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Bovine serum albumin (bsa)

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Bovine serum albumin is a protein derived from the serum of cattle. It is commonly used in various laboratory applications as a stabilizer, blocking agent, and cell culture supplement.

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Lab products found in correlation

Ripa buffer, by Thermo Fisher Scientific (3 mentions) Non fat dry milk, by Bio-Rad (2 mentions) Dc assay, by Bio-Rad (2 mentions) Chemidoc mp imaging system, by Bio-Rad (2 mentions) Protease and phosphatase inhibitor, by Thermo Fisher Scientific (2 mentions) Collagenase type 1, by Worthington (2 mentions) Fluoromount g with dapi, by Electron Microscopy Sciences (1 mentions) Triton x 100, by Merck Group (1 mentions) Lsm 780, by Zeiss (1 mentions) Ruthenium red, by Merck Group (1 mentions) Arsenazo 3, by Merck Group (1 mentions) Calcium green 5n, by Thermo Fisher Scientific (1 mentions) Hydrogen peroxide, by Honeywell (1 mentions) Biogel p6 resin, by Bio-Rad (1 mentions) Isopropyl β d 1 thiogalactopyranoside (iptg), by Thermo Fisher Scientific (1 mentions) Fluoro carbonyl cyanide phenylhydrazone (fccp), by Merck Group (1 mentions) Thiostrepton, by Merck Group (1 mentions) Glucose 6 phosphate dehydrogenase, by Thermo Fisher Scientific (1 mentions) Glucose 6 phosphate (g6p), by Thermo Fisher Scientific (1 mentions) Gentian violet, by Merck Group (1 mentions)

22 protocols using bovine serum albumin (bsa)

1

Immunofluorescence Staining of HeLa Cells

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At 24 h after transfection, HeLa cells were washed with PBS and treated for 12 min with 4% paraformaldehyde (Electron Microscopy Sciences, 15714-S) in PBS. Coverslips were washed twice for 5 min in PBS and permeabilized for 15 min in 0.2% Triton X-100 (Sigma, T8787). Cells were blocked for 30 min in 0.2% bovine serum albumin (GoldBio, A-421) in PBS (blocking solution) and stained for 30 min with primary antibodies in blocking solution at 37°C. Coverslips were then washed twice with PBS and incubated for 30 min at 37°C with secondary Alexa–conjugated antibodies in blocking solution. Coverslips were again washed twice with PBS and mounted on slides using Fluoromount-G with DAPI (Electron Microscopy Sciences, 17984-24). Images were acquired on an inverted confocal laser-scanning microscope (LSM780; Carl Zeiss) fitted with a 63×, 1.4 NA objective. Images were processed in ImageJ (Schneider et al., 2012 (link)).
Guardia C.M., Jain A., Mattera R., Friefeld A., Li Y, & Bonifacino J.S. (2021). RUSC2 and WDR47 oppositely regulate kinesin–1-dependent distribution of ATG9A to the cell periphery. Molecular Biology of the Cell, 32(21), ar25.
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2

Mitochondrial Calcium Regulation Assay

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All the chemicals used were analytic grade. Sucrose (S0389), CaCl2 (C5080), succinic acid (S7501), L‐glutamic acid (G12519), malic acid (M0625), EGTA (E0396), ADP (01905), safranine‐O (S2255), and Arsenazo III (A92775) were from Sigma Chem Co (MO, USA). Bovine serum albumin was from GoldBio (E217100, MO, USA). H3PO4, KCl and MgCl2 were from J.T. Baker Chemical Co. (NJ., USA), Ruthenium red was from Merck KGaA (R2751, Darmstadt, Germany). Cyclosporin A was from Sandimmum (Sandoz, Basilea, Swiss). Calcium Green‐5N was from Thermo Fisher Scientific (C3737 MA, USA).
Ricardez‐Garcia C., Reyes‐Becerril M., Mosqueda‐Martinez E., Mendez‐Romero O., Ruiz‐Ramírez A, & Uribe‐Carvajal S. (2024). Tissue‐specific differences in Ca2+ sensitivity of the mitochondrial permeability transition pore (PTP). Experiments in male rat liver and heart. Physiological Reports, 12(10), e16056.
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3

