Bovine serum albumin (bsa)

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Bovine serum albumin is a common laboratory-grade protein used in various biological applications. It is derived from bovine (cattle) blood serum and serves as a stabilizing agent, blocking buffer, and nutrient supplement in cell culture, biochemical assays, and other research procedures.

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Lab products found in correlation

2 366 protocols using bovine serum albumin (bsa)

PTEC Immunophenotyping by Flow Cytometry

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The PTEC immunophenotyping was performed by flow cytometry. The cells were detached with 1 mM EDTA solution prepared in PBS (Gibco, Carlsbad, CA, USA), and 3 × 10⁵ PTEC were used for each surface marker analysis. The cells were washed twice with 1 % bovine serum albumin (BSA) (Invitrogen, Carlsbad, CA, USA) in PBS and then incubated with primary monoclonal antibodies: CD13, CD14, CD44, CD45, CD54, and CD90 (Table S1, Supplementary Materials) at 4 °C for 30 min. The cells were washed twice with 1% BSA in PBS and then incubated with goat anti-mouse secondary antibody conjugated with R-phycoerythrin fluorescent dye (PA1-84395, Thermo Scientific, Waltham, MA, USA), diluted 1:25 in 1% BSA prepared in PBS at 4 °C for 30 min. The cells were washed twice and analyzed using the BD FACSCanto™ II system (BD Biosciences, San Jose, CA, USA), measuring 10,000 cells. For the determination of the background fluorescence, the PTEC samples were labeled with anti-mouse isotype controls (ab18413, Abcam, Cambridge, UK). The data were analyzed using Flowing Software (version 2.5.1) (Turku Bioscience, Turku, Finland).

Rinkūnaitė I., Šimoliūnas E., Bironaitė D., Rutkienė R., Bukelskienė V., Meškys R, & Bogomolovas J. (2021). The Effect of a Unique Region of Parvovirus B19 Capsid Protein VP1 on Endothelial Cells. Biomolecules, 11(4), 606.

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Flow Cytometry Analysis of pNF Cells

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Cryopreserved pNF pieces were thawed and digested as previously mentioned to obtain a single-cell suspension. Then, cells were washed with 1% BSA (Sigma) in PBS, incubated for 30 minutes on ice with unconjugated primary antibody p75 (1:1000), washed with 1% BSA in PBS, incubated with Alexa Fluor 488-conjugated secondary antibodies 1:1000 for 30 minutes on ice. Cells were then permeabilized with saponin (Thermo Fisher Scientific) for 10 minutes on ice, incubated with unconjugated primary antibody S100B (1:1000) for 30 minutes on ice, washed with 1% BSA in PBS, incubated with Alexa Fluor 647-conjugated secondary antibodies (Thermo Fisher Scientific) for 30 minutes on ice, washed with 1% BSA in PBS and resuspended in 100 mL of 1% BSA in PBS. Cells were analyzed by flow cytometry using BD LSR Fortessa SORP and BD FACSDiva 6.2 software. Doublets were discarded. At least 100 cells were counted for each p75+/S100B-, p75+/S100B+, p75-/S100B+, and p75-/S100B-cell population.

Mazuelas H., Magallón-Lorenz M., Fernández-Rodríguez J., Uriarte-Arrazola I., Richaud-Patin Y., Terribas E., Villanueva A., Castellanos E., Blanco I., Raya Á., Chojnacki J., Heyn H., Romagosa C., Lázaro C., Gel B., Carrió M, & Serra E. (2022). Modeling iPSC-derived human neurofibroma-like tumors in mice uncovers the heterogeneity of Schwann cells within plexiform neurofibromas. Cell reports, 38(7).

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Cell Sorting Buffer Optimization

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For the sake of brevity only the volumes used for sorting cells in 96-well plates (5 µL/well) are indicated. When miniaturizing the protocol, we decreased the volume of each reaction accordingly.
-Standard Triton Buffer (0.2% Triton final): 0.1 µL Triton X-100 (10% v/v, Sigma-Aldrich), -BSA-Triton Buffer (1 mg/mL BSA + 0.2% Triton): 0.5 µL BSA (10 mg/mL, ThermoFisher Scientific) were added to the Standard Triton Buffer described above.
-BSA Buffer (1 mg/mL BSA final): 0.5 µL BSA (10 mg/mL, ThermoFisher Scientific) were added to the Standard Triton Buffer described above but in this case Triton was not included.
-Guanidine-based Buffer (250 mM final): 0.03125 µL guanidine hydrochloride (8 M, Sigma-Aldrich) were added to the Standard Triton Buffer described above but in this case Triton was not included.
After cell sorting the plates were sealed and immediately stored at -80°C until ready for further processing. Lysed cells can be stored in these conditions for several months without any appreciable decrease in RNA quality. Freeze-thaw cycling should be avoided.

