Polystyrene microtiter plates

Manufactured by Greiner

Sourced in Austria, Spain

Polystyrene microtiter plates are a type of laboratory equipment used for a variety of applications. They consist of a flat plate with multiple small wells, typically made of polystyrene material. These plates are designed to hold small volumes of liquid samples, such as solutions, suspensions, or reagents, for various experimental or analytical purposes.

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Lab products found in correlation

Spectrostar nano, by BMG Labtech (3 mentions) Sigmafast opd, by Merck Group (2 mentions) Automated plate reader, by Tecan (2 mentions) Polarstar omega spectrophotometer, by BMG Labtech (1 mentions) Potassium chloride (kcl), by ITW Reagents (1 mentions) Sodium chloride (nacl), by ITW Reagents (1 mentions) Nah2po4 h2o, by Merck Group (1 mentions) Kh2po4, by ITW Reagents (1 mentions) Pherastar fs plate reader, by BMG Labtech (1 mentions) Crystal violet, by Merck Group (1 mentions) Fitc labeled lps, by Merck Group (1 mentions) Lf from human milk, by Merck Group (1 mentions) Bovine serum albumin heat shock fraction, by Merck Group (1 mentions) Melittin from honey bee venom, by Merck Group (1 mentions) O phenylenediamine, by Merck Group (1 mentions)

Spelling variants of this product

Microtiter plates (57 citations) Polystyrene plates (7 citations) 96-well polystyrene microtiter plates (5 citations) Sterile 24-well polystyrene microtiter plates (2 citations) Polystyrene microtiter 96-well plates (2 citations) Flat bottom polystyrene microtiter plates (2 citations)

10 protocols using polystyrene microtiter plates

ELISA for S. haematobium Infection Detection

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The urine of infected individuals (n = 98) from an area in Zimbabwe endemic for S. haematobium infection was analyzed by ELISA using all S. haematobium protein preparations described earlier. Urine from Australian volunteer donors that had never travelled to schistosomiasis endemic areas was used as a negative control (n = 14).
Polystyrene microtiter plates (Greiner Bio-One, Austria) were coated overnight at 4°C with 50 μl/well of a 5 μg/ml solution of S. haematobium adult ES, adult tegument, SEA or egg ES in 0.1 M carbonate coating buffer, pH 9.6. The plates were washed three times with PBS/0.05% Tween20 (PBST) and blocked for two hours at 37°C using 5% skimmed milk in PBST, followed by three wash steps in PBST for 15 min each. Plates were then incubated with 50 μl of urine (diluted 1:5 in PBS) and incubated at 37°C for 1.5 h followed by 3 washes using PBST. Fifty μl of HRP-conjugated polyclonal anti-human IgG (Sigma-Aldrich) was added at dilution of 1:5,000 and incubated for 1 hour at 37°C. Finally, plates were washed 3× with PBST and incubated with 3,3',5,5;-tetramethylbenzidine (TMB, Thermo Fisher Scientific, USA) for 10 min at RT in the dark. The reaction was stopped by adding 3 M HCl and absorbance read at 450 nm using a POLARstar Omega spectrophotometer (BMG Labtech, Australia).

Sotillo J., Pearson M.S., Becker L., Mekonnen G.G., Amoah A.S., van Dam G., Corstjens P.L., Murray J., Mduluza T., Mutapi F, & Loukas A. (2019). In-depth proteomic characterization of Schistosoma haematobium: Towards the development of new tools for elimination. PLoS Neglected Tropical Diseases, 13(5), e0007362.

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Optimizing rFhpCL Concentration for ELISA

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To investigate the optimal concentration of each rFhpCL for use as target in indirect ELISA, we tested several concentrations of each antigen in the range of 1–10 μg/mL in PBS. Polystyrene microtiter plates (Greiner Bio-One; Soria-Melguizo, Madrid, Spain) were coated with 100 μL/well of each rFhpCL dilution and incubated for 2 h at 37 °C. The plates were then washed three times with PBS and blocked with 200 μL/well of 1.5% sodium caseinate in PBS for 1 h at RT. Aliquots of 100 μL of an appropriate dilution of mAb MM3 (1/2000) in PBS containing 0.05% Tween 20 and 1% skimmed dry milk (PBS-T-SM) were then added to each well, and the plates were incubated for 30 min at RT with shaking at 750 rpm. The plates were then washed five times with PBS-T, and bound MM3 antibodies were detected after incubation with HRP-labeled goat anti-mouse IgG secondary antibodies (Bio-Rad, Madrid, Spain) diluted 1/3000 in PBS-T-SM for 30 min at RT with orbital shaking at 750 rpm. The plates were then washed, as above, and incubated for 20 min at RT with 100 μL/well of the enzyme substrate OPD (SigmaFast OPD, Sigma-Aldrich). Finally, the optical density (OD) was measured at 492 nm. Recombinant procathepsin dilutions containing the same equivalent concentration (i.e., yielding the same OD signal with mAb MM3) were selected for use in an indirect ELISA, as indicated below.

