http://lod.bco-dmo.org/id/dataset/997078 eng; USA utf8 dataset Highest level of data collection, from a common set of sensors or instrumentation, usually within the same research project Biological and Chemical Oceanography Data Management Office (BCO-DMO) Unavailable 508-289-2009 WHOI MS#36 Woods Hole MA 02543 USA info@bco-dmo.org http://www.bco-dmo.org Monday - Friday 8:00am - 5:00pm For questions regarding this resource, please contact BCO-DMO via the email address provided. pointOfContact 2026-04-20 ISO 19115-2 Geographic Information - Metadata - Part 2: Extensions for Imagery and Gridded Data ISO 19115-2:2009(E) Enzyme activity of Alteromonas macleodii exudates 2026-04-20 publication 2026-04-20 revision BCO-DMO Linked Data URI 2026-04-20 creation http://lod.bco-dmo.org/id/dataset/997078 Steven Biller Wellesley College principalInvestigator James Jeffrey Morris University of Alabama at Birmingham principalInvestigator Zhiying Lu University of Alabama at Birmingham principalInvestigator Biological and Chemical Oceanography Data Management Office (BCO-DMO) Unavailable 508-289-2009 WHOI MS#36 Woods Hole MA 02543 USA info@bco-dmo.org http://www.bco-dmo.org Monday - Friday 8:00am - 5:00pm For questions regarding this resource, please contact BCO-DMO via the email address provided. publisher Cite this dataset as: Morris, J. J., Biller, S., Lu, Z. (2026) Enzyme activity of Alteromonas macleodii exudates. Biological and Chemical Oceanography Data Management Office (BCO-DMO). (Version 1) Version Date 2026-04-20 [if applicable, indicate subset used]. http://lod.bco-dmo.org/id/dataset/997078 [access date] Enzyme Activity Dataset Description: Methods and Sampling: &lt;p&gt;&lt;em&gt;&lt;strong&gt;Strains and culture conditions:&amp;nbsp;&lt;/strong&gt; &lt;/em&gt;All strains used in this study were taken from those used for a Long-Term Phytoplankton Evolution (LTPE) experiment (1). &lt;em&gt;Prochlorococcus&lt;/em&gt; strains were streptomycin-resistant derivates of the high light-adapted strain MIT9312 obtained as described previously (2, 3), either before (Ancestor) or after 500 generations of evolution at either 400 ppm or 800 ppm pCO&lt;sub&gt;2&lt;/sub&gt; conditions (i.e., modern day or projected year 2100 conditions (4)). &lt;em&gt;Alteromonas&lt;/em&gt; strains were derivatives of strain EZ55, originally isolated from a &lt;em&gt;Prochlorococcus&lt;/em&gt; MIT9215 culture (3). As with our &lt;em&gt;Prochlorococcus&lt;/em&gt; strains, we used both ancestral and evolved varieties of EZ55 co-evolved with &lt;em&gt;Prochlorococcus &lt;/em&gt;at the two pCO&lt;sub&gt;2&lt;/sub&gt; treatments and subsequently isolated. &lt;em&gt;Prochlorococcus&lt;/em&gt; cultures were revived from cultures cryopreserved with 7.5% DMSO in liquid nitrogen vapor, and &lt;em&gt;Alteromonas &lt;/em&gt;cultures were revived from cultures preserved with 20% glycerol stored at -80&lt;sup&gt;o&lt;/sup&gt; C. Prior to use in experiments, all &lt;em&gt;Prochlorococcus &lt;/em&gt;cultures were grown in co-culture with &lt;em&gt;Alteromonas &lt;/em&gt;EZ55 helpers (3) and were acclimated to culture conditions for at least 4 generations prior to data collection.&lt;/p&gt; &lt;p&gt;&lt;em&gt;Alteromonas&lt;/em&gt; cultures were grown in YTSS medium (5) and &lt;em&gt;Prochlorococcus&lt;/em&gt; cultures were grown in Pro99 medium (6) or PEv medium (1), both made in an artificial seawater base (ASW) (1). Prior to addition to co-cultures &lt;em&gt;Alteromonas&lt;/em&gt; strains were pelleted at 2000 g for 2 minutes and washed twice in sterile ASW, then added to cultures at approximately 10&lt;sup&gt;6&lt;/sup&gt; cells ml&lt;sup&gt;-1&lt;/sup&gt;. &lt;em&gt;Alteromonas&lt;/em&gt; was grown at 30&lt;sup&gt;o&lt;/sup&gt; C with 120 rpm shaking. Unless otherwise noted, &lt;em&gt;Prochlorococcus &lt;/em&gt;and co-cultures were grown in static 13 mL conical bottom acid-washed glass tubes under approximately 75 mmol photons m&lt;sup&gt;-2&lt;/sup&gt; s&lt;sup&gt;-1&lt;/sup&gt; cool white light in a Percival incubator set to 23&lt;sup&gt;o&lt;/sup&gt; C. When medium additions were employed, all solutions were filter sterilized with a 0.2 mm filter. Cell densities of &lt;em&gt;Prochlorococcus &lt;/em&gt;cultures to standardize inoculations between experiments were determined using a Guava HT1 flow cytometer (Luminex Corporation, Austin, TX) by the distinctive signature of these cells on plots of forward light scatter vs. red fluorescence (Fig. S1A). Day-to-day culture growth was tracked using the &lt;em&gt;in vivo &lt;/em&gt;chlorophyll &lt;em&gt;a&lt;/em&gt; module for the Trilogy fluorometer (Turner Designs, San Jose, CA) with a custom 3D-printed adapter designed for conical bottom tubes. Fluorometer measurements and cell counts were linearly related across the range of cells examined in this study (Pearson correlation coefficient 0.835, p = 1.38 x 10&lt;sup&gt;-6&lt;/sup&gt;, Fig. S1B).&lt;/p&gt; &lt;p&gt;&lt;strong&gt;&lt;em&gt;Concentration of &lt;/em&gt;Alteromonas&lt;em&gt; exudates:&lt;/em&gt;&lt;/strong&gt; EZ55 was grown in Pro99 media supplemented with 0.1% glucose to sustain growth in the absence of &lt;em&gt;Prochlorococcus&lt;/em&gt; exudates. We scaled cultures up progressively from 12 mL to 2 L. The 2L culture was grown in a vented bottle with an outlet connected to a filter with 0.22 μm pore size. After removing most of the cells by centrifugation, we produced size-fractionated, concentrated exudates using tangential flow filtration using Sartorius Vivaflow 200 cassettes. The 2L culture supernatant was passed first through a 0.22 μm cassette using a Masterflex L/S peristaltic pump (Cole-Parmer) to remove bacterial cells, then through a 50 kDa module and a 5 kDa module in succession to produce &amp;gt;50 kDa and &amp;lt;50 kDa fractions that were each concentrated approximately 100-fold. A portion of the &amp;gt;50 kDa fraction was placed in boiling water for 5 minutes to denature proteins. When these concentrated extracellular products were added to culture media for growth experiments they were diluted 100-fold, returning them to approximately their original concentration prior to filtration.&lt;/p&gt; &lt;p&gt;&lt;strong&gt;&lt;em&gt;Enzyme activities of exudates&lt;/em&gt;:&lt;/strong&gt; We used a variety of enzymatic tests to evaluate the activity of &lt;em&gt;Alteromonas &lt;/em&gt;exudates. We used the fluorescent conjugates 4-nitrophenyl-α-D-glucopyranoside, 4-nitrophenyl-β-D-glucopyranoside, and 4-nitrophenyl-N-acetyl-β-D-glucopyranoside to measure the activities of the glycolytic enzymes α-glucosidase, β-glucosidase and N-acetyl-glucosaminidase, respectively (7). Phosphatase activity was measured by following the hydrolysis of fluorescent substrate 4-methylumbelliferyl phosphate (8). Enzyme activity for these experiments was expressed as the rate of fluorescent product accumulation over the first 2-5 hours, minus the rate of accumulation in an exudate-free media control. Protease activity was measured after a 30 minute incubation based on Sigma’s non-specific protease activity assay using casein as a substrate (9). Siderophore activity was determined after a 30 minute incubation using chrome azurol S (10). Both fluorescence and optical density traces for these assays were measured using a Biotek Synergy H1 plate reader (Agilent, Santa Clara, CA). Hydroperoxidase activity was assessed by measuring the elimination of a hydrogen peroxide spike after 2 hours, tracking the hydrogen peroxide concentration using acridinium ester chemiluminescence via the injection protocol described previously (2) but modified for use with the Synergy