Albumin standard

Manufactured by Thermo Fisher Scientific

Sourced in United States

The Albumin standard is a laboratory reagent used to determine the concentration of albumin in biological samples. It provides a consistent, known concentration of albumin that can be used to calibrate and validate albumin measurement methods.

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Bovine serum albumin standards (45 citations) Pierce™ Bovine Serum Albumin Standard (10 citations) Pierce™ Bovine Serum Albumin Standard Pre-Diluted Set (7 citations) Bovine Serum Albumin standard protein (5 citations) Pierce™ Bovine Serum Albumin Standard Ampules (4 citations) Bovine serum albumin standard (BSA) (2 citations) Bovine Serum Albumin Standard Set (2 citations)

23 protocols using albumin standard

Quantifying Total Protein by BCA Assay

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Standard curves were generated using albumin standard (Thermo Scientific). Total protein was quantified after extraction and after purification with 2 µl of sample in duplicate using the bicinchoninic acid method (Thermo Scientific Micro BCA Protein Assay Kit). Absorbance was measured on a Nanodrop ND-1000 spectrophotometer (Thermo Scientific).

Browning T.J., Saito M.A., Garaba S.P., Wang X., Achterberg E.P., Moore C.M., Engel A., Mcllvin M.R., Moran D., Voss D., Zielinski O, & Tagliabue A. (2023). Persistent equatorial Pacific iron limitation under ENSO forcing. Nature, 621(7978), 330-335.

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Urinary Protein Extraction Protocol

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Animals were placed individually in metabolic cages overnight (for 12 h) to collect urine samples. During urine collection, the mice had free access to water but not food to avoid urine contamination. The collected urine was centrifuged at 4 °C and 3,000 × g for 10 min to remove cells and particulate matter and then stored at −80 °C. Centrifugation of the samples at 4 °C and 12,000 × g for 30 min was performed to remove cell debris before urinary protein extraction. The supernatants were precipitated with three volumes of acetone precooled at −20 °C for 2 h, followed by centrifugation at 4 °C and 12,000 × g for 30 min. Then, the precipitate was resuspended in lysis buffer (8 mol/L urea, 2 mol/L thiourea, 25 mmol/L DTT, and 50 mmol/L Tris (Sigma-Aldrich, Germany))^{16 (link)}. The protein concentrations were measured using the Bradford assay at 595 nm. An albumin standard (Thermo Fisher, US) was used [bovine serum albumin (BSA) at 2 mg/mL in 0.9% saline and 0.05% sodium azide].

Liu Y., Wang Y., Cao Z, & Gao Y. (2019). Changes in the Urinary Proteome in a Patient-Derived Xenograft (PDX) Nude Mouse Model of Colorectal Tumor. Scientific Reports, 9, 4975.

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Capsicodendrin Modulates NF-κB Signaling

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Cells were treated with capsicodendrin at different concentrations (0.008, 0.016, 0.4, 2.0 and 10 μM) for 3 h. Briefly, cells were lysed using PhosphoSafe Lysis Buffer (Novagen). Protein concentration was determined by using a Bradford protein assay kit and albumin standard (Thermo Scientific). Absorbance was measured using a Fluostar Optima plate reader (BMG Labtech Inc, Durham, NC). Lysates were analyzed by western blot analysis with primary (1:1000) and secondary antibodies (1:2000). Equal amounts of protein (20 μg) were loaded together with a LDS sample loading buffer (Invitrogen) and resolved using Nu-PAGE 10% SDS-PAGE Bis-Tris gels together with SeeBlue® Plus2 Pre-Stained Standard (Invitrogen). Proteins were transferred to a polyvinyldiene fluoride (PVDF) membrane using transfer buffer, TBS-T. The blots were then blocked at room temperature using non-fat milk and probed using primary antibodies against each target protein including NF-κB p65, IKKβ, ICAM-1 and caspase-7, using BSA in TBS-T overnight. Conjugated antibodies were detected using chemiluminescent substrates with a Supersignal Femto kit from Thermo Scientific.

Acuña U.M., Ezzone N., Rakotondraibe L.H, & Carcache de Blanco E.J. (2021). Activity in MCF-7 Estrogen-Sensitive Breast Cancer Cells of Capsicodendrin from Cinnamosma fragrans. Anticancer research, 41(12), 5935-5944.