Proteomic Analysis of Redox Processes

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Thiostrepton (Millipore, Burlington, MA, USA), Gentian Violet (Sigma, St. Louis, MO, USA), 2-[2-[4-(trifluoromethoxy)phenyl]hydrazinylidene]-propanedinitrile (FCCP, Sigma), S-Methyl Methanethiosulfonate (MMTS, TCI Chemicals, Portland, OR, USA), Bovine Serum Albumin (BSA, GOLDBIO, St. Louis, MO, USA), TCEP (Fisher, Waltham, MA, USA), DTT (Fisher) Optima HPLC grade water (Fisher), hydrogen peroxide (Honeywell, Charlotte, NC, USA), NADPH (Roche, Basel, Switzerland), IPTG (Fisher), glucose 6-phosphate dehydrogenase (Alfa Aesar, Haverhill, MA, USA), glucose 6-phosphate (ACROS Organics, Morris Plains, NJ, USA), BioGel P6 Resin (BioRad, Hercules, CA, USA).
Nelson K.J., Messier T., Milczarek S., Saaman A., Beuschel S., Gandhi U., Heintz N., Smalley TL J.r., Lowther W.T, & Cunniff B. (2021). Unique Cellular and Biochemical Features of Human Mitochondrial Peroxiredoxin 3 Establish the Molecular Basis for Its Specific Reaction with Thiostrepton. Antioxidants, 10(2), 150.
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4

Western Blot Analysis of Retinal Proteins

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Retinal tissues (N = 3 biological replicates) were lysed with RIPA buffer (Thermo Fisher Scientific, Cat.# 89900) containing protease and phosphatase inhibitors (Thermo Fisher Scientific, Cat.# A32961), and protein concentrations were measured using the DC Assay (Bio-Rad Laboratories, Cat.# 5000114), according to the manufacturer’s protocol. An equal amount of protein samples was loaded and separated on an SDS-PAGE 7.5% PROTEAN TGX Stain-Free gel (Bio-Rad, Cat.# 4568024), then transferred to 0.2 µm PVDF membranes (Bio-Rad Laboratories, Cat.# 1,704,156). The PVDF membranes were blocked in 5% Nonfat dry milk (Bio-Rad Laboratories, Cat.# 1,706,404) in Tris-buffered saline with 0.1% Tween 20 (TBST) (VWR, Cat.# K873-4L). Samples were probed with the primary antibodies listed in Additional file 1: Table S1 overnight in 5% bovine serum albumin (Gold Biotechnology, Cat.# A-420-100) in TBST. Blots were incubated with horseradish peroxidase-conjugated species-specific secondary antibodies listed in Additional file 1: Table S1. Proteins were visualized with an enhanced chemiluminescence substrate (Thermo Fisher Scientific, Cat.# 34095) and digitally imaged on a ChemiDoc MP Imaging System (Bio-Rad Laboratories). Quantification of the band intensity was carried out using the Image J Software (NIH, Bethesda, MD).
Strong T.A., Esquivel J., Wang Q., Ledon P.J., Wang H., Gaidosh G., Tse D, & Pelaez D. (2023). Activation of multiple Eph receptors on neuronal membranes correlates with the onset of optic neuropathy. Eye and Vision, 10, 42.
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5