Martínez-Sernández V., Perteguer M.J., Hernández-González A., Mezo M., González-Warleta M., Orbegozo-Medina R.A., Romarís F., Paniagua E., Gárate T, & Ubeira F.M. (2018). Comparison of recombinant cathepsins L1, L2, and L5 as ELISA targets for serodiagnosis of bovine and ovine fascioliasis. Parasitology Research, 117(5), 1521-1534.

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ELISA for SARS-CoV-2 antibody detection

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In-house ELISAs were performed with nucleocapsid (Nc) or full-length spike (Sfull) or spike domain S1 or S2 recombinant proteins. Briefly, recombinant Nc or S were coated on 96-well polystyrene microtiter plates (Greiner Bio-One GmbH, Austria) at a concentration of 1 µg/ml in 100 µl coating bicarbonate buffer (pH9.8) at 4 °C overnight. After blocking with 1% bovine serum albumin (BSA), the plates were washed thoroughly with phosphate-buffered saline (PBS)-Tween. Patient and control sera were diluted 1:25 and loaded on the plates in duplicates. Plates were further incubated for 1 h at room temperature and detected by a goat anti-human IgG secondary antibody labelled with HRP (SouthernBiotech). Absorbance values of samples and positive and negative controls were measured at 450 nm, with a reference wavelength of 620 nm using an automated plate reader (Tecan Group Ltd, Switzerland). Anti-SARS-CoV-2 Sfull, S1, S2 and Nc IgG levels were performed in normalized values (OD sample / OD positive control). Cut-off values were determined by the mean value plus 2 times the standard deviation (SD) of the negative control.

Sinkovits G., Schnur J., Hurler L., Kiszel P., Prohászka Z.Z., Sík P., Kajdácsi E., Cervenak L., Maráczi V., Dávid M., Zsigmond B., Rimanóczy É., Bereczki C., Willems L., Toonen E.J, & Prohászka Z. (2022). Evidence, detailed characterization and clinical context of complement activation in acute multisystem inflammatory syndrome in children. Scientific Reports, 12, 19759.

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Biofilm Formation in C. glabrata

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C. glabrata strains were tested regarding their capacity to form biofilm on a polystyrene surface, recurring to the Presto Blue Cell Viability Assay. For that, the C. glabrata strains were grown in SDB (pH 5.6) medium and collected by centrifugation at mid-exponential phase. The cells were inoculated with an initial OD_600nm = 0.05 ± 0.005 in 96-well polystyrene microtiter plates (Greiner) in SDB (pH 5.6) medium. Cells were cultivated at 30 °C during 24 ± 0.5 h with mild orbital shaking (70 r.p.m.). After the incubation time, each well was washed two times with 100 µL of sterile phosphate-buffered saline (PBS) pH 7.4 (PBS contained per liter: 8 g NaCl (Panreac), 0.2 g KCl (Panreac), 1.81 g NaH₂PO₄.H₂O (Merck), and 0.24 g KH₂PO₄ (Panreac), to remove the cells unattached to the formed biofilm. Then, Presto Blue reagent was prepared in a 1 : 10 solution in the medium used for biofilm formation, adding 100 µL of the solution to each well. Plates were incubated at 37 °C for 30 min. Afterwards, absorbance reading, at the wavelength of 570 and 600 nm for reference, was determined in a microplate reader (SPECTROstar Nano, BMG Labtech).

Cavalheiro M., Pereira D., Formosa-Dague C., Leitão C., Pais P., Ndlovu E., Viana R., Pimenta A.I., Santos R., Takahashi-Nakaguchi A., Okamoto M., Ola M., Chibana H., Fialho A.M., Butler G., Dague E, & Teixeira M.C. (2021). From the first touch to biofilm establishment by the human pathogen Candida glabrata: a genome-wide to nanoscale view. Communications Biology, 4, 886.