H1. We also attempted to determine the role, if any, of intact EVs in enzyme function by sonicating a subsample of the &amp;gt;50 kDa fraction prior to assays. To accomplish this, the concentrates were treated with a Fisher Scientific sonic dismembrator for 3 cycles of 10 s with 10 s pause between (100W, 30% output efficiency). Both methylumbelliferyl and 4-nitrophenyl conjugate substrates are routinely used to measure membrane permeability due to their inability to cross membranes (11, 12), so an increase in apparent enzymatic activity post-sonication can be interpreted as an indication of membrane disruption.&lt;/p&gt; Funding provided by NSF Division of Ocean Sciences (NSF OCE) Award Number: OCE-2304066 Award URL: https://www.nsf.gov/awardsearch/show-award?AWD_ID=2304066 Funding provided by NSF Division of Ocean Sciences (NSF OCE) Award Number: OCE-2304067 Award URL: https://www.nsf.gov/awardsearch/show-award?AWD_ID=2304067 onGoing Steven Biller Wellesley College 781-283-3294 Department of Biological Sciences 106 Central St. Wellesley MA 02481 USA sbiller@wellesley.edu pointOfContact James Jeffrey Morris University of Alabama at Birmingham 205-934-9498 1300 University Blvd CH253 Birmingham AL 35294 USA evolve@uab.edu pointOfContact Zhiying Lu University of Alabama at Birmingham 1-252-773-2353 Campbell Hall, Office 474 1300 University Blvd Birmingham AL 35233 USA luzy@uab.edu pointOfContact asNeeded Dataset Version: 1 Unknown Strain Enzyme Treatment Value Percival Guava HT1 Biotek Synergy H1 Masterflex peristaltic pump (Cole-Parmer) theme None, User defined strain identifier enzyme_assay treatment number featureType BCO-DMO Standard Parameters Algal Growth Chamber Flow Cytometer plate reader Pump Turner Designs Trilogy fluorometer instrument BCO-DMO Standard Instruments otherRestrictions otherRestrictions Access Constraints: none. Use Constraints: Please follow guidelines at: http://www.bco-dmo.org/terms-use Distribution liability: Under no circumstances shall BCO-DMO be liable for any direct, incidental, special, consequential, indirect, or punitive damages that result from the use of, or the inability to use, the materials in this data submission. If you are dissatisfied with any materials in this data submission your sole and exclusive remedy is to discontinue use. Collaborative Research: Extracellular vesicles as vehicles for microbial interactions in marine Black Queen communities https://osprey.bco-dmo.org/project/893375 Collaborative Research: Extracellular vesicles as vehicles for microbial interactions in marine Black Queen communities <p><em>NSF Award Abstract:</em><br /> The function and stability of microbial communities in the ocean depends on exchanges of biological products and services between individual cells. Marine microbes are typically far apart from one another, so some of these exchanges occur through the release of products or services into the surrounding water, where they travel to other cells via simple diffusion. Understanding the degree to which such valuable products made by one organism are targeted to a specific partner, and how, has important implications for our understanding of the ecology and evolution of the marine microbiome. This project examines the role played by a poorly understood type of very small particle - extracellular membrane vesicles - in mediating functional interactions within the oceans. Extracellular vesicles are released by most marine microbes and are abundant in ocean waters, but our understanding of their functions remains in its infancy. As vesicles can contain diverse molecules, including active enzymes, and transport them between cells, they may work as a packaging and delivery system for goods and services traded between ecologically important microorganisms. Broader impacts of the project include providing hands-on research experiences for undergraduate and graduate students - including those from groups historically underrepresented in STEM fields - and the development of new active learning exercises to help increase knowledge about the roles microbes play in students' lives.