Spectramax plus spectrophotometer

Manufactured by Molecular Devices

Sourced in United States, United Kingdom

The SpectraMax Plus spectrophotometer is a versatile lab equipment designed for accurate absorbance measurements. It features a wide wavelength range and can be used for a variety of spectroscopic applications in a laboratory setting.

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Lab products found in correlation

Softmax pro v 7, by Molecular Devices (7 mentions) High binding 96 well microtitre plates, by Thermo Fisher Scientific (4 mentions) High binding 96 well microtiter plates, by Thermo Fisher Scientific (4 mentions) Hrp conjugated goat anti human igg, by Jackson ImmunoResearch (4 mentions) Immulon 4hbx plate, by Thermo Fisher Scientific (3 mentions) Tmb substrate chromogen, by Agilent Technologies (3 mentions) Avidin horseradish peroxidase, by BD (2 mentions) Biotinylated goat anti mouse total igg, by Jackson ImmunoResearch (2 mentions) Recombinant human fcγr ectodomains, by Sino Biological (2 mentions) Np bsa, by Biosearch Technologies (2 mentions) Visulize factor 7 antigen elisa kit, by Affinity Biologicals (2 mentions) Isocitric acid, by Merck Group (2 mentions) Nadph, by Merck Group (2 mentions) Goat anti mouse igg, by Jackson ImmunoResearch (2 mentions) Sureblue reserve 3, by Avantor (2 mentions) 384 well elisa plates, by Corning (2 mentions) Mts activity assay, by Promega (2 mentions) Bca protein assay kit, by Thermo Fisher Scientific (2 mentions) Dc protein assay kit, by Bio-Rad (1 mentions) Hepes, by Thermo Fisher Scientific (1 mentions)

Spelling variants of this product

SpectraMax Plus (371 citations) SpectraMax spectrophotometer (65 citations) SpectraMax Plus 384 spectrophotometer (57 citations) SpectraMax Plus microplate spectrophotometer (26 citations) SPECTRAmax PLUS Microplate Spectrophotometer Plate Reader (6 citations) SpectraMax® ABS Plus spectrophotometer (4 citations) SpectraMax Plus 384 UV-VIS Spectrophotometer (4 citations) SpectraMax Plus UV-visible spectrophotometer (2 citations)

55 protocols using spectramax plus spectrophotometer

Kinetic Analysis of Mutant IDH1 and YF Variants

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20 ng purified IDH1 and YF variant proteins that pre-treated with or without recombinant active tyrosine kinases in an in vitro kinase assay were incubated with various concentrations of NADP⁺ (0–200 μM; Sigma-Aldrich) or isocitrate acid (0–200 μM; Sigma-Aldrich) and 1 mM isocitric Acid (Sigma-Aldrich) or 0.5 mM NADP⁺ (Sigma-Aldrich), respectively at 100 μl enzyme activity assay buffer (25 mM Tris-HCl pH7.5), 10 mM MgCl₂, 5 mM DTT). Absorbance at 340 nm was measured every 20 seconds for 5 minutes using a SpectraMax Plus spectrophotometer (Molecular Devices).
20 ng purified IDH1 R132H and YF variants proteins that pre-treated with or without recombinant active tyrosine kinases in an in vitro kinase assay were incubated with various concentrations of NADPH (0–10μM; Sigma-Aldrich) and 1.5 mM α-KG (Sigma-Aldrich) or various concentrations of α-KG (0–1500 μM; Sigma-Aldrich) and 15 μM NADPH (Sigma-Aldrich) at 100 μl enzyme activity assay buffer (25 mM Tris-HCl (pH7.5), 10 mM MgCl₂, 5 mM DTT). Absorbance at 340 nm was measured every 20 seconds for 5 minutes using a SpectraMax Plus spectrophotometer (Molecular Devices). Non-linear regression analysis (Michaelis-Menten) was performed in Graphpad Prism 6.0.

Chen D., Xia S., Wang M., Lin R., Li Y., Mao H., Aguiar M., Famulare C.A., Shih A.H., Brennan C.W., Gao X., Pan Y., Liu S., Fan J., Jin L., Song L., Zhou A., Mukherjee J., Pieper R.O., Mishra A., Peng J., Arellano M., Blum W.G., Lonial S., Boggon T.J., Levine R.L, & Chen J. (2019). Mutant and wild-type isocitrate dehydrogenase 1 share enhancing mechanisms involving distinct tyrosine kinase cascades in cancer. Cancer discovery, 9(6), 756-777.