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Quantifying Biofilm Formation in P. aeruginosa

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Biofilm formation was examined in a modified microtiter plate assay using crystal violet as described previously [53 (link)]. Overnight P. aeruginosa cultures grown in LB were diluted to OD_600nm = 0.001 in the desired medium with appropriate supplements. A total of 100 µL aliquots were dispensed into 96-well polystyrene microtiter plates (Greiner). A minimum of four technical replicates within each experiment was carried out and each experiment was reproduced at least three times. Bacteria were incubated (37 °C) under aerobic and anaerobic conditions for 20 h. Total bacterial growth was determined using optical density (600 nm) in a PHERAstar FS plate reader (BMG Labtech). Biofilms were washed and stained with 0.1% (w/v) crystal violet (CV) for 15 min at room temperature. After vigorous washing with water, the stained biofilms were made soluble with 30% acetic acid and the biofilm density determined by absorbance (550 nm).

Mettrick K., Hassan K., Lamont I, & Reid D. (2020). The Iron-chelator, N,N’-bis (2-hydroxybenzyl) Ethylenediamine-N,N’-diacetic acid is an Effective Colistin Adjunct against Clinical Strains of Biofilm-Dwelling Pseudomonas aeruginosa. Antibiotics, 9(4), 144.

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SARS-CoV-2 Spike Protein ELISA Protocol

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In-house ELISA tests were performed with SARS-CoV-2 full-length spike (S) recombinant protein (R&D systems, Minneapolis, USA). Briefly, recombinant S protein was coated on 96-well polystyrene microtiter plates (Greiner Bio-One GmbH, Austria) at a concentration of 1 µg/ml in 100 µl of coating bicarbonate buffer (pH 9.8) at 4 °C overnight. After blocking with 1% bovine serum albumin (BSA), we washed the plates thoroughly with phosphate-buffered saline (PBS)-Tween. Patient and control sera were diluted 1:25 and loaded on the plates in duplicates. Plates were further incubated at room temperature for 1 h and developed with HRP-labeled goat anti-human IgG secondary antibody (SouthernBiotech, USA). Absorbance values of samples and positive and negative controls were measured at 450 nm, at a reference wavelength of 620 nm using an automated plate reader (Tecan Group Ltd, Switzerland). Cut-off values were determined by the mean value plus two times the standard deviation (SD) of the negative control.

Kiszel P., Sík P., Miklós J., Kajdácsi E., Sinkovits G., Cervenak L, & Prohászka Z. (2023). Class switch towards spike protein-specific IgG4 antibodies after SARS-CoV-2 mRNA vaccination depends on prior infection history. Scientific Reports, 13, 13166.

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Biofilm Formation Assay for Candida glabrata

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C. glabrata strains were tested for their capacity for biofilm formation by use of the crystal violet method. For that, the C. glabrata strains were grown in SDB medium and harvested by centrifugation at mid-exponential phase. The cells were inoculated with an initial OD₆₀₀ of 0.05 ± 0.005 in 96-well polystyrene microtiter plates (Greiner) in either SDB (pH 5.6) or RPMI (pH 4) medium. Cells were cultivated at 30°C for 15 ± 0.5 h or 4 ± 0.5 h with mild orbital shaking (70 rpm). After the incubation time, each well was washed three times with 200 µl of deionized water to remove cells not attached to the biofilm matrix. Then 200 µl of a 1% crystal violet (Merck) alcoholic solution was used to stain the biofilm present in each well. Following 15 min of incubation with the dye, each well was washed with 250 µl of deionized water. The stained biofilm was eluted in 200 µl of 96% (vol/vol) ethanol, and the absorbance of each well was read in a microplate reader at a wavelength of 590 nm (SPECTROstar Nano; BMG Labtech).

Cavalheiro M., Costa C., Silva-Dias A., Miranda I.M., Wang C., Pais P., Pinto S.N., Mil-Homens D., Sato-Okamoto M., Takahashi-Nakaguchi A., Silva R.M., Mira N.P., Fialho A.M., Chibana H., Rodrigues A.G., Butler G, & Teixeira M.C. (2018). A Transcriptomics Approach To Unveiling the Mechanisms of In Vitro Evolution towards Fluconazole Resistance of a Candida glabrata Clinical Isolate. Antimicrobial Agents and Chemotherapy, 63(1), e00995-18.

