Bovine serum albumine (bsa)

Manufactured by Merck Group

Sourced in United States, Germany

Bovine serum albumin (BSA) is a protein commonly used in various laboratory applications. It is derived from bovine (cattle) blood serum and is a purified, water-soluble protein. BSA is often used as a blocking agent, stabilizer, or carrier protein in biochemical and immunological assays.

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Bovine serum (80 citations)

51 protocols using bovine serum albumine (bsa)

Cell Culture Reagents and Antibodies

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Dulbecco’s modified Eagle’s medium (DMEM), fetal bovine serum (FBS), penicillin and streptomycin, L-glutamine were obtained from GIBCO (Paisley, Scotland). DNase 1, gelatin, lypopolysaccharide (LPS), 1,10 phenanthroline (PA), poly-L-lysine (PLL), trypsin, trypan blue, 3-(4,5-dimethylthiazol-2-yl)-2,5 diphenyltetrazolium bromide (MTT), phorbol 12-myristate 13-acetate, bovine serum albumine was provided by Sigma (St. Louis, MO, USA). Glial fibrillary acidic protein (GFAP) antibodies were purchased from Serotec (Oxford, UK). Standard proteins, G-250and R-250 coomassie brilliant blue were purchased from Bio-Rad (Hercules, CA, USA). Purified MMP-2 and MMP-9 were purchased from Alexis Biochemicals (San Diego, CA, USA). Primer pairs specific for MMP-2, MMP-9 and 18S were from Sigma Genosys (Cambridge, UK). RNeasy mini kit and QuantiTect Reverse Transcription were from Qiagen (Valencia, CA, USA). Antibodies against extracellular–regulated protein kinases (ERK) 1/2, and phosporilated ERK 1/2 (p-ERK 1/2) were from Santa Cruz Biotechnology (Santa Cruz, CA). Hybond-P PVDF membranes, enhanced chemiluminescence (ECL) Western Blotting Analysis System and anti-mouse-HRP secondary antibody were from GE Healthcare Life Sciences (Little Chalfont, Buckinghamshire, UK).

Di Bari G., Gentile E., Latronico T., Corriero G., Fasano A., Nonnis Marzano C, & Liuzzi G.M. (2015). Inhibitory Effect of Aqueous Extracts from Marine Sponges on the Activity and Expression of Gelatinases A (MMP-2) and B (MMP-9) in Rat Astrocyte Cultures. PLoS ONE, 10(6), e0129322.

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Western Blot Analysis of GBM CSCs

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Lysates from GBM CSCs and GCLs were homogenized in 10× volume of RIPA lysis buffer. Proteins were separated by electrophoresis on 8–10% polyacrilamide (Sigma, St. Louis, MO) gels and transferred onto trans-blot nitrocellulose membranes (Amersham). Primary antibodies were diluted in 3% bovine serum albumine (Sigma) in TBS-T, and incubated with the membranes overnight at 4 °C. The primary antibody was removed, and the blots were washed in TBS-T and then incubated for 1 h at room temperature in horseradish peroxidase-conjugated secondary antibodies (Amersham). Reactive proteins were visualized using LiteBlot (Euroclone, Padriciano, Italy) or SuperSignal West Femto chemiluminescence reagent (Pierce Biotechnology, Rockford, IL) and exposure to X-ray film (BioMax MR; Kodak, Rochester, NY). For NanoPro assay, all isoelectric separations were performed on the NanoPro 1000 (ProteinSimple, Santa Clara, CA, USA) with the Premix Generation 2 pH 3–10 separation mix. Details can be found in Supplementary Methods.

Narayanan A., Gagliardi F., Gallotti A.L., Mazzoleni S., Cominelli M., Fagnocchi L., Pala M., Piras I.S., Zordan P., Moretta N., Tratta E., Brugnara G., Altabella L., Bozzuto G., Gorombei P., Molinari A., Padua R.A., Bulfone A., Politi L.S., Falini A., Castellano A., Mortini P., Zippo A., Poliani P.L, & Galli R. (2018). The proneural gene ASCL1 governs the transcriptional subgroup affiliation in glioblastoma stem cells by directly repressing the mesenchymal gene NDRG1. Cell Death and Differentiation, 26(9), 1813-1831.

