Modified lowry protein assay kit

Manufactured by Thermo Fisher Scientific

Sourced in United States, Canada, Spain

The Modified Lowry Protein Assay Kit is a colorimetric method for the determination of protein concentration in a sample. The kit uses a copper-based reagent to react with peptide bonds in the protein, resulting in a color change that can be measured spectrophotometrically. The intensity of the color is proportional to the protein concentration in the sample.

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Lab products found in correlation

Uv 1800, by Shimadzu (3 mentions) Infinite m200, by Tecan (3 mentions) Bovine serum albumin (bsa), by Thermo Fisher Scientific (2 mentions) Folin ciocalteau reagent, by Thermo Fisher Scientific (2 mentions) Modified lowry reagent, by Thermo Fisher Scientific (2 mentions) Dye reagent, by Bio-Rad (1 mentions) Pymol 0.99rc6, by DeLano Scientific (1 mentions) Leupeptin, by Cell Signaling Technology (1 mentions) Phenyl methyl sulfonyl fluoride (pmsf), by Cell Signaling Technology (1 mentions) Ohmmeter, by World Precision Instruments (1 mentions) Sephadex g 50 column, by GE Healthcare (1 mentions) Monosaccharide, by Merck Group (1 mentions) Sodium persulphate, by Merck Group (1 mentions) Ethanol, by Merck Group (1 mentions) Toluene, by Merck Group (1 mentions) Formic acid, by Merck Group (1 mentions) Acetic acid, by Merck Group (1 mentions) 6 hydroxy 2 5 7 8 tetramethylchromane 2 carboxylic acid trolox, by Merck Group (1 mentions) 2 2 azino bis 3 ethylbenzothiazoline 6 sulfonic acid diammonium salt, by Merck Group (1 mentions) Sod activity assay kit, by Abcam (1 mentions)

Close spelling variants of this product

Modified Lowry Protein Assay Modified Lowry assay Lowry Protein Assay Protein assay

31 protocols using modified lowry protein assay kit

Protein Quantification and Structural Analysis

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Protein was determined (Bradford, 1976 (link)) with a commercial dye reagent (from Bio-Rad) using bovine serum albumin as standard. However, with S. elongatus extracts, to avoid chlorophyll interference, protein was determined according to Lowry (Lowry et al., 1951 (link)), again with a commercial Lowry reagent (Modified Lowry protein Assay Kit, from Thermo Scientific) and bovine serum albumin as standard, measuring the absorbance at 750 nm.
Protein structures were represented using PyMOL 0.99rc6 (DeLano Scientific LLC), utilizing the Protein DataBank (PDB; http://www.rcsb.org/pdb/) files 2XG8, 2XKO, and 2V5H for PII-PipX, NtcA-PipX, and PII-NAGK, respectively (Llácer et al., 2007 (link), 2010 (link)).

Labella J.I., Obrebska A., Espinosa J., Salinas P., Forcada-Nadal A., Tremiño L., Rubio V, & Contreras A. (2016). Expanding the Cyanobacterial Nitrogen Regulatory Network: The GntR-Like Regulator PlmA Interacts with the PII-PipX Complex. Frontiers in Microbiology, 7, 1677.

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Hippocampal Fractionation and Mitochondrial Isolation

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A particulate and soluble fractions together with a pure-mitochondria fraction were obtained from the CA1 and CA2-4,DG regions of the hippocampi of control and ischemic gerbils. Hippocampi were homogenized in ice-cold isotonic buffer (15 mM Tris/HCl, pH 7.5, 0.25 M sucrose, 1 mM MgCl₂, 1 mM EGTA, 2 mM EDTA, 1 mM PMSF, and 1 mM DTT), prior to centrifugation (1000× g, 10 min, 4 °C). The supernatant was centrifuged at 11,000× g for 20 min at 4 °C to yield a particulate fraction enriched with mitochondria (P2). The pure mitochondrial pellet was obtained after centrifugation of P2 (100,000× g, 30 min, 4 °C) with 12% Ficoll, as described earlier [4 (link),30 (link)]. For Western blot analysis of MPC1 and MPC2 the tissue was homogenized under nondenaturing conditions, in cell lysis buffer containing 20 mM Tris–HCl at pH 7.5, 150 mM NaCl, 1 mM Na₂EDTA, 1 mM EGTA, 1% Triton, 2.5 mM sodium pyrophosphate, 1 mM β-glycerophosphate, 1 mM Na₃VO₄, 1 μg/mL leupeptin, and 1 mM PMSF (Cell Signaling Technology, Danvers, MA, USA). After homogenization samples were sonicated four times for 5 s and centrifuged 14,000× g at 4 °C for 20 min to obtain clear tissue lysates. The protein concentration was determined using a Modified Lowry Protein Assay Kit (Thermo Scientific, Grand Island, NY, USA).