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Western Blot Analysis of Protein Samples

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Cells were lysed in NP40 lysis buffer (Invitrogen, Waltham, MA, USA) containing a protease inhibitor cocktail (GenDEPOT, Barker, TX, USA) on ice for 30 min. The protein concentration was quantified using an albumin standard (Thermo Scientific, Waltham, MA, USA). Equal amounts of proteins were resolved by sodium dodecyl sulfate polyacrylamide gel electrophoresis (SDS-PAGE) and transferred to polyvinylidene difluoride (PVDF) membranes (Merck Millipore, Darmstadt, Germany). The membranes were blocked at room temperature for 1 h with 3% bovine serum albumin (BSA) in TBS with tween 20. Following blocking, the membranes were incubated with primary antibodies (1:1000 dilution) for 16 h at 4 °C. The membranes were then washed thrice with TBST and incubated with the HRP-conjugated secondary antibodies followed by incubation with the enhanced chemiluminescence (ECL) solution (Dynebio, Seongnam, Korea). Proteins were visualized using an Amersham imager 600 (GE Healthcare, Chicago, IL, USA) and quantified with the ImageJ program.

Kim G., Han D.W, & Lee J.H. (2023). The Cytoprotective Effects of Baicalein on H2O2-Induced ROS by Maintaining Mitochondrial Homeostasis and Cellular Tight Junction in HaCaT Keratinocytes. Antioxidants, 12(4), 902.

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Cell Lysis and Protein Quantification

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For Western blot analysis, cells were lysed in RIPA buffer (50 mM Tris HCl, pH 7.5, 150 mM NaCl, 1% NP40, 0.5% sodiumdeoxycholate, 0.1% SDS). For that, cells were harvested from six‐well plate and pellets were lysed in RIPA buffer supplemented with protease inhibitor cocktail (Roche) and phosphatase inhibitor cocktail (Roche) for 20 min on ice. Total cellular proteins were recovered upon centrifugation at 18,531 g for 20 min at 4°C. For proteasome activity assays, proteins were extracted from cells using native lysis buffer (50 mM Tris HCl pH 7.5, 2 mM DTT, 5 mM MgCl₂, 10% glycerol, 2 mM ATP, 0.05% digitonin) supplemented with protease inhibitor cocktail (Roche) for 20 min on ice and centrifuged at 18,531 g for 20 min at 4°C. Protein concentration in cell lysates was determined by Bradford assay using the BCA detection reagent according to the manufacturer's instructions (Thermo Fisher Scientific) and an albumin standard (Thermo Fisher Scientific).

Wang X., Zhang H., Wang Y., Bramasole L., Guo K., Mourtada F., Meul T., Hu Q., Viteri V., Kammerl I., Konigshoff M., Lehmann M., Magg T., Hauck F., Fernandez I.E, & Meiners S. (2023). DNA sensing via the cGAS/STING pathway activates the immunoproteasome and adaptive T‐cell immunity. The EMBO Journal, 42(8), e110597.

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Protein Quantification using Pierce 660 nm Assay

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Protein concentration was measured using Pierce 660 nm Protein Assay Reagent (Thermo Scientific) and Albumin Standard (Thermo Scientific) as the standard according to the manufacturer’s instructions.

Nutahara E., Abe E., Uno S., Ishibashi Y., Watanabe T., Hayashi M., Okino N, & Ito M. (2019). The glycerol-3-phosphate acyltransferase PLAT2 functions in the generation of DHA-rich glycerolipids in Aurantiochytrium limacinum F26-b. PLoS ONE, 14(1), e0211164.

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Biochemical Assays for Cellular Cytotoxicity Analysis

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Thiazolyl blue tetrazolium bromide (MTT), 2″,7″-dichlorodihydro-fluorescein diacetate (DCFH-DA) and other reagents were purchased from Sigma-Aldrich Co. (St. Louis, MO, USA). Tris was purchased from Duchefa Biochemie (BH Haarlem, The Netherlands), dimethyl sulfoxide (DMSO) from Junsei Chemical Co. (Tokyo, Japan). Fetal bovine serum (FBS) and penicillin-streptomycin (P/S) were purchased from Gibco (Los Angeles, CA, USA). Dulbecco's Modified Eagle's Medium (DMEM) was purchased from Welgene Inc. (Gyeongsangbuk-do, Korea). BCA reagent and albumin standard were from Thermo Scientific (Waltham, MA, USA). Primary Bcl-2 antibody was purchased from Oncogene (Bracknell, England). Bax and PAPR antibodies were obtained from Cell Signaling (Danvers, MA, USA) and cytochrome c, caspase-9, and β-actin antibodies from Santa Cruz (Paso Robles, CA, USA). Caspase-3 antibody was obtained from EMD Millipore (Billerica, MA, USA). Secondary antibodies goat anti-rabbit IgG, pAb, goat anti-mouse IgG, pAb, and caspase-3 activity assay kit were obtained from Enzo Life Sciences (Farmingdale, NY, USA). West-Q chemiluminescent substrate was purchased from GenDEPOT (Katy, TX, USA). The solvents used were of HPLC grade, unless stated otherwise.