</p> <p>This project explores vesicle functions across multiple scales, combining -omics analyses, field experiments, and functional studies in cultures of diverse and ecologically important microbes to arrive at new understandings of vesicle contributions to cellular exchanges. These experiments incorporate an evolutionary perspective for exploring the range of vesicle functions and genetic mechanisms affecting their production, examining how their contents have changed in co-cultures of phytoplankton and heterotrophic bacteria following hundreds of generations of experimental laboratory evolution. Fundamental ecological questions are addressed concerning whether vesicles, and their associated functions, act as truly 'public goods' in the oceans or can instead be targeted to a subset of cells, possibly yielding 'club goods' that define interacting, cooperative networks. Collectively, this effort will generate new insights into the mechanisms marine microbes use to interact with one another, and experimentally define the functional potential and ecological impact of EV-mediated trafficking networks in the oceans.</p> <p>This project is jointly funded by the Biological Oceanography Program and the Established Program to Stimulate Competitive Research (EPSCoR). This award reflects NSF's statutory mission and has been deemed worthy of support through evaluation using the Foundation's intellectual merit and broader impacts review criteria.</p> Vesicle Interactions largerWorkCitation project eng; USA oceans 2026-04-20 Laboratory cultures 0 BCO-DMO catalogue of parameters from Enzyme activity of Alteromonas macleodii exudates Biological and Chemical Oceanography Data Management Office (BCO-DMO) Unavailable 508-289-2009 WHOI MS#36 Woods Hole MA 02543 USA info@bco-dmo.org http://www.bco-dmo.org Monday - Friday 8:00am - 5:00pm For questions regarding this resource, please contact BCO-DMO via the email address provided. pointOfContact http://lod.bco-dmo.org/id/dataset-parameter/997092.rdf Name: Strain Units: unitless Description: <p>The Prochlorococcus/Alteromonas co-culture from which the Alteromonas strain was isolated. LTPE26 was an ancestral culture; LTPE397 was evolved for 500 generations at 400 ppm pCO2 before culture isolation; and LTPE403 was evolved for 500 generations at 800 ppm pCO2 before isolation. &quot;Blank&quot; indicates the value of the negative controls for each assay.</p> http://lod.bco-dmo.org/id/dataset-parameter/997093.rdf Name: Enzyme Units: unitless Description: <p>Indicates which of the enzymatic assay each data point corresponds to. AP, alkaline phosphatase; H2O2, hydroperoxidase/catalase; Protease, Sigma protease assay; Siderophore, siderophore chrome azurol S assay; AG, alpha-glucosidase; NAG, N-acetylglucosaminidase; BG, beta-glucosidase.</p> http://lod.bco-dmo.org/id/dataset-parameter/997094.rdf Name: Treatment Units: unitless Description: <p>E, &gt;50 KDa fraction containing Enzymes; F, 5-50 kDa filtered fraction; S, Sonicated &gt;50 KDa fraction; M, Media control</p> http://lod.bco-dmo.org/id/dataset-parameter/997095.rdf Name: Value Units: nm Description: <p>The measured value for each assay. The exact type of data measured differs for the different assays: AP: Fluorescence at 449 nm (excitation at 359 nm), H2O2: Proportion of initial H2O2 remaining, Protease: Optical density at 660 nm, Siderophore: Optical density at 630 nm, AG/NAG/BG: Optical density at 405 nm</p> GB/NERC/BODC > British Oceanographic Data Centre, Natural Environment Research Council, United