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Ls 30 spectrofluorometer

Manufactured by PerkinElmer
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The LS 30 spectrofluorometer is a high-performance instrument designed for the analysis of fluorescent samples. It measures the intensity of fluorescence emitted by a sample when exposed to light of a specific wavelength. The LS 30 can be used to determine the concentration of fluorescent analytes, study molecular interactions, and characterize the properties of fluorescent materials.

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Lab products found in correlation

Boc leu ser thr arg amc, by Merck Group (2 mentions) Ac gly pro leu asp amc, by Merck Group (2 mentions) Suc leu leu val tyr amc, by Merck Group (2 mentions) Tri carb 2910 tr, by PerkinElmer (1 mentions) 3 h methyl thymidine, by PerkinElmer (1 mentions) Gf f filter, by Cytiva (1 mentions) Whatman gf f filters, by Cytiva (1 mentions) Tri carb 1600 tr, by Hewlett-Packard (1 mentions)

5 protocols using ls 30 spectrofluorometer

1

E-cadherin Destabilization and Permeability Assay

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Calcium rigidifies the extracellular E-cadherin domain. In the absence of calcium, E-cadherin loses its affinity for the facing E-cadherin which causes cells to lose their adhesion to each other. EGTA was used to chelate calcium and destabilize E-cadherin anchoring bridges between cells. Fully grown CAOMECS were incubated after two weeks with EGTA from sigma at 2.5 mM and 5 mM dissolved in cell culture media for 24 hours. CAOMECS were then harvested and cell lysates were analyzed for E-cadherin levels.

Rabbit oral mucosa epithelial cell sheets were cocultured for two weeks in Transwell® insert permeable support (24 mm insert, 0.4 μm; Corning Incorporated, Kennebunk, ME) with NIH-3T3 feeder cells at the bottom of the 6-multiplate well. When CAOMECS were fully grown, they were incubated with Cascade Blue at 20 μM for 24 hours. CAOMECS were then harvested and fluorescence was measured in 1 μg of total protein from cell media and from CAOMECS cell lysates. Controls were CAOMECS cultured and harvested without Cascade Blue addition. Fluorescence was measured using a Perkin Elmer LS 30 spectrofluorometer at λ excitation 370 nm and λ emission: 430 nm.

Bardag-Gorce F., Hoft R.H., Wood A., Oliva J., Niihara H., Makalinao A., Thropay J., Pan D., Meepe I., Tiger K., Garcia J., Laporte A., French S.W, & Niihara Y. (2016). The Role of E-Cadherin in Maintaining the Barrier Function of Corneal Epithelium after Treatment with Cultured Autologous Oral Mucosa Epithelial Cell Sheet Grafts for Limbal Stem Deficiency. Journal of Ophthalmology, 2016, 4805986.
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2

Proteasome Activity Assay

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One μg of total protein from sample homogenates was used. The reaction mixture contained 50 mM Tris–HCl pH = 8, 1 mM DTT, and 40 μM Suc-Leu-Leu-Val-Tyr-AMC (Sigma Aldrich) substrate for chymotrypsin-like activity or 40 μM of Boc-Leu-Ser-Thr-Arg-AMC for trypsin-like activity or 100 μM of Ac-Gly-Pro-Leu-Asp-AMC (Sigma Aldrich) for Caspase-like activity. To distinguish the 26S proteasome activity from the 20S proteasome activity, 5 mM ATP was added to the reaction mixture. The mixture was then incubated for 30 min at 37 °C. The reaction was stopped by adding 100 mM monochloroacetate and 30 mM sodium acetate pH = 4.3. Fluorescence was determined by measuring the release of AMC (λ excitation: 370 nm, λ emission: 410 nm), using a Perkin Elmer LS 30 spectrofluorometer.
Bardag-Gorce F., Hoft R., Meepe I., Garcia J., Tiger K., Wood A., Laporte A., Pan D., Makalinao A., Niihara R., Oliva J., Florentino A., Gorce A.M., Stark J., Cortez D., French S.W, & Niihara Y. (2017). Proteasomes in corneal epithelial cells and cultured autologous oral mucosal epithelial cell sheet (CAOMECS) graft used for the ocular surface regeneration. The ocular surface, 15(4), 749-758.
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3