Lee S.E., Lim C., Ahn S.C, & Cho S. (2017). A Study of the Anti-Cancer Effects of the Hexane Fraction of the Methanol Extract of Forsythiae Fructus. Pharmacognosy Magazine, 13(52), 719-724.

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Immunoblot Analysis of AmbI Inhibition in MCF-7 Cells

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Immunoblot was performed following a previous published protocol.^{6 (link)} MCF-7 cells were treated at different concentrations of AmbI (0.008, 0.016, 0.4, 2.0 and 10 μM) for 3 h. The cells were lysed using PhosphoSafe Lysis Buffer (Novagen), and the lysates were analyzed by western blot analysis with primary (1:1000) and secondary antibodies (1:2000). Protein concentration in the lysate was determined using a Bradford protein assay kit with an albumin standard (Thermo Scientific). Absorbance was measured using Fluostar Optima plate reader (BMG Labtech Inc, Durham, NC). Equal amounts of protein (20 μg) were loaded together with LDS sample loading buffer (Invitrogen) and resolved using Nu-PAGE 10% SDS-PAGE Bis-Tris gels together with SeeBlue® Plus2 Pre-Stained Standard (Invitrogen).
Electrophoresis was performed using SDS-PAGE buffer in a Nu-PAGE XCell SureLock Module from Invitrogen. Proteins were transferred to a polyvinyldiene fluoride (PVDF) membrane using transfer buffer. The blots were blocked at room temperature using non-fat milk and probed using primary antibodies against each target protein using BSA in TBS-T overnight. Conjugated antibodies were detected using Chemiluminescent substrates Supersignal Femto kit from Thermo Scientific and relative band densities were determined.

Acuña U.M., Zi J., Orjala J, & Carcache de Blanco E.J. (2015). Ambiguine I Isonitrile from Fischerella ambigua Induces Caspase-Independent Cell Death in MCF-7 Hormone Dependent Breast Cancer Cells. International journal of cancer research, 49(1), 1655-1662.

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Quantitative Proteomic Sample Preparation

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Ammonium bicarbonate, dithiothreitol, trichloroacetic acid solution (6.1N), iodoacetamide, sodium deoxycholate, and sucrose were obtained from Sigma-Aldrich (St. Louis, MO). Sodium chloride, Optima grade acetone, Optima LC/MS grade water, acetonitrile, water with 0.1% (v/v) formic acid, and formic acid were purchased from Fisher Scientific (Fair Lawn, NJ). Imidazole and phenylmethylsulfonyl fluoride (PMSF) were from Acros Organics (NJ, USA), and EDTA was from Fluka Biochemika (Buchs, Switzerland). Anhydrous 2-propanol was acquired from Alfa Aesar (Ward Hill, MA). Bicinchoninic acid assay (BCA) and albumin standard were from Thermo Scientific (Rockford, IL). Frozen sequencing grade modified trypsin was purchased from Promega (Madison, WI). Synthetic ¹³C and ¹⁵N stable isotope-labeled (SIL heavy peptides) crude signature peptides were manufactured by ThermoFisher Scientific (> 99% isotopic enrichment according to the manufacturer) and were delivered in 50% acetonitrile and 0.1% trifluoroacetic acid.

Qiu X., Doyle L.M, & Wang M.Z. (2022). Development of a UPLC-MRM-based targeted proteomic method to profile subcellular organelle marker proteins from human liver tissues. Scientific Reports, 12, 10985.

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Protein Isolation and Quantification

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Protein was isolated using RIPA lysis buffer (Millipore, 20-188) containing 1X proteinase and phosphatase inhibitor (Thermo Scientific, 1861281). The concentration of protein was calculated using BCA protein assay kit (Thermo Scientific, 23228). An Albumin standard (Thermo Scientific, 23209) was used for generating the standard curve for the BCA assay. For western blot analysis, proteins were diluted with RIPA lysis buffer and 4X Laemmli sample buffer (BIO-RAD, 1610747) containing 10 % β-mercaptoethanol (Sigma, M7522). Then protein samples were heated at 95 °C for 5 minutes and stored at −80 °C for long-term storage.

Hiroi N., Brown J.R., Haile C.N., Ye H., Greenberg M.E, & Nestler E.J. (1997). FosB mutant mice: Loss of chronic cocaine induction of Fos-related proteins and heightened sensitivity to cocaine’s psychomotor and rewarding effects. Proceedings of the National Academy of Sciences of the United States of America, 94(19), 10397-10402.

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