlsbad, CA). The molecular weight marker Kaleidoscope was used as a standard (Bio-Rad, Hercules, CA). The proteins were then transferred to a nitrocellulose membrane (Invitrogen). Membranes were blocked with 5% non-fat dry milk in PBS with 0.05% Tween-20 (PBST), and incubated used to incubate primary anti-mouse antibodies for Plakoglobin (PG-11E4, Thermo Scientific, Waltham, MA), periplakin (C-20, Santa Cruz, Dallas, TX), Histone H1 (C-17, Santa Cruz, Dallas, TX), keratin 10 (K-14, Santa Cruz, Dallas, TX), keratin 15 (G-12, Santa Cruz, Dallas, TX). Secondary antibody anti-goat at 1:5000 coupled to horseradish peroxidase (SigmaAldrich, St. Louis, MO). Detection was performed with a SuperSignal® West Dura Extended Duration Substrate kit (Pierce, Rockland, IL) according to the manufacturer’s instructions.

Val S., Burgett K., Brown K.J, & Preciado D. (2016). SuperSILAC Quantitative Proteome Profiling of Murine Middle Ear Epithelial Cell Remodeling with NTHi. PLoS ONE, 11(2), e0148612.

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SDS-PAGE Analysis of VP1 Protein

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The VP1 protein was analyzed by SDS-PAGE under reduced and denatured conditions. The VP1 protein samples (10 µg) were mixed with buffer (v/v; 80 mM Tris-HCl, pH 6.8, 12% glycerol (v/v), 2% SDS (w/v), 5% β-mercaptoethanol (v/v), and 0.05% bromophenol blue (w/v)), and after boiling for a duration of 3 min, they were loaded into 12% Bis–Tris gel and run at 150 V, 15 mA for 40 min. The gels were stained with Coomassie Blue stain to visualize proteins, and Kaleidoscope^® (Bio-Rad) prestained protein standards were used to monitor the electrophoresis of the assayed VP1 protein.

dos Santos G.M., Alves C.R., Pinto M.A., Amado Leon L.A, & Souza-Silva F. (2021). Detection of Antibodies against Hepatitis A Virus (HAV) by a Surface Plasmon Resonance (SPR) Biosensor: A New Diagnosis Tool Based on the Major HAV Capsid Protein VP1 (SPR-HAVP1). Sensors (Basel, Switzerland), 21(9), 3167.

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SDS-PAGE and Blue Native Protein Visualization

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Samples were reduced with dithiothreitol or tris(2-carboxyethyl)phosphine and analyzed by SDS PAGE using tris-glycine 10–20% acrylamide gels (Life Technologies) with bovine complex I and a molecular weight ladder (Kaleidoscope, Bio-Rad) for comparison. Mitochondria from U2OS cells were analyzed by Blue Native PAGE (3–12% acrylamide gels, Life Technologies) at 4 °C according to the manufacturers instructions; after 1 h the standard cathode buffer was replaced with one containing 10% of the Coomassie concentration. All gels were stained with Coomassie R-250.

Bridges H.R., Mohammed K., Harbour M.E, & Hirst J. (2017). Subunit NDUFV3 is present in two distinct isoforms in mammalian complex I. Biochimica et Biophysica Acta, 1858(3), 197-207.

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Western Blot Analysis of Protein Expression

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Proteins were extracted using RIPA buffer (50 mM Tris·HCl pH 7.4, 150 mM NaCl, 5 mM EDTA, 5 mM MgCl₂, 0.05% NP-40, 1% sodium deoxycholate, 1% Triton X-100, 0.1% SDS supplemented with anti-phosphatase 1X and anti-protease cocktail 1X (Sigma-Aldrich)). Cell extract was then sonicated and heated during 5 minutes at 95° C. Protein extracts were dosed using BCA kit (Sigma-Aldrich). Samples were then subjected to SDS-PAGE and Western blot analysis as described previously [91 (link), 92 (link)]. The blots were treated with primary antibody solutions overnight then for 1 hour with secondary HRP-conjugated antibody and developed with enhanced chemiluminescence kit (Merck Millipore). The apparent molecular weight was estimated according to the position of prestained protein markers (Kaleidoscope; Bio-Rad). The density of β-actin served as an internal loading control and levels of protein expression were quantified by GeneTools image analysis 4.3.5 Software.

Cabanas H., Harnois T., Magaud C., Cousin L., Constantin B., Bourmeyster N, & Déliot N. (2018). Deregulation of calcium homeostasis in Bcr-Abl-dependent chronic myeloid leukemia. Oncotarget, 9(41), 26309-26327.

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Protein Expression Analysis by Western Blot

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The cytoplasmic muscle fraction was used for western blot analysis. 15 µg of protein was loaded on the gel, and proteins were transferred onto PVDF membrane. Kaleidoscope (Bio‐Rad) was used as a molecular weight marker. Blots were incubated overnight with the primary antibodies found in the Supporting Information. Blots were then washed with TBST (3 × 5 min), incubated with anti‐rabbit, HRP‐conjugated secondary antibody, washed with TBST (3 × 5 min) and TBS (2 × 5 min) and detected via chemiluminescence (West Femto, Thermo Scientific). Images were obtained with a UVP bioimaging system, and densitometry was analyzed using Image Studio Lite (version 5.2; Licor).

