Bovine serum albumin standard

Manufactured by Thermo Fisher Scientific

Sourced in United States

Bovine serum albumin (BSA) standards are laboratory reagents used for the quantification and standardization of protein concentrations in various analytical applications. These standards provide a consistent and reliable reference point for measuring the protein content in biological samples.

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Lab products found in correlation

Phosphate buffered saline (pbs), by Bio Basic (4 mentions) Enhanced chemiluminescence ecl western blotting chemiluminescent substrate, by Thermo Fisher Scientific (3 mentions) Bca reagent, by Thermo Fisher Scientific (3 mentions) Pierce 660 assay, by Thermo Fisher Scientific (3 mentions) Protease inhibitor cocktail, by Roche (2 mentions) Triton x 100, by Merck Group (2 mentions) Protease inhibitor, by Merck Group (2 mentions) Trifluoroacetic acid, by Merck Group (2 mentions) Cresyl violet, by Merck Group (2 mentions) 2 3 5 triphenyltetrazolium chloride, by Merck Group (2 mentions) Manganese superoxide dismutase mnsod, by Cell Signaling Technology (2 mentions) Oct compound cryostat embedding medium, by Thermo Fisher Scientific (2 mentions) β actin, by Cell Signaling Technology (2 mentions) Kanamycin, by GoldBio (2 mentions) Spectinomycin, by GoldBio (2 mentions) Horseradish peroxidase conjugated secondary antibody, by Cell Signaling Technology (2 mentions) Lysis buffer, by Cell Signaling Technology (2 mentions) Bca protein assay kit, by Thermo Fisher Scientific (2 mentions) Hybond c, by Cytiva (2 mentions) Anti cd73 antibody, by Cell Signaling Technology (2 mentions)

Close spelling variants of this product

Bovine serum (215 citations) Albumin standard (23 citations) Bovine albumin (7 citations)

45 protocols using bovine serum albumin standard

Enzyme Activity Extraction Protocol

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Adult E. servus, C. hilaris, N. viridula (n = 1/rep, head and thorax), and P. guildinii (n = 2/rep, head and thorax) were homogenized (Homogenizer, Thomas Scientific, Swedesboro, NJ, USA) in 500 μL of ice-cold sodium phosphate buffer (0.1 M, pH 7.2) containing 0.1% Triton X-100 and a protease inhibitor in a 2.0 mL screw cap tube. The homogenates were centrifuged at 10,000× g for 15 min at 4 °C, and the resulting supernatant was transferred to a 1.5 mL centrifuge tube. An undiluted sample was used for the cytochrome P450 assay, a 4-fold dilution of supernatant was used for the protein, GST, and AChE assays, and a 20-fold dilution was used for the esterase assay. The supernatants were diluted using homogenization buffer without Triton X-100. The total protein concentration of each enzyme extract was determined using a Bradford protein assay kit with a bovine serum albumin standard [23 (link)] (Thermo Scientific, Waltham, MA, USA). Each sample for all assays was measured with three technical replicates.

Du Y., Scheibener S., Zhu Y.C., Allen K.C, & Reddy G.V. (2024). Insecticide Susceptibilities and Enzyme Activities of Four Stink Bug Populations in Mississippi, USA. Insects, 15(4), 265.

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Western Blot Analysis of ER Stress Proteins