Hahaut V., Pavlinić D., Cowan C.S., & Picelli S. (2021). Lightning Fast and Highly Sensitive Full-Length Single-cell sequencing using FLASH-Seq.

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Transwell Migration Assay for Chemokine-Induced Cell Movement

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Migration assays were performed in 12-well 8μm pore-sized transwell plates (Costar, Corning, NY, USA). Cells were seeded above the filters at a density of 1 × 10⁵ cells/well. The lower compartment was filled with the following media: 10% FBS/0.5% BSA; 200 ng/mL CXCL12/0.5% BSA (PeproTech, Rocky Hill, NJ, USA); 10% FBS/200 ng/mL CXCL12/0.5% BSA and 0.5% BSA was used as negative control. After 24 hours, the number of cells which migrated through the filter and reached the lower compartment was counted. Values were expressed as percentage of the input (cells applied directly to the lower compartment) set as 100%.

Barbutti I., Xavier J.M., Machado-Neto J.A., Ricon L., Traina F., Bohlander S.K., Saad S.T, & Archangelo L.F. (2016). CATS (FAM64A) abnormal expression reduces clonogenicity of hematopoietic cells. Oncotarget, 7(42), 68385-68396.

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Real-time Cell Adhesion Monitoring

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The real-time xCELLigence cell analyser RTCA (Roche
Diagnostics, Germany) was used to measure cell adhesion over time. RTCA measures
the impedance that is expressed as a cell index. Cell index value presents the
impedance between electrodes (bottom sensors). The 96-well E-plate (Roche) was
coated with fibronectin and collagen or 0.1% BSA (Gibco) in PBS, followed by
blocking with 0.1% BSA in PBS, both at 37°C for 1 h. BSA-coated wells
were used as negative controls. siRNA-treated and/or transfected cells (HEK293
or MDA-MB-231) were detached with Hyclone® HyqTase, washed with full
medium including 10% FBS and 20000 cells/well were seeded on E-plates in
serum-free medium. Cell index was measured in real-time.

Lilja J., Zacharchenko T., Georgiadou M., Jacquemet G., De Franceschi N., Peuhu E., Hamidi H., Pouwels J., Martens V., Nia F.H., Beifuss M., Boeckers T., Kreienkamp H.J., Barsukov I.L, & Ivaska J. (2017). SHANK proteins limit integrin activation by directly interacting with Rap1 and R-Ras. Nature cell biology, 19(4), 292-305.

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Real-time Cell Adhesion Monitoring

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Isolation of Stromal Vascular Cells from Mouse Adipose Tissue

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Stromal vascular cells (SVCs) were isolated from epididymal fat pads using a well-established collagenase-based method [39 (link)]. Mouse epididymal fat pads were removed, weighed, and minced in phosphate-buffered saline (PBS, Gibco, Waltham, MA, USA) containing 2% bovine serum albumin (BSA, Gibco, USA). Collagenase type 2 (10 mg/mL, Worthington) and deoxyribonuclease I (2 mg/mL, Roche, Indianapolis, IN, USA) were added to the samples before incubation at 37 °C for 20 min with shaking. Digested adipose tissue was filtered through a 100 μm cell strainer (BD Biosciences, San Diego, CA, USA) to remove non-digested adipose tissue and then added 2% BSA/PBS and 5 mM EDTA. The suspension was centrifuged at 300 g for 5 min, and the pellet was resuspended in 2% FBS (Sigma-Aldrich)/PBS. The suspension was then filtered through a 100 μm nylon mesh to remove unnecessary tissue and centrifuged at 300 g for 5 min. The pellets containing SVCs were resuspended with 2% FBS/PBS, and prepared for staining.

Lee A.G., Kang S., Im S, & Pak Y.K. (2022). Cinnamic Acid Attenuates Peripheral and Hypothalamic Inflammation in High-Fat Diet-Induced Obese Mice. Pharmaceutics, 14(8), 1675.