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Western Blot and Immunofluorescence Protocol

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Cells were lysed in a solution containing 50 mM Tris pH 7.5, 150 mM NaCl, 1% Triton X-100, 5 mM EDTA and a cocktail of protease inhibitors^{48 (link)}. Proteins were separated in 10–15% sodium dodecyl sulfate polyacrylamide gel electrophoresis (SDS-PAGE) gels, and transferred to nitro-cellulose membrane (hybond C-Extra, Amersham Biosciences). After blocking with 5% non-fat milk in PBS-0.05% Tween, membranes were incubated with primary and HRP-secondary antibodies and the signals detected by Chemiluminescent substrate HRP (Thermofisher, Millipore) using a conventional developer or a digital detection system (ChemiDoc, Biorad). Alternatively, fluorescent-labelled secondary antibodies were used and detection was performed thanks to the Odyssey® CLx imaging system (LI-COR). Uncropped scans of immunoblots are included as Supplementary Fig. 5. For immunofluorescence, cells were fixed with 4% Paraformaldehyde (PFA) for 15 min Blocking and permeabilisation were performed in PBS/0.1%Triton, 4% Bovine Serum Albumine (Sigma), 4% Donkey Serum (Sigma) for 1 h at room temperature. Subsequently primary antibodies, diluted in blocking buffer was incubated overnight at 4 °C. Following washes with PBS/0.1%Triton, secondary antibodies was incubated for 1 h at room temperature, and mounted in Mowiol solution (Sigma, 81381).

Scrivo A., Codogno P, & Bomont P. (2019). Gigaxonin E3 ligase governs ATG16L1 turnover to control autophagosome production. Nature Communications, 10, 780.

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Western Blot Protein Detection

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Cells and tissues were homogenized and lysed in a custom made total protein lysis buffer (50 mM Tris HCl, pH 7.5, 150 mM NaCl, 0.1% SDS, 1% deoxycholate, 1% Triton X-100) containing a protease and phosphatase inhibitor cocktail (Roche, Basel, Switzerland). Protein concentrations were measured by a bicinchoninic acid (BCA) assay (Pierce), and 30 mg protein was loaded per lane for all the immunoblots. The protein lysates were fractionated by electrophoresis using NuPAGE Novex 4-12% Bis-Tris Gel (Invitrogen) and transblotted to nitrocellulose membranes using the XCell II Blot Module (Invitrogen). Adequate sample transfer was confirmed by staining the blot with Ponseau S solution (Sigma). Thereafter the membranes were blocked with 5% bovine serum albumine (Sigma) for 60 min, before immunoblotting overnight with the primary antibody. The immobilized antibody was detected using a horseradish peroxidase-conjugated secondary antibody and stained with SuperSignal West Pico Chemiluminescent Substrate (Thermo Scientific). The immunoreaction was visualized using a LAS-3000 imaging system (FujiFilm, Tokyo, Japan). Immunoblots for actin were made for all samples to assure equal protein loading. The western blot protein bands were compared by automated densitometry using Image J software (NIH, USA).

Steinskog E.S., Sagstad S.J., Wagner M., Karlsen T.V., Yang N., Markhus C.E., Yndestad S., Wiig H, & Eikesdal H.P. (2016). Impaired lymphatic function accelerates cancer growth. Oncotarget, 7(29), 45789-45802.

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Biophysical Characterization of Molecular Interactions

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Bovine serum albumine (fatty acid-free; LOT number: SLCB1005), hen egg-white lysozyme (LOT number: K49054981), sodium polystyrene sulfonate (average molecular weight 70,000 g/mol), polyethylene glycols with an average molecular weight of 400 g/mol (PEG-400) and 3000 g/mol (PEG-3000), sucrose, sucralose, and NaI (>99%) were purchased from Sigma Aldrich, Burlington, MA, USA. Alkaline metal salts of >99% purity (NaCl, NaBr), concentrated acetic acid (CH₃COOH), sodium acetate (CH₃COONa), and 1

mol / L

NaOH solution were purchased from Merck KGaA. Polyethylene glycol with an average molecular weight of 20,000 g/mol (PEG-20000) was obtained from Fluka.