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Cells were lysed in ice-cold RIPA buffer (Cell Signaling Technology) containing protease inhibitor cocktail (Roche) and phosphatase inhibitor cocktails (Sigma-Aldrich). The lysates were incubated on ice for 30 minutes, and then centrifuged at 13,000 rpm for 20 minutes at 4℃. The protein concentration of the supernatant was quantified using the Bradford protein assay (Bio-Rad Protein Assay, BioRad, Hercules, CA, USA) with bovine serum albumin standard (Thermo Scientific, Rockford, IL, USA). Equal amounts of protein (20 µg) were electrophoresed on 4% to 12% Bis-Tris Nupage gels (Invitrogen) and transferred to polyvinylidene difluoride membranes using the iBlot Dry Blotting System (Invitrogen). After transfer, the membranes were blocked in 5% bovine serum albumin /Tris buffered saline with Tween-20 buffer for 1 hour, and then incubated overnight at 4℃ with antibodies to SEPP1, fetuin-A, IRE1α, P-IRE1α, PERK, P-PERK, ATF6, XBP-1, CHOP, and β-actin followed by incubation with horseradish peroxidase conjugated secondary antibodies. Immunoreactive bands were visualized with enhanced chemiluminescence Western blotting detection reagents (GE Healthcare, Chalfont St. Giles, UK).

Lee J., Hong S.W., Park S.E., Rhee E.J., Park C.Y., Oh K.W., Park S.W, & Lee W.Y. (2015). Exendin-4 Inhibits the Expression of SEPP1 and Fetuin-A via Improvement of Palmitic Acid-Induced Endoplasmic Reticulum Stress by AMPK. Endocrinology and Metabolism, 30(2), 177-184.

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Protein Purification and Quantification

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Culture homogenate was purified using a His GraviTrap column (GE Healthcare # 11-0033-99). Eluted protein sample was separated by SDS-PAGE, stained with Coomassie G-250, and quantified using densitometry relative to a bovine serum albumin standard (Thermo). Purified protein samples were diluted in LB-L and stored at 4 °C for enzyme activity assays.

Metcalf K.J., Bevington J.L., Rosales S.L., Burdette L.A., Valdivia E, & Tullman-Ercek D. (2016). Proteins adopt functionally active conformations after type III secretion. Microbial Cell Factories, 15, 213.

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TCDD-Induced Lung Metabolism Profiling

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Following Harrigan’s protocol [16 (link)], C57BL/6 mice (male, 7–8 weeks old) were treated with TCDD (5 μg/kg, 2% DMSO in corn oil, i.p.) or vehicle (n = 4). Forty- eight hours later, all mice were sacrificed and lung samples were harvested. Lung tissues were flash-frozen in liquid nitrogen and stored at −80 °C until further analysis.
The study protocol was approved by the Institutional Animal Care and Use Committee of the University of Pittsburgh. One hundred mg of lung tissue was homogenized in 500 μL of 1 × PBS at 0 °C. The homogenate was centrifuged at 9,000 g for 25 min at 4 °C and the resulting supernatant was designated as lung S9 fraction. The total protein concentration of the S9 fraction was determined by bovine serum albumin standard (Thermo Fisher, Waltham, MA) calibration curves.
Incubations were conducted in 1 × PBS (pH 7.4), containing 30 μM DTG, 2.5 mM NH₂OMe, 2 mg/mL lung S9, and 1 mM NADPH in a final volume of 200 μL. The incubations were continued at 37 °C for 1 hour, and terminated with 200 pl of methanol. The resulting mixture was vortexed and dried, and reconstituted in 100 μL of water/acetonitrile/methanol (1:2:2, v/v/v). The suspension was vortexed and centrifuged at 15,000 rpm for 10 min. A 10 μL of the supernatant was injected into the UPLC-QTOFMS system for metabolite analysis.

Zhu J., Wang P., Li F., Lu J., Shehu A.I., Xie W., McMahon D, & Ma X. (2018). CYP1A1 and 1B1-mediated metabolic pathways of dolutegravir, an HIV-1 integrase inhibitor. Biochemical pharmacology, 158, 174-184.