Konopka A.R., Laurin J.L., Schoenberg H.M., Reid J.J., Castor W.M., Wolff C.A., Musci R.V., Safairad O.D., Linden M.A., Biela L.M., Bailey S.M., Hamilton K.L, & Miller B.F. (2018). Metformin inhibits mitochondrial adaptations to aerobic exercise training in older adults. Aging Cell, 18(1), e12880.

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Protein Purification and Analysis Protocol

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Amicon ultra centrifugal filters were obtained from Merck-Millipore (Merck Millipore, Germany). Bis-ANS (4,4'-dianilino-1,1'-binaphthyl-5,5'-disulfonic acid, dipotassium Salt) and iodoacetamide-fluorescein (IAF) were from Molecular Probe (Life Technologies do Brasil Ltda). Bromophenol blue, tetramethylethylenediamine (TEMED), molecular weight marker Kaleidoscope, glycerol, glycine, acrylamide were obtained from Bio-Rad Laboratories (CA, USA). Acids and solvents (HPLC grade) were from J.T. Baker (Avantor Performance Materials, Mexico). All other reagents were from Sigma (St. Louis, MO). All aqueous solutions were prepared with ultrapure water purified by a Direct-Q3 system (Merck Millipore, Germany) and treated with Chelex 100 before use.

Appolinário P.P., Medinas D.B., Chaves-Filho A.B., Genaro-Mattos T.C., Cussiol J.R., Netto L.E., Augusto O, & Miyamoto S. (2015). Oligomerization of Cu,Zn-Superoxide Dismutase (SOD1) by Docosahexaenoic Acid and Its Hydroperoxides In Vitro: Aggregation Dependence on Fatty Acid Unsaturation and Thiols. PLoS ONE, 10(4), e0125146.

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Western Blot Analysis of Exosome Proteins

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A previously described protocol was used for western blotting (27 (link)). Ten microliters of isolated vesicles from each sample were mixed with 20 µl of RIPA buffer (SigmaAldrich, St. Louis, MO) and incubated at room temperature to liberate exosome proteins. They were mixed with Laemmli buffer and placed at 95 °C for 10 min. Samples were then separated by electrophoresis on NuPAGE Novex 4–12% Bis-Tris gels (Life Technologies, Carlsbad, CA). The molecular weight marker Kaleidoscope was used as a standard (Bio-Rad, Hercules, CA). Proteins were then transferred to a nitrocellulose membrane (Life Technologies). Membranes were blocked with 5% non-fat dry milk in PBS with 0.05% Tween-20 (PBST), and incubated with the rabbit HSP70 antibody (System Biosciences) at 1:5,000 and rabbit CD63 antibody (Systems Biosciences) at 1:5,000. A secondary antibody anti-rabbit at 1:10,000 coupled to horseradish peroxidase (System Biosciences). Detection was performed with a SuperSignal West Dura Extended Duration Substrate kit (Pierce, Rockland, IL) according to the manufacturer’s instructions.

Val S., Jeong S., Poley M., Krueger A., Nino G., Brown K, & Preciado D. (2017). Purification and characterization of microRNAs within middle ear fluid exosomes: implication in otitis media pathophysiology. Pediatric research, 81(6), 911-918.

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Western Blot Analysis of Folate Receptor and TS

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The culture medium of the cells in log phase was collected in 15 mL-tubes and centrifuged to collect the suspended cells. The detached cells were washed twice with cold PBS and harvested on ice with 200 μL of lysis buffer containing 1% Triton X-100, 150 mM NaCl, 0.5% sodium deoxycholate, 0.1% SDS in 50 mM Tris, pH 8.0. To inhibit the proteasome degradation of proteins, a tablet of complete mini EDTA free protease inhibitor cocktail (Roche) was added in the lysis buffer. The extract was incubated on ice for 20 min, passed through a 25-gauge needle, and finally centrifuged at 15,000 × g for 20 min at 4 °C. The supernatant was removed in a 1.5 mL tube, and protein concentration was measured by using a BCA protein kit. A protein sample of 50 μg was loaded and electrophoresed on 10% SDS-polyacrylamide gels. Size standards from 10-250 kDa (BioRad Kaleidoscope) were included. Polypeptides were electro-transferred to nitrocellulose membranes. The membranes were blocked with Odyssey^™ blocking buffer (Li-Cor) and probed with anti-human folate receptor or anti-human TSase antibody (Santa Cruz Biotechnology). For visualization, antispecies secondary antibodies labeled with AlexaFluor680 or AlexFluor800 were used. The membranes were blotted on a Li-Cor Odyssey scanner.

Nilaweera T.D., Saeed M, & Kohen A. (2015). Targeting the de novo Biosynthesis of Thymidylate for the Development of PET Probe for Pancreatic Cancer Imaging. Biochemistry, 54(5), 1287-1293.

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