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Phenotypic Analysis of M2 Macrophages

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Polarized M2 macrophages (0.1x10⁶) were collected and resuspended in staining buffer (PBS supplemented with 0.5% bovine serum albumin (Gibco; Thermo Fisher Scientific, Inc.)) and preincubated with FcR blocking reagent (Miltenyi Biotec, Inc.) for 15 min at 4˚C. Cells were simultaneously stained for 20-40 min at 4˚C with CD209-V450 (cat. no. 561275), CD86-FITC (cat. no. 555657) and CD163-PE (cat. no. 556018; all from BD Biosciences; dilution 1:50), which are markers of M2a, M2b and M2c macrophages, respectively. Cells were washed with staining buffer [PBS supplemented with 0.5% bovine serum albumin (Gibco; Thermo Fisher Scientific, Inc.)] by centrifugation at 1,500 x g, at 4˚C for 5 min and resuspended in PBS supplemented with 1% paraformaldehyde. Finally, phenotypic analysis of M2 macrophages was performed on a flow cytometer (FACScan; BD Biosciences) and the acquired data were analyzed using FlowJo software (v7.6; FlowJo LLC).

Zhao S., Si M., Deng X., Wang D., Kong L, & Zhang Q. (2022). HCV inhibits M2a, M2b and M2c macrophage polarization via HCV core protein engagement with Toll-like receptor 2. Experimental and Therapeutic Medicine, 24(2), 522.

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Quantifying Viral Antibody Responses

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Nunc Maxisorp immunoplates (Fisher Scientific, Pittsburgh, PA) were coated overnight at 4°C with UV-irradiated MHV68 virus stock (740,000 microjoules/cm² × 2; Stratalinker UV Crosslinker 1800 - Agilent Technologies, Santa Clara, CA). Plates were washed five times with PBS-Tween (0.05%), blocked for 1 h with PBS-Tween (0.05%)-bovine serum albumin (3%, Fisher Scientific), incubated with serial 3-fold dilutions of experimental serum in PBS-Tween (0.05%)-bovine serum albumin (0.5%) for 1 h, and washed five times. Bound antibody was detected with horse radish peroxidase-conjugated goat anti-mouse IgM and goat anti-mouse IgG (heavy + light chain) (all from Jackson ImmunoResearch, West Grove,PA) using 3,3′, 5,5′-tetramethylbenzidine substrate (Life Technologies, Gaithersburg, MD). HRP enzymatic activity was stopped by the addition of 1 N HCL (Sigma-Aldrich, St. Louis, MO) and the absorbance read at 450 nm on a model 1420 Victor³V Multilabel Plate Reader (PerkinElmer, Waltham, MA).

Kulinski J.M., Darrah E.J., Broniowska K.A., Mboko W.P., Mounce B.C., Malherbe L.P., Corbett J.A., Gauld S.B, & Tarakanova V.L. (2015). ATM facilitates mouse gammaherpesvirus reactivation from myeloid cells during chronic infection. Virology, 483, 264-274.

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Visualizing YAP1 Localization and Actin Cytoskeleton

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To evaluate YAP1 localization and F-actin cytoskeletal organization, after experimentation cells were immunostained. The cells were fixed with 10% formalin (Sigma Aldrich) for 15 min and rinsed with PBS three times. Cells were then permeabilized for 10 min with 0.1% Triton X-100 (Fisher Scientific) in PBS and rinsed with PBS three times. Cells were blocked for 30 min with 1% bovine serum albumin (Fisher Scientific) in PBST (0.1% (v/v) Tween 20 (Fisher Scientific) in PBS). Following blocking, cells were incubated with anti-YAP1 [EP1674Y] monoclonal antibody (ab52771, abcam) diluted 1:500 in l% bovine serum albumin in PBST overnight at 4 °C. Cells were then rinsed four times with PBS. Afterward, cell cytoskeletal F-actin was stained with Texas Red labeled phalloidin (Invitrogen) diluted in 1% bovine serum albumin (Fisher Scientific) in 0.1% Tween 20 (Fisher Scientific) in PBS following the manufacturer’s instructions. In this same solution, anti-rabbit AlexaFluor 488 tagged secondary antibody (ab150077, abcam) was added at a dilution of 1:500. Incubation with the phalloidin and secondary antibody was for 1 h at room-temperature followed by five rinses with PBS. The CCR region of the chamber was then excised from the chamber and mounted using ProLong Diamond Antifade Mountant with DAPI (Invitrogen) onto a glass slide (ThermoFisher Scientific).

James B.D, & Allen J.B. (2021). Sex-Specific Response to Combinations of Shear Stress and Substrate Stiffness by Endothelial Cells In Vitro. Advanced healthcare materials, 10(18), e2100735.

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