Isolation of Adipose Progenitor Cells

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Epididymal, inguinal, and axillary fat pads were dissected immediately after mice were sacrificed. The fat pads were incubated in Hank’s Balanced Salt Solution (Gibco) containing 3% (w/v) bovine serum albumin (Gold Biotechnology; St. Louis, MO, USA) for 15 min at room temperature, followed by centrifugation at 200× g for 7 min. The fat pads were digested with 0.1% (w/v) collagenase II (Gibco; Waltham, MA, USA) in 37 °C for 60 min followed by filtering through 70 µm cell strainer. Adipose progenitor cells (APCs) were then enriched using Adipose Tissue Progenitor Isolation Kit (Miltenyi Biotec; Bergisch Gladbach, Germany) according to the manufacturer’s protocol.
Joseph J., Cho D.S, & Doles J.D. (2018). Metabolomic Analyses Reveal Extensive Progenitor Cell Deficiencies in a Mouse Model of Duchenne Muscular Dystrophy. Metabolites, 8(4), 61.
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6

Oligomeric State Determination of ApoE Isoforms

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To determine the oligomeric state of the heteromeric mixtures, His-apoE3/His-apoE4 samples (~10 mg/ml) were subjected to FPLC size exclusion chromatography using Bio-Rad BioLogic DuoFlow™ (Bio-Rad, Hercules, CA, USA) on a Superdex 200 Increase 10/300 GL column (G.E. Healthcare Life Sciences, Pittsburgh, PA, USA) that was equilibrated with PBS. FPLC was performed at a flow rate of 0.5 ml/min at 24 ºC and monitored at 280 nm. In control experiments, His-apoE4 was analyzed at similar concentrations. Horse heart myoglobin (Sigma-Aldrich, St. Louis, MO, USA), bovine serum albumin (GoldBio Technology, St. Louis, MO, USA) and bovine immunoglobulin (Sigma-Aldrich, St. Louis, MO, USA) with molecular masses corresponding to ~16,950, 66,430 and 150,000 Da, respectively, were used as standards.
Kai-Han T., Abhari D, & Narayanaswami V. (2019). Conformational Analysis of Apolipoprotein (apo) E3/apoE4 heteromerization. The FEBS journal, 286(10), 1986-1998.
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7

Isolation and Purification of Adipose Stromal Cells

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As previously described (Merrick et al., 2019 (link); Wang et al., 2019 (link)), iWAT tissue was dissected, minced gently and digested with Collagenase Type I (1.5 units/ml; Worthington) and Dispase II (2.4 units/ml; Roche) in DMEM/F12 containing 1% fatty acid-free bovine serum albumin (Gold Biotechnology) in a gentleMACS dissociator (Miltenyi Biotec) on program ‘37 MR ATDK-1’. The digestion was quenched with DMEM/F12 containing 10% FBS, and the dissociated cells were passed through a 100 μm filter and spun at 400 x g for 4 min. The pellet was resuspended in red blood cell lysis buffer (BioLegend), incubated for 4 min at RT, then quenched with DMEM/F12 containing 10% serum. Cells were passed through a 70 μm filter, spun, resuspended, then passed through a final 40 μm filter, spun at 400 x g for 4 min and plated or underwent further processing for FACS. Mice were not pooled unless indicated.
Holman C.D., Sakers A.P., Calhoun R.P., Cheng L., Fein E.C., Jacobs C., Tsai L., Rosen E.D, & Seale P. (2024). Aging impairs cold-induced beige adipogenesis and adipocyte metabolic reprogramming. eLife, 12, RP87756.
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8