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Quantifying Cell Protein via NaOH Lysis

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Another method was used to measure cell protein in some experiments. After removal of the media, the cells were used for total cell protein measurements as follows. One mL of 0.1 N NaOH was added to the cells in each well and the mixture was frozen at − 20 °C overnight. The following day, the cell lysate was harvested, and protein concentrations were determined using a DC Protein assay kit (Bio-Rad, Hercules, CA). Bovine Serum Albumin reference standard (10 µL) or cell lysate (10 µL) was pipetted into a cell of a Microplate. Reagents A (25 µL) and Reagent B (200 µL) were then added to each well (Reagent A and B are as described by the manufacturer of the DC Protein assay kit) and incubated at room temperature for 15 min. At the end of this incubation, absorbance was measured at 690 nm in a Spectra Max Plus Molecular Devices spectrophotometer.

Srivastava R.A., Cornicelli J.A., Markham B, & Bisgaier C.L. (2018). Gemcabene, a first-in-class lipid-lowering agent in late-stage development, down-regulates acute-phase C-reactive protein via C/EBP-δ-mediated transcriptional mechanism. Molecular and Cellular Biochemistry, 449(1), 167-183.

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Photosynthetic Pigments and Biomolecules in Tomato Leaves

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Photosynthetic pigments extracted and determined according to Xiong^{69 (link)} method. 0.1 g of fresh tomato leaves were grinded in liquid nitrogen using a mortar and pestle. The concentration of pigments was calculated according to the following formulae⁷⁰:

C h l o r o p h y l l a (mg L^{- 1}) = 16.82 \cdot A 665 - 9.28 \cdot A 652

C h l o r o p h y l l b (mg L^{- 1}) = 36.92 \cdot A 652 - 16.54 \cdot A 665

C a r o t e n o i d s (mg L^{- 1}) = (1000 \cdot A 470 - 1.91 \cdot C a - 95.15 \cdot C b) / 225

Soluble proteins in tomato leaves was extracted according to Fleurence^{71 (link)} and determined following Bradford⁶⁶ method by recording absorbance at 595 nm by Spectra Max Plus Molecular Devices spectrophotometer using BSA as standard. Total sugar was determined according to phenol–sulfuric method^{67 (link)}. Total phenols were calorimetrically determined using Folin-Ciocalteu reagent as described by^{72 (link)}.

Fal S., Aasfar A., Ouhssain A., Choukri H., Smouni A, & El Arroussi H. (2023). Aphanothece sp. as promising biostimulant to alleviate heavy metals stress in Solanum lycopersicum L. by enhancing physiological, biochemical, and metabolic responses. Scientific Reports, 13, 6875.

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Intracellular Sodium Regulation in Chondrocytes

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Sterilized 0.9% NS were purchased from Baxter (Deerfield, IL, USA), and culture media (DMEM/F-12 with supplements) served as a control for all experiments. HEPES (Life Technologies) as a zwitterionic sulfonic acid buffering agent and sodium bicarbonate (NaHCO₃; Research Products International) were added to the NS for final concentrations of 25 mM and 0.5 mM, respectively. The pH scales for all 4 irrigation solutions were measured using a pH meter (Accumet^TM AB315, Thermo Fisher Scientific, Waltham, MA, USA) before and after exposure to chondrocytes. All solutions were incubated for up to 3 h in a static culture condition.
The amounts of intracellular sodium were measured using a cell-permeant sodium fluorescent indicator (SBFI-AM, Santa Cruz Biotechnology, Dallas, TX, USA) according to the manufacturer’s instruction. Briefly, bovine chondrocytes were exposed with culture media (control), 0.9% NS, 25 mM HEPES, or 0.5 mM sodium bicarbonate (NaHCO₃) for 30 min, and then 10 µM SBFI-AM dissolved in anhydrous dimethyl sulfoxide (Biotium, Fremont, CA, USA) mixed with 0.1% (w/v) F-127 Pluronic acid (Millipore Sigma) was added. After 1 h incubation, the samples were gently centrifuged (50× g for 30 s (s)) and measured for fluorescence using a SpectraMax Plus spectrophotometer (Molecular Devices, San Jose, CA, USA). The raw data were normalized by the control.

