Savant spd1010 speedvac concentrator

Manufactured by Thermo Fisher Scientific

Sourced in United States

The Savant SPD1010 SpeedVac Concentrator is a laboratory equipment designed to concentrate liquid samples by removing solvents through evaporation. It features a compact design and can accommodate a variety of sample vessels.

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Lab products found in correlation

Zorbax bonus rp column, by Agilent Technologies (2 mentions) Agilent 1100 series micro fc g1364d micro fraction collector, by Agilent Technologies (2 mentions) Agilent 1200 series hplc system, by Agilent Technologies (2 mentions) Vortex genie 2, by Avantor (2 mentions) Ultraflextreme instrument, by Bruker (2 mentions) Trypsin, by Promega (1 mentions) 1100 hplc, by Agilent Technologies (1 mentions) Acetonitrile, by Merck Group (1 mentions) Trifluoroacetic acid, by Merck Group (1 mentions) C17 ceramide d18 1 17 0, by Avanti Polar Lipids (1 mentions) Tmt 10 plex reagent, by Thermo Fisher Scientific (1 mentions) Instantblue, by Abcam (1 mentions) Pierce c18 spin column, by Thermo Fisher Scientific (1 mentions) Sonifier slpe cell disruptor, by Emerson (1 mentions) 10 k centrifugal filter device, by Merck Group (1 mentions) Viia 7 real time pcr system, by Thermo Fisher Scientific (1 mentions) Faststart universal sybr green master, by Roche (1 mentions) Veriti thermal cycler, by Thermo Fisher Scientific (1 mentions) Steponeplus real time pcr system, by Thermo Fisher Scientific (1 mentions) Human agilent s mirna microarray system, by Agilent Technologies (1 mentions)

Close spelling variants of this product

Savant SPD1010 SpeedVac SPD1010 SpeedVac Concentrator Savant SpeedVac Concentrator Savant SPD1010 SpeedVac SPD1010 Savant SpeedVac SpeedVac concentrator SPD1010 SpeedVac

25 protocols using savant spd1010 speedvac concentrator

Protein Purification and Digestion Protocol

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The concentrated
sample was redissolved in water. The resuspension was precipitated
with a methanol/chloroform extraction. The precipitate was resuspended
in 31 μL of a solution of 8 M urea, 0.4 M Tris-HCl, and 20 mM
calcium chloride; 3 μL of 45 mM dithiothreitol (DTT) was added
to the solution, and the sample was incubated at 60 °C for 10
min. The reaction was placed on ice for 30 s and then incubated at
room temperature for 3 min; 3 μL of 100 mM iodoacetamide was
added, and the reaction was incubated at room temperature in the dark
for 30 min. The reaction was quenched with 0.67 μL of DTT; 16
μL of 1 M Tris-HCl pH 8.0 was added. Trypsin (Promega) was added
at a ratio of 1:50 Trypsin/protein. Water was added to bring the urea
concentration to 1 M. The digest was incubated at 37 °C overnight.
The following day, the reaction was brought to 1% trifluoroacetic
acid (TFA). The peptides were desalted using Nest Group MicroSpin
columns (C18, 300 Å) and eluted in 80% acetonitrile/0.1% TFA.
The elution was concentrated on a Savant SPD1010 SpeedVac concentrator
(Thermo Scientific).

D’Lima N.G., Khitun A., Rosenbloom A.D., Yuan P., Gassaway B.M., Barber K.W., Rinehart J, & Slavoff S.A. (2017). Comparative Proteomics Enables Identification of Nonannotated Cold Shock Proteins in E. coli. Journal of Proteome Research, 16(10), 3722-3731.

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Quantification of Glucosamine in Dog Serum

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The working standards of glucosamine were added to blank dog serum (100 μL) in microcentrifuge tubes to achieve the desired final concentration previously described along with 40 μL of internal standard, caffeine (diluted to a concentration of 0.1 μg/mL from stock solution). One milliliter of cold acetonitrile (−20 °C) was added to the samples to precipitate proteins. The samples were vortexed and centrifuged at 20,160× g for 5 min. The supernatant was transferred to new microcentrifuge tubes and evaporated to dryness using a Savant SPD1010 SpeedVac Concentrator (Thermo Fisher Scientific, Inc., Asheville, NC, USA). The residues were reconstituted with 50 μL of starting mobile phase (0.05% aqueous formic acid), vortexed for 30 seconds and centrifuged at 20,160× g for 5 min. The supernatants were transferred to 30 kDa centrifugal filter tubes and centrifuged for 30 min at 9000× g. The filtrate was transferred to HPLC vials and 5 μL were injected into the LC-MS/MS system.

Martinez S.E., Lillico R., Lakowski T.M., Martinez S.A, & Davies N.M. (2017). Pharmacokinetic Analysis of an Oral Multicomponent Joint Dietary Supplement (Phycox®) in Dogs. Pharmaceutics, 9(3), 30.