Kingdom Biological and Chemical Oceanography Data Management Office (BCO-DMO) Unavailable 508-289-2009 WHOI MS#36 Woods Hole MA 02543 USA info@bco-dmo.org http://www.bco-dmo.org Monday - Friday 8:00am - 5:00pm For questions regarding this resource, please contact BCO-DMO via the email address provided. pointOfContact https://osprey.bco-dmo.org/dataset/997078/data/download download onLine dataset &lt;p&gt;&lt;em&gt;&lt;strong&gt;Strains and culture conditions:&amp;nbsp;&lt;/strong&gt; &lt;/em&gt;All strains used in this study were taken from those used for a Long-Term Phytoplankton Evolution (LTPE) experiment (1). &lt;em&gt;Prochlorococcus&lt;/em&gt; strains were streptomycin-resistant derivates of the high light-adapted strain MIT9312 obtained as described previously (2, 3), either before (Ancestor) or after 500 generations of evolution at either 400 ppm or 800 ppm pCO&lt;sub&gt;2&lt;/sub&gt; conditions (i.e., modern day or projected year 2100 conditions (4)). &lt;em&gt;Alteromonas&lt;/em&gt; strains were derivatives of strain EZ55, originally isolated from a &lt;em&gt;Prochlorococcus&lt;/em&gt; MIT9215 culture (3). As with our &lt;em&gt;Prochlorococcus&lt;/em&gt; strains, we used both ancestral and evolved varieties of EZ55 co-evolved with &lt;em&gt;Prochlorococcus &lt;/em&gt;at the two pCO&lt;sub&gt;2&lt;/sub&gt; treatments and subsequently isolated. &lt;em&gt;Prochlorococcus&lt;/em&gt; cultures were revived from cultures cryopreserved with 7.5% DMSO in liquid nitrogen vapor, and &lt;em&gt;Alteromonas &lt;/em&gt;cultures were revived from cultures preserved with 20% glycerol stored at -80&lt;sup&gt;o&lt;/sup&gt; C. Prior to use in experiments, all &lt;em&gt;Prochlorococcus &lt;/em&gt;cultures were grown in co-culture with &lt;em&gt;Alteromonas &lt;/em&gt;EZ55 helpers (3) and were acclimated to culture conditions for at least 4 generations prior to data collection.&lt;/p&gt; &lt;p&gt;&lt;em&gt;Alteromonas&lt;/em&gt; cultures were grown in YTSS medium (5) and &lt;em&gt;Prochlorococcus&lt;/em&gt; cultures were grown in Pro99 medium (6) or PEv medium (1), both made in an artificial seawater base (ASW) (1). Prior to addition to co-cultures &lt;em&gt;Alteromonas&lt;/em&gt; strains were pelleted at 2000 g for 2 minutes and washed twice in sterile ASW, then added to cultures at approximately 10&lt;sup&gt;6&lt;/sup&gt; cells ml&lt;sup&gt;-1&lt;/sup&gt;. &lt;em&gt;Alteromonas&lt;/em&gt; was grown at 30&lt;sup&gt;o&lt;/sup&gt; C with 120 rpm shaking. Unless otherwise noted, &lt;em&gt;Prochlorococcus &lt;/em&gt;and co-cultures were grown in static 13 mL conical bottom acid-washed glass tubes under approximately 75 mmol photons m&lt;sup&gt;-2&lt;/sup&gt; s&lt;sup&gt;-1&lt;/sup&gt; cool white light in a Percival incubator set to 23&lt;sup&gt;o&lt;/sup&gt; C. When medium additions were employed, all solutions were filter sterilized with a 0.2 mm filter. Cell densities of &lt;em&gt;Prochlorococcus &lt;/em&gt;cultures to standardize inoculations between experiments were determined using a Guava HT1 flow cytometer (Luminex Corporation, Austin, TX) by the distinctive signature of these cells on plots of forward light scatter vs. red fluorescence (Fig. S1A). Day-to-day culture growth was tracked using the &lt;em&gt;in vivo &lt;/em&gt;chlorophyll &lt;em&gt;a&lt;/em&gt; module for the Trilogy fluorometer (Turner Designs, San Jose, CA) with a custom 3D-printed adapter designed for conical bottom tubes. Fluorometer measurements and cell counts were linearly related across the range of cells examined in this study (Pearson correlation coefficient 0.835, p = 1.38 x 10&lt;sup&gt;-6&lt;/sup&gt;, Fig. S1B).