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Radiolabeled BAT and NAB Synthesis

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BAT (NSC 320846), NAB (NSC 611001), N-propyl BAT, ¹⁴C-BAT and differentially deuterated (d3- and d4-) BAT were provided by the Developmental Therapeutics Program, DCTD, NCI. ¹⁴C-NAB, d3-NAB, and d4-NAB were prepared in situ by incubating BAT with NAT2 and acetyl-CoA. β-Nicotinamide adenine dinucleotide phosphate, reduced form 95% (NADPH), acetyl coenzyme A sodium salt (acetyl-CoA), DL-dithiothreitol, Bis(p-nitrophenyl) phosphate sodium salt (BNPP), Tris-HCl, L-glutathione reduced form (GSH), 0.5% triton X-100 and ammonium acetate were purchased from Sigma Aldrich (St. Louis, MO). Acetonitrile was purchased from Fisher Scientific (Fairlawn, NJ). HPLC grade water, methanol, and sodium hydroxide (NaOH) were purchased from EMD (Billerica, MA). Bovine serum albumin standard was purchased from Thermo Scientific (Waltham, MA). Ultrapure salmon sperm DNA was purchased from Invitrogen (Grand Island, NY). Ultima gold scintillation fluid was purchased from Perkin Elmer (Waltham, MA).

Covey J.M., Reid J.M., Buhrow S.A., Kuffel M., Walden C., Behrsing H, & Ames M.M. (2016). Comparative Metabolism of Batracylin (NSC 320846) and N-acetylbatracylin (NSC 611001) Using Human, Dog, and Rat Preparations In Vitro. Journal of drug metabolism & toxicology, 7(2), 203.

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Quantifying Leaf N, Chlorophyll, and Rubisco

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The leaf N, chlorophyll and rubisco protein content were determined according to [40 (link)]. Leaf samples were ground with homogenization buffer (50 mM sodium phosphate, 5%(v/v) glycerol and 1 mM sodium iodoacetate). The aliquot was used for leaf N and chlorophyll determination based on the Kjeldahl method and [41 (link)]. For rubisco protein quantification, leaf soluble fractions were applied to sodium dodecyl sulfate polyacrylamide gel electrophoresis (SDS-PAGE). After Coomassie brilliant blue (CBB) staining, the bands corresponding to the large and small subunits of rubisco were excised, and the dye extracted with formamide was colorimetrically quantified. Bovine serum albumin (BSA) protein (Bovine Serum Albumin Standard, Thermo Fisher Scientific, Waltham, MA, USA) was used as a standard sample, and a standard curve was prepared.

Wada S., Amako K, & Miyake C. (2021). Identification of a Novel Mutation Exacerbated the PSI Photoinhibition in pgr5/pgrl1 Mutants; Caution for Overestimation of the Phenotypes in Arabidopsis pgr5-1 Mutant. Cells, 10(11), 2884.

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Mouse Brain Tissue Homogenization

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A unilateral brain tissue punch (24 mouse brain tissue) was homogenized using a motorized tissue grinder (Fisher Scientific, Waltham, MA, USA) in lysis buffer (20 mM Tris pH 7.5 (Fisher Scientific), 150 mM sodium chloride (Fisher Scientific), 2 mM EDTA pH 8.0 (Sigma-Aldrich), 1% triton X-100 (Sigma-Aldrich), 10% glycerol (Sigma-Aldrich), 1% protease inhibitors (Sigma-Aldrich), 2% phosphatase inhibitor cocktail II (Sigma-Aldrich) and 2% phosphatase inhibitor cocktail III (Sigma-Aldrich)) prepared in dH₂O. Samples were then centrifuged at 10,000× g for 10 min at 4 °C. A Pierce 660 nm protein assay with bovine serum albumin standard (Thermo Fisher Scientific) was used to measure protein concentrations in the supernatant.

Piggott V.M., Lloyd S.C., Matchynski J.I., Perrine S.A, & Conti A.C. (2021). Traumatic Stress, Chronic Ethanol Exposure, or the Combination, Alter Cannabinoid System Components in Reward and Limbic Regions of the Mouse Brain. Molecules, 26(7), 2086.