Hlas A., Ganesh V., Marks J., He R., Salem A.K., Buckwalter J.A., Duchman K.R., Shin K., Martin J.A, & Seol D. (2024). Buffering Mitigates Chondrocyte Oxidative Stress, Metabolic Dysfunction, and Death Induced by Normal Saline: Formulation of a Novel Arthroscopic Irrigant. International Journal of Molecular Sciences, 25(2), 1286.

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ELISA for Anti-HIV Gag Antibodies

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Immulon 4HBX plates (Thermo Scientific) were coated overnight at 4°C with HIV Gag protein diluted in 0.1 M Carbonate Buffer (pH 9.8). Plates were then blocked with 1% FBS/PBS, and plasma from Gag immunized mice was applied in serial 10-fold dilutions in ELISA diluent (0.1% FBS/PBS) and incubated for 1 h at 37°C. Biotinylated Goat-anti-mouse total IgG (Jackson Immuno-Research, Westgrove, Pennsylvania) was added and incubated for 1 h at 37°C. For detection, Avidin-Horse Radish Peroxidase (BD) was added and incubated for 30 minutes at room temperature, followed by the addition of TMB substrate-chromogen (Dako, Glostrup, Denmark) and a 2N sulfuric acid stop solution. Washing was performed between steps with PBS + 0.05% Tween 20. Plates were read on a SpectraMax Plus spectrophotometer (Molecular Devices) at 450 nm. Data was analyzed in Prism to generate a non-linear regression fit to estimate EC50 (midpoint titer) or EC05 (endpoint titers).

Lynn G.M., Laga R., Darrah P.A., Ishizuka A.S., Balaci A.J., Dulcey A.E., Pechar M., Pola R., Gerner M.Y., Yamamoto A., Buechler C.R., Quinn K.M., Smelkinson M.G., Vanek O., Cawood R., Hills T., Vasalatiy O., Kastenmuller K., Francica J.R., Stutts L., Tom J.K., Ryu K.A., Esser-Kahn A.P., Etrych T., Fisher K.D., Seymour L.W, & Seder R.A. (2015). In vivo characterization of the physicochemical properties of TLR agonist delivery that enhance vaccine immunogenicity. Nature biotechnology, 33(11), 1201-1210.

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Quantifying Biofilm Formation by Crystal Violet

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In order to assess biofilm mass after 24 h, the biofilm was stained with crystal violet. Briefly, after removing the growth media, each biofilm was washed three times with sterile distilled H₂O (dH₂O) and the plates were blotted on absorbent paper prior to 30 min room-temperature incubation with 10% formaldehyde (Sigma-Aldrich). After three additional dH₂O washes, a 0.5% crystal violet solution (Sigma-Aldrich) was incubated on the biofilm for 30 min followed by additional dH₂O washes to remove excess crystal violet. Next 2-propanol was added for 60 min to extract the crystal violet prior to reading the optical density of each well at 490 nm on a SpectraMax Plus spectrophotometer (Molecular Devices, Sunnyvale, CA, USA).

Wagenknecht D.R, & Gregory R.L. (2021). Analyses of the Effects of Arginine, Nicotine, Serotype and Collagen-Binding Proteins on Biofilm Development by 33 Strains of Streptococcus mutans. Frontiers in Oral Health, 2, 764784.

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Measuring Cell Proliferation with BrdU Assay

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A cell proliferation enzyme-linked immunosorbent assay (BrdU kit; Amersham Biosciences, Piscataway, NJ, USA) was used to measure the incorporation of BrdU during DNA synthesis. Briefly, islets were transduced with either Ad-BTC or Ad-LacZ and then treated with interleukin-1β (1 U ml⁻¹) and interferon-γ (100 U ml⁻¹). After a 48-h incubation, BrdU (10 μM) was added to the culture medium for 12 h, the BrdU-labeled cells were fixed and the DNA was denatured in fixative solution for 30 min at room temperature. Islets were incubated with peroxidase-conjugated anti-BrdU antibody for 2 h at room temperature and washed three times with washing solution. Immune complexes were detected by the 3, 3′, 5, 5′-tetramethylbenzidine substrate reaction and absorbance measured at 405 nm with a Spectra Max Plus spectrophotometer (Molecular Devices, Sunnyvale, CA, USA).