Beręsewicz-Haller M., Krupska O., Bochomulski P., Dudzik D., Chęcińska A., Hilgier W., Barbas C., Zablocki K, & Zablocka B. (2021). Mitochondrial Metabolism behind Region-Specific Resistance to Ischemia-Reperfusion Injury in Gerbil Hippocampus. Role of PKCβII and Phosphate-Activated Glutaminase. International Journal of Molecular Sciences, 22(16), 8504.

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Transepithelial Transport of Soy Peptide Hydrolysates

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Preparation of trans-well plates and transport experiments followed the procedures described in Fan et al. [7 (link)] and Liang et al. [9 (link)]. After cells were seeded for one week, transepithelial electrical resistance (TEER) was monitored every two days using an ohmmeter (World Precision Instruments, Sarasota, FL, USA), and, on day 21, only wells with TEER values >400 Ω/cm² were used. The gastrointestinal digest of SPH-T (20 mg/mL) was dissolved in HBSS, pre-warmed, and added to the apical chambers (0.5 mL); the permeates in the basolateral chambers (1.5 mL) were collected for up to 4 h. Only samples in wells with TEER values >400 Ω/cm² after transport study were used for later analysis. Peptide concentrations were determined by the Modified Lowry Protein Assay Kit (Thermo Fisher Scientific, Burlington, ON, Canada). The permeability of transport was expressed as the % (w/w) of peptides transported. Chromatograms of the samples before and after transport were analyzed using an Acquity BEH C18 column (1.7 μm, 2.1 × 100 mm) on a reverse-phase ultra-performance liquid chromatography (RP-UPLC) system. Samples (10 μL) were eluted using a gradient of chromatographic grade H₂O and ACN (both containing 0.05% TFA) at 0.3 mL/min as follows: 1% B (0–3 min) and 1–23% B (3–28 min); absorbance was monitored at 220 nm.

Fan H., Yu W., Liao W, & Wu J. (2020). Spent Hen Protein Hydrolysate with Good Gastrointestinal Stability and Permeability in Caco-2 Cells Shows Antihypertensive Activity in SHR. Foods, 9(10), 1384.

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Extraction and Quantification of Protoporphyrin IX in Cells

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PpIX in cultured cells or tissue samples was isolated in 50 μL of NaOH (0.1 M) and homogenized on ice using Powermasher II (Assist; Tokyo, Japan). An aliquot (10 μL) of the NaOH-treated sample was withdrawn and used for a protein concentration assay (modified Lowry protein assay kit, Thermo Scientific; Rochford, IL, USA), while the remaining 40 μL of the NaOH-treated sample was denatured by the addition of 150 μL of N,N-dimethylformamide:isopropanol (100:1, v/v) solution. After overnight incubation, the prepared samples were centrifuged at 12,000 rpm for 10 min. Porphyrin concentration was determined by spectrophotometry at the Soret maximum (405 nm), and fluorescence was measured using an excitation wavelength of 405 nm and an emission wavelength of 635 nm [51 (link)].

Takahashi J., Nagasawa S., Doi M., Takahashi M., Narita Y., Yamamoto J., Ikemoto M.J, & Iwahashi H. (2021). In Vivo Study of the Efficacy and Safety of 5-Aminolevulinic Radiodynamic Therapy for Glioblastoma Fractionated Radiotherapy. International Journal of Molecular Sciences, 22(18), 9762.