Simončič M, & Lukšič M. (2022). Modulating Role of Co-Solutes in Complexation between Bovine Serum Albumin and Sodium Polystyrene Sulfonate. Polymers, 14(6), 1245.

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Determination of Sugars and Proteins

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All reagents, standards and solvents were of analytical grade. Glucose monohydrate and bovine serum albumine used for the determination of sugars and proteins were purchased from Sigma Aldrich (Steinheim, Germany). Petroleum ether, sulfuric acid, copper sulphate, potassium iodide, potassium sodium tartarate and sodium hydroxide were purchased from Kefo (Zagreb, Croatia). Phenol was provided by Acros Organics (Geel, Belgium). Deionized water used for the preparation of reagents, standards and solvents was obtained using the Millipore Milli-Q instrument.

Grassino A.N., Karlović S., Šošo L., Dujmić F., Sabolović M.B., Marelja M, & Brnčić M. (2024). Influence of Different Drying Processes on the Chemical and Texture Profile of Cucurbita maxima Pulp. Foods, 13(4), 520.

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Immunofluorescent Staining of Muscle Sections

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Immunofluorescent staining was carried out on frozen muscle sections (10 μm). In summary, sections were incubated for 60 min at room temperature with BSA (Bovine Serum Albumine, Sigma Aldrich, Saint-Quentin-Fallavier, France) diluted to 3% in PBS (Phosphate Buffered Saline, Sigma Aldrich). They were then incubated for 60 min with a primary antibody cocktail containing FNDC5 (1:200, ab174833, Abcam) and MHC I or MHC IIA antibodies (1:200, BA-D5 or SC-71, respectively, DSHB) at 37 °C, followed by three rinses. Fluorescence-conjugated secondary antibodies (Alexa Fluor 488 and Alexa fluor 555 (1:250, A11008 and A21422, respectively, Thermofischer, Villebon-sur-Yvette, France) or Alexa fluor 647 (1:250, 1090-31, Southern Biotech, Clinisciences, Nanterre, France)) were applied for 30 min at 37 °C in obscurity, followed by three rinses. Finally, the sections were mounted in ProLong Gold Antifade Mountant (P36934, Invitrogen, Villebon-sur-Yvette, France) and coverslipped. Images were acquired using a Leica DMI8 inverted microscope, fitted with an automated motorized platform for mosaic imaging with the LAS X software (https://imillermicroscopes.com/pages/software-download accessed on 4 February 2024, Leica, Nanterre, France).

Dupuis O., Girardie J., Van Gaever M., Garnier P., Coq J.O., Canu M.H, & Dupont E. (2024). Early Movement Restriction Affects FNDC5/Irisin and BDNF Levels in Rat Muscle and Brain. International Journal of Molecular Sciences, 25(7), 3918.

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Electrochemical Analysis of Biosensing Materials

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3,4-Ethylenedioxythiophene (EDOT, 97%), Poly(sodium 4-styrenesulfonate) (PSS), Gold (III) chloride solution (HAuCl₄, 99%) and bovine serum albumine (BSA, ≥98%) were purchased from Sigma-Aldrich. Chloride potassium, disodium hydrogen phosphate, potassium phosphate monobasic, potassium hexacyanoferrate (II) trihydrate, potassium hexacyanoferrate (III) were acquired from Neon. Sodium chloride was obtained from Anidrol. All chemicals were used as received. The solutions were prepared using deionized water by Elga Purelab Flex method (18.2 MΩ.cm).
PBS buffer at pH 7.2 was prepared mixing NaCl 137.0 mmol L ⁻ ¹, KCl 2.7 mmol L ⁻ ¹, Na₂HPO₄ 10 mmol L ⁻ ¹ and KH₂PO₄ 2.0 mmol L ⁻ ¹. PBS buffer was used for biological samples dissolution and as electrolyte for electrochemical tests.
All electrochemical procedures were performed in a DropSens μStat-i-400 s and DropView 8400 software. A three-electrodes setup consisting of a steel mesh (geometric area of 0.5 cm²), platinum wire and Ag/AgCl/Cl⁻_sat as working, counter and reference electrodes, respectively, was used for all procedures.