Song M.Y., Bae U.J., Jang K.Y, & Park B.H. (2014). Transplantation of betacellulin-transduced islets improves glucose intolerance in diabetic mice. Experimental & Molecular Medicine, 46(5), e98-.

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Quantifying HDAC Inhibitor-Iron Complexes

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Formation of HDACi-Fe complexes could be visually assessed by the appearance of a dark purple color upon complexation for both SAHA-Fe and LAQ-Fe. The UV-Vis absorption spectrum was monitored over a broad range of wavelength using a SpectraMax Plus spectrophotometer (Molecular Devices). Peak absorbance at 500 nm was used to quantify complex concentration. The method of continuous variation was used to determine the reaction stoichiometry between SAHA/LAQ and Fe (18 (link)). For example, SAHA and FeCl₃ were mixed in 10 mM HCl solutions at different molar ratios while keeping the total mole concentration of SAHA and Fe constant at 0.4 mM. Reaction mixtures were measured at 500 nm, with absorbance directly correlating to increasing presence of HDACi-Fe complexes; this absorbance was then plotted with respect to mole percentage of drug to generate a maximum curve. The point of intersection from the tangents of the curves from each side was used to determine the theoretical binding stoichiometry of SAHA or LAQ to Fe.

Wang Y., Tu S., Steffen D, & Xiong M.P. (2014). Iron Complexation to Histone Deacetylase Inhibitors SAHA and LAQ824 in PEGylated Liposomes Can Considerably Improve Pharmacokinetics in Rats. Journal of pharmacy & pharmaceutical sciences : a publication of the Canadian Society for Pharmaceutical Sciences, Societe canadienne des sciences pharmaceutiques, 17(4), 583-602.

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Cytotoxicity Evaluation of GT3 and AT

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LNCaP, PC-3, and RWPE-1 cells were dosed with GT3 or AT at concentrations of 10, 20, 40, 60, and 80 μM. After treatment, 3-(4, 5-methylthiazol-2-yl)-2, 5-diphenyl-tetrazolium bromide (MTT) was added and incubated for 3 h (Invitrogen, Carlsbad, CA). Formazan products were solubilized with acidified SDS overnight. Optical density was measured at 570 nm using a Spectramax Plus spectrophotometer (Molecular Devices, Sunnyvale, CA, USA). All experiments were done at least three times.

Moore C., Palau V.E., Mahboob R., Lightner J., Stone W, & Krishnan K. (2020). Upregulation of pERK and c-JUN by γ-tocotrienol and not α-tocopherol are essential to the differential effect on apoptosis in prostate cancer cells. BMC Cancer, 20, 428.

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FcγR Binding Assay with Immune Complexes

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Recombinant human FcγR ectodomains (Sinobiological) (5 μg ml⁻¹) were immobilized into high-binding 96-well microtitre plates (Nunc), and after overnight incubation at 4 °C, plates were blocked with PBS plus 2% (w/v) BSA and 0.05% (v/v) Tween20 for 2 h. IgG immune complexes were prepared by incubating for 1 h at 4 °C Fc variants of the anti-NP (4-hydroxy-3-nitrophenylacetyl) monoclonal antibody Ab 3B62 with NP-BSA (27 conjugation ratio, Biosearch Technologies) at a molar ratio of 1:10 (antigen:antibody). IgG immune complexes or monomeric IgG (for FcγRI) were serially diluted (1:3 consecutive dilutions in PBS starting at 10 μg ml⁻¹ (IgG concentration) for immune complexes or 1 μg ml⁻¹ for monomeric IgG) and applied to FcγR-coated plates. After 1 h incubation at room temperature, bound IgG was detected using horseradish peroxidase (HRP)-conjugated goat F(ab’)₂ anti-human IgG (1 h; 1:5,000; Jackson Immunoresearch). Plates were developed using the TMB (3,3′,5,5′-tetramethylbenzidine) two-component peroxidase substrate kit (KPL) and reactions were stopped with the addition of 1 M phosphoric acid. Absorbance at 450 nm was immediately recorded using a SpectraMax Plus spectrophotometer (Molecular Devices) and background absorbance from negative control samples was subtracted. Data were collected and analysed using SoftMax Pro v.7.0.2 software (Molecular Devices).

Bournazos S., Corti D., Virgin H.W, & Ravetch J.V. (2020). Fc-optimized antibodies elicit CD8 immunity to viral respiratory infection. Nature, 588(7838), 485-490.

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