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Conjugation of Monoclonal Antibodies with IR700 Dye

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The methods of conjugation were referenced in a previous report.⁹ Briefly, panitumumab or trastuzumab (1 mg, 6.8 nmol) were incubated with IR700 NHS ester (66.8 µg, 34.2 nmol) in 0.1 M Na₂HPO₄ (pH 8.5) at room temperature for 3 h. The mixture was purified with a gel‐filtration Sephadex G50 column (PD‐10; GE Healthcare), and Panitumumab‐IR700 (Pan‐IR700) or Trastuzumab‐IR700 (Tra‐IR700) conjugates were derived. Protein concentrations were determined using a Modified Lowry Protein Assay Kit (Thermo Fisher Scientific Inc) by measuring the absorption at 750 nm with a microplate reader (Infinite M200; Tecan Austria GmbH). The concentration of IR700 was measured by absorption at 689 nm with a spectrophotometer (UV‐1800; Shimadzu Corp.) to confirm the number of fluorophore molecules to each mAb. The IR700 to mAb ratio was approximately 3.

Hirata H., Kuwatani M., Nakajima K., Kodama Y., Yoshikawa Y., Ogawa M, & Sakamoto N. (2021). Near‐infrared photoimmunotherapy (NIR‐PIT) on cholangiocarcinoma using a novel catheter device with light emitting diodes. Cancer Science, 112(2), 828-838.

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Posidonia oceanica Leaves Biomass Characterization

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Biomass waste material consisting of Posidonia oceanica (P. oceanica) leaves was collected from the shore in Calpe, Alicante (Spain) (38°38′09″N 0°04′16″E) in February–March 2017 (two different batches were collected). The collected leaves had a dark brown coloration. The material was washed vigorously with water to remove sand and salts and stored at 4 °C until its use.
2,2′-Azino-bis (3-ethylbenzothiazoline-6-sulfonic acid) diammonium salt (ABTS), (±)-6-Hydroxy-2,5,7,8-tetramethylchromane-2-carboxylic acid (Trolox) 97%, ethanol (>99.8%), toluene, acetic acid, formic acid and sodium persulphate were purchased from Sigma–Aldrich (Darmstadt, Germany). The Folin–Ciocalteau reagent, modified Lowry reagent and bovine serum albumin were obtained from the “modified Lowry protein assay kit” purchased from Thermo Fisher scientific (Madrid, Spain). All the salts, reagents and monosaccharides used for the carbohydrate composition analysis were purchased from Merck (Sigma, Darmstadt, Germany).

Benito-González I., López-Rubio A., Martínez-Abad A., Ballester A.R., Falcó I., González-Candelas L., Sánchez G., Lozano-Sánchez J., Borrás-Linares I., Segura-Carretero A, & Martínez-Sanz M. (2019). In-Depth Characterization of Bioactive Extracts from Posidonia oceanica Waste Biomass. Marine Drugs, 17(7), 409.

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Enzymatic Activity Assay Protocol

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Microsomal cytochrome P-450 (cyt.P-450),[15 (link)] glutathione S-transferase (GST) activity[16 (link)] and uridine diphosphate glucuronyl transferase (UDPGT) activity[17 (link)] were determined using the referred methods. Catalase activity using catalase activity assay kit (BioVision, Milpitas, USA), superoxide dismutase (SOD) activity using SOD activity assay kit (BioVision, Mountain View, USA) and protein using modified Lowry protein assay kit (Thermo Scientific, Rockford, USA) were determined.

Ghosh M.K., Patra F., Ghosh S., Hossain C.M, & Mukherjee B. (2014). Antisense oligonucleotides directed against insulin-like growth factor-II messenger ribonucleic acids delay the progress of rat hepatocarcinogenesis. Journal of Carcinogenesis, 13, 2.