&lt;/p&gt; &lt;p&gt;&lt;strong&gt;&lt;em&gt;Concentration of &lt;/em&gt;Alteromonas&lt;em&gt; exudates:&lt;/em&gt;&lt;/strong&gt; EZ55 was grown in Pro99 media supplemented with 0.1% glucose to sustain growth in the absence of &lt;em&gt;Prochlorococcus&lt;/em&gt; exudates. We scaled cultures up progressively from 12 mL to 2 L. The 2L culture was grown in a vented bottle with an outlet connected to a filter with 0.22 μm pore size. After removing most of the cells by centrifugation, we produced size-fractionated, concentrated exudates using tangential flow filtration using Sartorius Vivaflow 200 cassettes. The 2L culture supernatant was passed first through a 0.22 μm cassette using a Masterflex L/S peristaltic pump (Cole-Parmer) to remove bacterial cells, then through a 50 kDa module and a 5 kDa module in succession to produce &amp;gt;50 kDa and &amp;lt;50 kDa fractions that were each concentrated approximately 100-fold. A portion of the &amp;gt;50 kDa fraction was placed in boiling water for 5 minutes to denature proteins. When these concentrated extracellular products were added to culture media for growth experiments they were diluted 100-fold, returning them to approximately their original concentration prior to filtration.&lt;/p&gt; &lt;p&gt;&lt;strong&gt;&lt;em&gt;Enzyme activities of exudates&lt;/em&gt;:&lt;/strong&gt; We used a variety of enzymatic tests to evaluate the activity of &lt;em&gt;Alteromonas &lt;/em&gt;exudates. We used the fluorescent conjugates 4-nitrophenyl-α-D-glucopyranoside, 4-nitrophenyl-β-D-glucopyranoside, and 4-nitrophenyl-N-acetyl-β-D-glucopyranoside to measure the activities of the glycolytic enzymes α-glucosidase, β-glucosidase and N-acetyl-glucosaminidase, respectively (7). Phosphatase activity was measured by following the hydrolysis of fluorescent substrate 4-methylumbelliferyl phosphate (8). Enzyme activity for these experiments was expressed as the rate of fluorescent product accumulation over the first 2-5 hours, minus the rate of accumulation in an exudate-free media control. Protease activity was measured after a 30 minute incubation based on Sigma’s non-specific protease activity assay using casein as a substrate (9). Siderophore activity was determined after a 30 minute incubation using chrome azurol S (10). Both fluorescence and optical density traces for these assays were measured using a Biotek Synergy H1 plate reader (Agilent, Santa Clara, CA). Hydroperoxidase activity was assessed by measuring the elimination of a hydrogen peroxide spike after 2 hours, tracking the hydrogen peroxide concentration using acridinium ester chemiluminescence via the injection protocol described previously (2) but modified for use with the Synergy H1. We also attempted to determine the role, if any, of intact EVs in enzyme function by sonicating a subsample of the &amp;gt;50 kDa fraction prior to assays. To accomplish this, the concentrates were treated with a Fisher Scientific sonic dismembrator for 3 cycles of 10 s with 10 s pause between (100W, 30% output efficiency). Both methylumbelliferyl and 4-nitrophenyl conjugate substrates are routinely used to measure membrane permeability due to their inability to cross membranes (11, 12), so an increase in apparent enzymatic activity post-sonication can be interpreted as an indication of membrane disruption.&lt;/p&gt; Specified by the Principal Investigator(s) &lt;p&gt;ll statistical analyses were performed in R v. 4.4.1. Most analyses used linear models followed by post hoc extended marginal means testing of pairwise differences between treatment groups using the &lt;em&gt;emmeans&lt;/em&gt; package (1). Assumptions of linear regression were checked for models by Shapiro-Wilk tests of the normality of residuals and plots of residuals vs. fitted values for homoscedasticity; where these assumptions were violated we used the Box-Cox procedure to find an optimal power transformation (2). Statistical differences between lysate and exudate protein localization counts were determined using Fisher’s exact test implemented in R.