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Protein-based ELISA Assay Protocol

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FITC-labeled LPS from Escherichia coli serotypes O111:B4 and O55:B5, PMX sulphate salt, ovalbumin (OVA, grade V), bovine serum albumin (BSA, heat shock fraction), myoglobin from equine skeletal muscle (MYO), HB from bovine blood, LF from human milk, melittin from honey bee venom (MEL), histone f1 fraction from calf thymus (HF1) and SigmaFast OPD were purchased from Sigma-Aldrich (Madrid, Spain). Bovine casein (CAS, Hammarstein grade) was supplied by BDH Prolabo (VWR International Eurolab, Barcelona, Spain). Biotinylated PMX was obtained from Hycult Biotech (Uden, The Netherlands). Lysozyme from chicken egg white (LSZ) and deglycosylated avidin from hen egg white were procured from Fluka Analytical (Sigma-Aldrich, Steinheim, Germany). HRP-conjugated sheep anti-FITC was provided by Abd Serotec (Oxford, UK). Tween^® 20 (TW2) and Triton^® X-100 (TTX) were purchased from Merck KGaA (Darmstadt, Germany). Polystyrene microtiter plates were provided by Greiner Bio-One (Soria-Melguizo, Madrid, Spain). The synthetic peptide P3L (MCQCVQKYGTEFCKKRLA, 90% pure) from Anisakis simplex was synthesized at the Centro Nacional de Microbiología (Instituto de Salud Carlos III, Madrid, Spain). The synthetic protein corresponding to protein sMF6p/FhHDM-1 secreted by Fasciola hepatica (MF6p, gb CCA61804.1, 95% pure) was obtained from GeneCust Europe (Dudelange, Luxembourg).

Martínez-Sernández V., Orbegozo-Medina R.A., Romarís F., Paniagua E, & Ubeira F.M. (2016). Usefulness of ELISA Methods for Assessing LPS Interactions with Proteins and Peptides. PLoS ONE, 11(6), e0156530.

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Quantifying Bacterial Biofilm Formation

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Biofilm formation on the surface of polystyrene was quantified using the dye crystal violet, based on previously described methods [47 (link)]. Briefly, polystyrene microtiter plates (Greiner Bio-One) containing LB liquid medium were inoculated with exponential phase bacterial cultures using an initial OD₆₄₀ of 0.05 and incubated for 24 and 48 h at 37 °C without agitation. Quantification of the biofilm formed was accomplished by removing the unattached bacteria after the indicated time of incubation and rinsing the wells three times with deionized water. The attached bacteria were then stained by adding to each well 200 μL of a 1% (w/v) crystal violet solution and incubating for 15 min at room temperature. After incubation the solution was removed and three gentle washes with deionized water were performed. Biofilm quantification was performed after dissolving the bound crystal violet with 200 μL of 95% ethanol and measuring the absorbance at 595 nm in a microplate reader SpectroStar Nano (BMG Labtech, Ortenberg, Germany). Results are mean values of at least 12 replicates from three independent experiments.

Seixas A.M., Sousa S.A., Feliciano J.R., Gomes S.C., Ferreira M.R., Moreira L.M, & Leitão J.H. (2021). A Polyclonal Antibody Raised against the Burkholderia cenocepacia OmpA-like Protein BCAL2645 Impairs the Bacterium Adhesion and Invasion of Human Epithelial Cells In Vitro. Biomedicines, 9(12), 1788.

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Detecting E. coli O157:H7 Antibodies in Milk

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Example 5

Detection of Specific Antibodies Against E. Coli O157:H7 in Milk by Enzyme Linked Immunosorbent Assay (ELISA)

For milk antibody screening, the ELISA was performed. Flat bottomed 96 well polystyrene microtiter plates (Greiner, Germany) were coated with 100 μl of 10 μg/ml E. coli O157:1-17 antigens in carbonate-bicarbonate buffer (pH 9.6) overnight at 4° C. The plates were washed 3 times with 100 μl of 0.15 Molar (M) Phosphate Buffered Saline (PBS) (pH 7.2) containing 0.05% Tween 20 and blocked with 100 μl of 2% bovine serum albumin (BSA) in PBS for one hour at room temperature (RT). The Plates were washed again and 100 μl of serum samples diluted at 1:100 in 1% BSA were added in duplicates and incubated one hour at RT, whereas, the milk samples were added in duplicates without dilution Negative and positive control samples were incorporated in each plate. After washing, 100 μl of one of the horse radish peroxidase (HRP) conjugated protein A and protein G were diluted at 1:1000 in 1% BSA, and were added separately to each well. The Plates were incubated for one hour at RT and washed again. Finally, 100 μl of 0.1% O-phenylenediamine (Sigma, USA) containing hydrogen peroxide in 0.1 M citrate buffer (pH 4.5) were added to each well and absorbance was measured at 490 nm using ELISA reader (AsysHitech, Switzerland).

US10278404B2. Immunized camel milk-based composition for the treatment or prevention of gastrointestinal infections (2019-05-07). None [JO], None [JO], None [JO], None [GB]. Inventors: Khaled Mahmood Al-Qaoud [JO], Penelope Agmad Shihab [JO], Luay Fawzi Abu-Oatousch [JO], Christopher R. Lowe [GB].

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