Lorenzen A.L., dos Santos A.M., dos Santos L.P., da Silva Pinto L., Conceição F.R, & Wolfart F. (2021). PEDOT-AuNPs-based impedimetric immunosensor for the detection of SARS-CoV-2 antibodies. Electrochimica Acta, 404, 139757.

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Cell Fractionation and Enzymatic Assays

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Upon reaching an exponential growth phase, a 50 ml culture volume was subject to cell fractionation. Cells were harvested, washed twice with 50 mM Tris–HCl (pH 8.0), and re-suspended in 10 mM Tris–HCl (pH 8.0), 500 mM sucrose, and 3 mM ethylenediaminetetraacetic acid (EDTA). Lysozyme (chicken egg white, EC 3.2.1.17) at 0.2 mg ml⁻¹ final concentration and a few grains of DNase I (bovine pancreas, EC 3.1.21.1) were added. This mixture was incubated after shaking for 30 min at 30°C. The sphaeroplasts formed were harvested by centrifugation (13 000×g) for 15 min at 4°C and the periplasm was recovered. Sphaeroplasts were re-suspended in a volume of 10 ml in 100 mM Tris–HCl (pH 8.0) and disrupted by sonication, and cytoplasmic and membrane fractions were separated by ultracentrifugation (40 000×g). Assimilatory NADH-dependent nitrate reductase activity was assayed in cytoplasmic fractions in the presence of NADH as an electron donor by measuring the nitrite formed from nitrate [35 ]. β-Galactosidase activity was determined spectrophotometrically, as previously described [36 ]. Protein concentration was measured using a Bradford protein assay kit (Bio-Rad, U.K.) with bovine serum albumine as standard (Fraction V, Sigma, U.K.).

Luque-Almagro V.M., Manso I., Sullivan M.J., Rowley G., Ferguson S.J., Moreno-Vivián C., Richardson D.J., Gates A.J, & Roldán M.D. (2017). Transcriptional and translational adaptation to aerobic nitrate anabolism in the denitrifier Paracoccus denitrificans. Biochemical Journal, 474(11), 1769-1787.

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Isolation and Analysis of Neuronal F-Actin

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F-actin was isolated from cerebral cortices (E17.5) or neuronal cell cultures (E14+5DIV) after modification of a published protocol 37 (link). Four cortices for each condition were dissected and transferred into 1 ml of homogenization buffer (100 mM Na₂HPO4 – 100 mM NaH₂PO4 at pH 7.2, 2 mM ATP, 2 mM MgCl₂, 0.1% Triton X-100) containing phosphatase and protease inhibitor cocktails (Sigma). For analysis on cultures, 16 wells of 24-well plates were pooled for each condition. When needed, cells were incubated for 10 min with 10 μM of the calcium ionophore A23187 (Tocris) before the lysis. Neurons were then lysed and homogenized, like tissues, at 4°C into 1 ml of homogenization buffer by pipetting up and down using a 18G needle. Biotinylated phalloidin (1 unit for each condition, Invitrogen) was then added to homogenates and incubated under rotation for 1 h at room temperature. In parallel, streptavidin-coated magnetic beads (50μl for each condition; Invitrogen) were blocked for 30 min in PBS (Sigma) with 5% bovine serum albumine (Sigma), washed and added to homogenates with biotinylated phallodin for 1 h at room temperature. The precipitated material was then washed five times with homogenization buffer, resuspended in 1X laemmli sample buffer (Bio-Rad) and analyzed by western blotting using primary antibodies against actin and CaMKIIβ according to the protocol described below.

Nicole O., Bell D.M., Leste-Lasserre T., Doat H., Guillemot F, & Pacary E. (2018). A novel role for CAMKIIβ in the regulation of cortical neuron migration: implications for neurodevelopmental disorders. Molecular psychiatry, 23(11), 2209-2226.

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