&lt;/p&gt; Specified by the Principal Investigator(s) asNeeded 7.x-1.1 Biological and Chemical Oceanography Data Management Office (BCO-DMO) Unavailable 508-289-2009 WHOI MS#36 Woods Hole MA 02543 USA info@bco-dmo.org http://www.bco-dmo.org Monday - Friday 8:00am - 5:00pm For questions regarding this resource, please contact BCO-DMO via the email address provided. pointOfContact Percival Percival PI Supplied Instrument Name: Percival Instrument Name: Algal Growth Chamber Instrument Short Name: Instrument Description: A chamber specifically designed for the growth of algae in flasks. The chamber typically provides controlled temperature, humidity, and light conditions. Guava HT1 Guava HT1 PI Supplied Instrument Name: Guava HT1 Instrument Name: Flow Cytometer Instrument Short Name:Flow Cytometer Instrument Description: Flow cytometers (FC or FCM) are automated instruments that quantitate properties of single cells, one cell at a time. They can measure cell size, cell granularity, the amounts of cell components such as total DNA, newly synthesized DNA, gene expression as the amount messenger RNA for a particular gene, amounts of specific surface receptors, amounts of intracellular proteins, or transient signalling events in living cells. (from: http://www.bio.umass.edu/micro/immunology/facs542/facswhat.htm) Community Standard Description: http://vocab.nerc.ac.uk/collection/L05/current/LAB37/ Biotek Synergy H1 Biotek Synergy H1 PI Supplied Instrument Name: Biotek Synergy H1 Instrument Name: plate reader Instrument Short Name: Instrument Description: Plate readers (also known as microplate readers) are laboratory instruments designed to detect biological, chemical or physical events of samples in microtiter plates. They are widely used in research, drug discovery, bioassay validation, quality control and manufacturing processes in the pharmaceutical and biotechnological industry and academic organizations. Sample reactions can be assayed in 6-1536 well format microtiter plates. The most common microplate format used in academic research laboratories or clinical diagnostic laboratories is 96-well (8 by 12 matrix) with a typical reaction volume between 100 and 200 uL per well. Higher density microplates (384- or 1536-well microplates) are typically used for screening applications, when throughput (number of samples per day processed) and assay cost per sample become critical parameters, with a typical assay volume between 5 and 50 µL per well. Common detection modes for microplate assays are absorbance, fluorescence intensity, luminescence, time-resolved fluorescence, and fluorescence polarization. From: http://en.wikipedia.org/wiki/Plate_reader, 2014-09-0-23. Masterflex peristaltic pump (Cole-Parmer) Masterflex peristaltic pump (Cole-Parmer) PI Supplied Instrument Name: Masterflex peristaltic pump (Cole-Parmer) Instrument Name: Pump Instrument Short Name: Instrument Description: A pump is a device that moves fluids (liquids or gases), or sometimes slurries, by mechanical action. Pumps can be classified into three major groups according to the method they use to move the fluid: direct lift, displacement, and gravity pumps PI Supplied Instrument Name: Instrument Name: Turner Designs Trilogy fluorometer Instrument Short Name:Turner Trilogy Instrument Description: The Trilogy Laboratory Fluorometer is a compact laboratory instrument for making fluorescence, absorbance, and turbidity measurements using the appropriate snap-in application module. Fluorescence modules are available for discrete sample measurements of various fluorescent materials including chlorophyll (in vivo and extracted), rhodamine, fluorescein, cyanobacteria pigments, ammonium, CDOM, optical brighteners, and other fluorescent compounds.