Measuring Chlorophyll-a and Bacterial Production

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Samples for chlorophyll-a (Chl-a) were filtered onto Whatman® GF/F filters, extracted overnight in the dark in 95% ethanol, and then measured on a PerkinElmer LS 30 spectrofluorometer (Waltham, MA, United States) operating at excitation and emission wavelengths of 433 and 673 nm, respectively.
Bacterial net production (BP) was measured using the [3H-methyl]-thymidine incorporation method (Fuhrman and Azam, 1982 (link)). Three 1 ml replicates and one killed control were incubated in the dark at 15°C for 1 h with [3H-methyl]-thymidine (84 Ci mmol−1, PerkinElmer®, Massachusetts, United States) at a final concentration of 24 nM. The incubation was stopped by the addition of 100 μl of ice-cold 50% trichloroacetic acid (TCA) and the samples were then centrifuged at 4°C at 13,000 rpm for 10 min. The resulting pellet was washed with 5% trichloroacetic acid (TCA) and, and after adding 1 ml of scintillation cocktail (OptiPhase 3, PerkinElmer), the samples were analyzed in a scintillation counter (PerkinElmer Tri-Carb 2910 TR). Bacterial production was calculated using a conversion factor of 1.4 × 1018 cells mol−1 (Wikner and Hagström, 1999 (link)) and a carbon conversion factor of 20 fg C cell−1 (Lee and Fuhrman, 1987 (link)).
Rodríguez J., Andersson A., Björn E., Timonen S., Brugel S., Skrobonja A, & Rowe O. (2022). Inputs of Terrestrial Dissolved Organic Matter Enhance Bacterial Production and Methylmercury Formation in Oxic Coastal Water. Frontiers in Microbiology, 13, 809166.
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4

Measuring Primary Production Using 14C Method

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Primary production (PP) was measured using the 14C method (Gargas, 1975 ). Five milliliter samples of seawater were added to four 20 mL transparent polycarbonate tubes and mixed with 7.2 μL Na214CO3 (Centralen Denmark, specific activity = 100 μCi mL-1). The tubes were incubated in situ for approximately 3 h at 1 m depth, with one of the replicates being incubated in dark. Next, a sub-sample of 5 mL from each tube was mixed with 150 μL 6 M HCl. After 30 min of bubbling, 15 mL scintillation cocktail was added and thoroughly mixed. The samples were analyzed in a scintillation counter (Beckman Coulter LS 6500/Packard Tri-Carb 1600 TR) and net PP was calculated as describe in Andersson et al. (1996) (link).
Samples for chlorophyll-a (Chl-a) were filtered onto Whatman®GF/F filters, extracted overnight in the dark in 95% ethanol, and then measured on a Perkin Elmer LS 30 spectrofluorometer (Waltham®, Middlesex, MA, United States) operating at excitation and emission wavelengths of 433 and 673 nm, respectively.
Rodríguez J., Gallampois C.M., Timonen S., Andersson A., Sinkko H., Haglund P., Berglund Å.M., Ripszam M., Figueroa D., Tysklind M, & Rowe O. (2018). Effects of Organic Pollutants on Bacterial Communities Under Future Climate Change Scenarios. Frontiers in Microbiology, 9, 2926.
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5

Proteasome Activity Assay

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One μg of total protein from sample homogenates was used. The reaction mixture contained 50 mM Tris–HCl pH = 8, 1 mM DTT, and 40 μM Suc-Leu-Leu-Val-Tyr-AMC (Sigma Aldrich) substrate for chymotrypsin-like activity or 40 μM of Boc-Leu-Ser-Thr-Arg-AMC for trypsin-like activity or 100 μM of Ac-Gly-Pro-Leu-Asp-AMC (Sigma Aldrich) for Caspase-like activity. 5 mM ATP was added to the reaction mixture to distinguish 26S proteasome activity from 20S proteasome activity. The mixture was then incubated for 30 min at 37 °C, and stopped by adding 100 μM monochloroacetate and 30 mM sodium acetate pH = 4.3. Fluorescence was determined by measuring the release of AMC (λ excitation: 370 nm, λ emission: 410 nm), using a Perkin Elmer LS 30 spectrofluorometer.
Bardag-Gorce F., Makalinao A., Meepe I., Hoft R.H., Cortez D., Oliva J., Laporte A., Stark J., Gorce A., Di Lorenzo M., French S.W., Lungo W, & Niihara Y. (2018). Corneal keratin aggresome (CKAGG) formation and clearance by proteasome activation. Heliyon, 4(12), e01012.
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