Isolation of Activated Human Platelets

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Whole blood from three healthy adult males with no known bleeding diathesis or history of antiplatelet or anticoagulant therapy was collected in sodium citrate (0.109 M) (Becton Dickinson, Franklin Lakes, NJ) on six separate days (18 mL total). Blood was immediately centrifuged at 200×g for 20 min at room temperature. The resulting platelet-rich plasma was diluted with an equal volume of modified HEPES-buffered Tyrode’s solution (HT, 137 mM NaCl, 2.7 mM KCl, 2mM MgCl2, 0.42mM NaH2PO4, 5 mM glucose, 10 mM HEPES, pH 7.4), and Prostaglandin-E1 (Cayman Chemicals, Ann Arbor, Mich) was added to a final concentration of 1 μM to prevent premature platelet activation during preparation. Contaminating erythrocytes and leukocytes were then pelleted by centrifugation at 100×g for 20 min at room temperature. The resulting platelet-rich plasma was again supplemented with 1 μM. Prostaglandin-E1 and centrifuged at 800×g for 20 min to pellet platelets. The diluted plasma supernatant was removed, and the platelet pellet was washed twice with HT buffer. Platelets were resuspended in HT buffer supplemented with 3 mg/mL bovine serum albumin (Gold Biotechnology, St. Louis, Mo), counted, and diluted further with HT to a final concentration of 2.5×108/mL. Platelets were used immediately after preparation and not stored.
Fields A.T., Matthay Z.A., Nunez-Garcia B., Matthay E.C., Bainton R.J., Callcut R.A, & Kornblith L.Z. (2021). GOOD PLATELETS GONE BAD: THE EFFECTS OF TRAUMA PATIENT PLASMA ON HEALTHY PLATELET AGGREGATION. Shock (Augusta, Ga.), 55(2), 189-197.
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9

Western Blot Analysis of Retinal Proteins

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Retinal tissues (N = 3 biological replicates) were lysed with RIPA buffer (Thermo Fisher Scientific, Cat.# 89900) containing protease and phosphatase inhibitors (Thermo Fisher Scientific, Cat.# A32961), and protein concentrations were measured using the DC Assay (Bio-Rad Laboratories, Cat.# 5000114), according to the manufacturer’s protocol. An equal amount of protein samples was loaded and separated on an SDS-PAGE 7.5% PROTEAN TGX Stain-Free gel (Bio-Rad, Cat.# 4568024), then transferred to 0.2 μm PVDF membranes (Bio-Rad Laboratories, Cat.# 1704156). The PVDF membranes were blocked in 5% Nonfat dry milk (Bio-Rad Laboratories, Cat.# 1706404) in Tris-buffered saline with 0.1% Tween 20 (TBST) (VWR, Cat.# K873-4L). Samples were probed with the primary antibodies listed in Supplemental Table 1 overnight in 5% bovine serum albumin (Gold Biotechnology, Cat.# A-420-100) in TBST. Blots were incubated with horseradish peroxidase-conjugated species-specific secondary antibodies listed in Supplemental Table 1. Proteins were visualized with an enhanced chemiluminescence substrate (Thermo Fisher Scientific, Cat.# 34095) and digitally imaged on a ChemiDoc MP Imaging System (Bio-Rad Laboratories)
Strong T.A., Esquivel J., Wang Q., Ledon P.J., Wang H., Gaidosh G., Tse D, & Pelaez D. (2023). Activation of Multiple Eph Receptors on Neuronal Membranes Correlates with The Onset of Traumatic Optic Neuropathy. bioRxiv.
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10

EGF Internalization in INS-1 Cells

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INS-1 cells washed twice with PBS were serum-starved for 2 h in DMEM with 0.1% BSA (GoldBio). After two washes with PBS on ice, cells were incubated with epidermal growth factor (EGF)–Alexa Fluor 647 (Thermo Fisher Scientific) at a concentration of 1 μg/mL for 1 h on ice. Unbound EGF was removed by washing with ice-cold PBS in presence of 0.5% BSA. Cells were chased for the indicated times at 37°C before fixation with 4% PFA in PBS for 30 min on ice. Cells were imaged using a spinning-disk confocal microscope.
Burns C.H., Yau B., Rodriguez A., Triplett J., Maslar D., An Y.S., van der Welle R.E., Kossina R.G., Fisher M.R., Strout G.W., Bayguinov P.O., Veenendaal T., Chitayat D., Fitzpatrick J.A., Klumperman J., Kebede M.A, & Asensio C.S. (2020). Pancreatic β-Cell–Specific Deletion of VPS41 Causes Diabetes Due to Defects in Insulin Secretion. Diabetes, 70(2), 436-448.
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