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Quantification of Synthetic Lipoproteins

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Synthetic AIPs were purchased from Biopetide Co., Inc. (San Diego, CA). Human LDL was purchased from Biomedical Technologies, Inc., (Stoughton MA). Superose 6 10/300 prepacked columns were obtained from GE Healthcare Life Sciences. Other reagents were obtained as follows: rabbit anti-mouse apoB polyclonal antibody (LS-C20729, LifeSpan Biosciences); alkaline phosphatase conjugated anti-rabbit IgG (Sigma-Aldrich); nitro-blue tetrazolium and 5-bromo-4-chloro-3′-indolyphosphate (NBT/BCIP, Pierce), Modified Lowry Protein Assay Kit (Thermo Scientific); 3–8% Tris-Acetate protein gel (NuPAGE, Novex; Life Technologies); 4-aminopyrazole-(3,4-D)pyrimidine (4APP), (Sigma-Aldrich).

Elmore B.O., Triplett K.D, & Hall P.R. (2015). Apolipoprotein B48, the Structural Component of Chylomicrons, Is Sufficient to Antagonize Staphylococcus aureus Quorum-Sensing. PLoS ONE, 10(5), e0125027.

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Immunogen Preparation for Anti-Daunomycin Serum

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The immunogen was prepared according to our previous method for anti-daunomycin serum using a heterobifunctional agent GMBS [11 (link), 12 (link)]. Briefly, FLV maleate (5 mg, 11.5 μmol) in 2.0 mL of 0.1 M phosphate buffer (PB, pH 7.0) and GMBS (1.6 mg, 5.7 μmol) in 0.5 mL tetrahydrofuran were mixed, constantly stirred, and incubated for 60 min at room temperature (RT), thus yielding a GMBS-acylated FLV solution. The sample was centrifuged for 10 min at 2000 rpm and the supernatant was collected. Acetylmercaptosuccinyl BSA (15 mg, approximately 0.1 μmol) was dissolved in 200 μL of 0.1 M PB and incubated with 50 μL of 0.5 M hydroxylamine (pH 7.4) for 10 min at RT to remove the acetyl group. The resulting mercaptosuccinyl BSA was diluted with 1 mL of 0.1 M PB, then immediately added to the GMBS-acylated FLV supernatant and incubated for 60 min with slow stirring. The conjugate was applied to a 2.5 × 45 cm Sephadex G-75 (Sigma Aldrich Co. Inc. St. Louis, MO, USA) column, previously equilibrated with 10 mM PB and eluted with the same buffer. The eluate, absorbance monitored at 280 nm, was collected in 3 mL fractions and the concentration of the conjugate was determined using the modified Lowry protein assay kit (Thermo Fisher Scientific, Waltham, MA, USA). The peak fractions were used for immunization.

Shin M., Yamamoto Y., Kataoka H, & Saita T. (2022). Development of immunohistochemistry for detecting fluvoxamine in rat tissues using newly prepared monoclonal antibody: its precise localization in small intestine, kidney, and liver of rats. Medical Molecular Morphology, 56(1), 28-37.

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H7N9 Virus Purification and Quantification

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The H7N9 bulks produced in sMDCK cells were purified according to a previous study [22 (link)] with the following modifications. First, 400 mL of the harvested virus was inactivated, and then the cell debris was removed using centrifugation at 1800×g for 30 min. Next, the inactivated virus was further purified using Capto Q and Capto core 700 anion exchange chromatography columns in an AKTA purifier 100 system (GE Healthcare). The flow-through virus solution was diafiltered with PBS using tangential flow filtration with a 100 kDa membrane cassette (Sartorius). Finally, this purified virus bulk was sterilized by using a 0.22 μm filter and stored at 4 °C. The amount of HA antigen in the bulk virus stock was calculated based on the band intensity of the viral protein on a 10% NuPAGE Bis-Tris gel (Thermo Fisher Scientific), and the amount of total viral protein was measured using a Modified Lowry Protein Assay kit (Thermo Fisher Scientific) [23 ].

Tzeng T.T., Chen P.L., Weng T.C., Tsai S.Y., Lai C.C., Chou H.I., Chen P.W., Lu C.C., Liu M.T., Sung W.C., Lee M.S, & Hu A.Y. (2020). Development of high-growth influenza H7N9 prepandemic candidate vaccine viruses in suspension MDCK cells. Journal of Biomedical Science, 27, 47.

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