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Protein Extraction and Quantification

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MDA-MB-231 (4175) LM2 cells were washed twice with PBS, then harvested, pelleted, and resuspended in 300 µL lysis buffer (50 mM Tris/HCl, pH 8, 150 mM NaCl, and 1% Nonidet P-40). Protein concentration was determined using a microplate reader to measure absorbance at 562 nm with a bovine serum albumin standard (Cat # 23209; Thermo Fisher Scientific). Experiments were performed in triplicate, and samples were analyzed in duplicate.

Cook M.T., Liang Y., Besch-Williford C, & Hyder S.M. (2016). Luteolin inhibits lung metastasis, cell migration, and viability of triple-negative breast cancer cells. Breast Cancer : Targets and Therapy, 9, 9-19.

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Brain Tissue and Blood Sample Preparation

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Immediately following the final LMA test session, the mice were euthanized by cervical dislocation, and brains were removed and stored at -80°C until microdissection to obtain striatal tissue samples. Trunk blood samples from the BEC-Test cohort were also collected and centrifuged at 5,000 rpm for 10 min to obtain plasma, which was stored at -80°C until use. Brains from the Immuno-Home cohort were sliced into 2 mm sections using a rodent brain slicer matrix (Zivic Instruments, Pittsburgh, PA), and unilateral 1.5 mm tissue punches (Miltex, Inc., York, PA) from the left anterior-dorsal striatum at 1.5 to -0.5 mm anterior to bregma were taken and stored at -80°C until immunoassay. A unilateral punch was then homogenized for approximately 20 seconds in lysis buffer (20 mM Tris pH 7.5, 150 mM NaCl, 2mM EDTA, 1% triton X-100, 10% glycerol with Phosphatase Inhibitor Cocktail 2 P5726, Phosphatase Inhibitor Cocktail 3 P0044 and Protease Inhibitor P8340 from Sigma Aldrich, St. Louis, MO), then centrifuged at 4°C for 10 min at 10,000 x g, and the protein was quantified using a Pierce 660 nm protein assay using a bovine serum albumin standard (Thermo Scientific, Rockford, IL).

Matchynski-Franks J.J., Susick L.L., Schneider B.L., Perrine S.A, & Conti A.C. (2016). Impaired Ethanol-Induced Sensitization and Decreased Cannabinoid Receptor-1 in a Model of Posttraumatic Stress Disorder. PLoS ONE, 11(5), e0155759.

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Purification and Characterization of Enzymes

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Enzymes (hEPl wt and hEPl scC112S) were expressed, refolded and purified in-house [11 (link)]. Polyclonal sheep-anti-mouse and donkey-anti-rabbit antibodies were from Dianova (Hamburg, Germany), monoclonal mouse-anti-EGF, EGF protein and polyclonal rabbit-anti-EGF were from Abcam (Cambridge, UK). Citric acid and Tween®20 were from Serva Electrophoresis (Heidelberg, Germany), Tris(hydroxymethyl)-aminomethan was from Applichem (Darmstadt, Germany). C₆-Succinimidyl-4-formylbenzoate and C₆-Succinimidyl-4-hydrazinonicotinate acetone hydrazone were from Acris Antibodies (Herford, Germany). Sodium chloride, hydrochlorid acid (conc.), Na₂HPO₄x12H₂O, KH₂PO₄, GD₄K-na and DMSO were purchased from Sigma-Aldrich (Taufkirchen, Germany) in the highest purities available. Roti®-Block was ordered from Roth (Karlsruhe, Germany). Bovine serum albumin standard was from Thermo Fisher Scientific (Rockford, USA). Deionized water was obtained from a Purelab Ultra water purification system (ELGA LabWater, Celle, Germany; 18.2 MΩ*cm).

Prasse A.A., Zauner T., Büttner K., Hoffmann R, & Zuchner T. (2014). Improvement of an antibody-enzyme coupling yield by enzyme surface supercharging. BMC Biotechnology, 14, 88.

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