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Peptide Fractionation via ERLIC-LC-MS/MS

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Peptides were fractionated
prior to LC–MS/MS via electrostatic repulsion–hydrophilic
interaction chromatography (ERLIC).^{22 (link)} Desalted
samples were redissolved in 50 μL of 85% acetonitrile/0.1% formic
acid and loaded on a polyWAX LP column (150 × 1.0 mm; 5 μm
300 Å; PolyLC) attached to an Agilent 1100 HPLC at a 0.05 mL/min
flow rate. The samples were separated over an 80 min gradient as follows
(solvent A: 80% acetonitrile, 0.1% formic acid; solvent B: 30% acetonitrile,
0.1% formic acid). Isocratic flow was maintained at 100% A at a flow
rate of 0.3 mL/min for 5 min, followed by a 17 min linear gradient
to 8% B and a 25 min linear gradient to 45% B. Finally, a 10 min gradient
to 100% B was followed by a 5 min hold at 100% B before a 10 min linear
gradient back to 100% A, followed by an 8 min hold at 100% A. Fractions
were collected every several minutes, resulting in 15–17 samples
for further LC–MS/MS analysis. Each fraction was vacuum-dried
using a Savant SPD1010 SpeedVac concentrator (Thermo Scientific).

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Plasma and Cell Metabolite Analysis

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Blood samples were centrifuged for 10 min at 2000× g and the plasma and cell fractions collected and stored at −80 °C. For LC-MS/MS analysis, 10 μg/mL of the internal standard, creatine-d_3, dissolved in citrate buffer (0.13 g citrate/mL distilled water, pH 4.3), was added to 100 μL of plasma from each sample. Then, 1 mL of cold acetonitrile (with 0.3% Formic acid, pH 3) was added to each sample to precipitate protein. The samples were vortexed for 2 min and centrifuged at 15,000× g for 5 min. The supernatant was transferred to new tubes and evaporated to dryness using a Savant SPD1010 SpeedVac Concentrator (Thermo Fisher Scientific, Inc., Asheville, NC, USA) at 45°. The cell fraction from the collected blood was thawed and the lysed cells were then processed as described above for plasma samples.

Alraddadi E.A., Lillico R., Vennerstrom J.L., Lakowski T.M, & Miller D.W. (2018). Absolute Oral Bioavailability of Creatine Monohydrate in Rats: Debunking a Myth. Pharmaceutics, 10(1), 31.

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Copper Accumulation Assay in Bacterial Cells

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To determine the copper accumulation in cells, all nine strains used in the in vivo complementation assays were grown in LB media as described above. When cells reached an OD₆₀₀ = 0.8–0.9, cells were given 1 mM IPTG and 0.5 mM CuSO₄, and growth was continued at 37°C. Cell aliquots were collected before induction as 0 hr samples, and then aliquots were collected at 3 and 6 hrs after addition of IPTG and CuSO₄. All cultures were normalized to a final OD₆₀₀ of 0.8 and centrifuged to obtain cell pellets. The cell pellets were washed three times with sterile 1X PBS containing 1 mM EDTA to remove excess extracellular copper. Washed pellets were dried at 75°C for 2 hr in Savant SPD1010 SpeedVac Concentrator (Thermo Scientific). To each pellet, 1 mL of 70% trace metals nitric acid was added and cells were mineralized at 80°C for 2 hr. Samples were then diluted to a final nitric acid concentration of 4% with nano-pure water. Samples were analyzed in a graphite furnace iCE3400 atomic absorption spectrometer (Thermo Scientific). A standard calibration curve was generated using 0 to 40 ppb Cu, with final R² ≥ 0.99. The concentration of copper for each strain was determined as an average of four replicates. Statistical significance of the data was determined using t-test analysis.

Affandi T., Issaian A.V, & McEvoy M.M. (2016). The Structure of the Periplasmic Sensor Domain of the Histidine Kinase CusS Shows Unusual Metal Ion Coordination at the Dimeric Interface. Biochemistry, 55(37), 5296-5306.

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Peptide Sample Preparation for LC-MS

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All fractionation centrifugations were performed at 1100 g for 2 min at RT. The samples were resuspended in 150 µl of 1% (v/v) trifluoroacetic acid (TFA; Sigma-Aldrich)/H₂O and 90% of the sample volume was transferred to a stage tip containing polystyrene-divinylbenzene copolymer modified with sulphonic acid (SDB-RPS, Supelco) and centrifuged at 3000 g for 3 min. Columns were desalted by washing with 0.2% TFA (60 µl) before elution into separate tubes, with the sequential addition of three buffers (Table S2). The samples were evaporated to dryness in a Savant SPD1010 SpeedVac Concentrator (Thermo Fisher Scientific) at 45°C. Prior to separation and analysis by Q Exactive LC-MS, the dried fractionation samples were resuspended in 2% acetonitrile (Sigma-Aldrich), 0.5% TFA in H₂O (LC-MS grade) by gentle agitation and sonication, to give a final concentration of ∼1 µg/µl. A stage tip filter was prepared containing three layers of PVDF Durapore filter (0.1 µm; Millipore). The samples (12 µl) were transferred to stage tips and centrifuged into LC-MS vials at 4000 g for 5 min at RT.

Yahiya S., Saunders C.N., Hassan S., Straschil U., Fischer O.J., Rueda-Zubiaurre A., Haase S., Vizcay-Barrena G., Famodimu M.T., Jordan S., Delves M.J., Tate E.W., Barnard A., Fuchter M.J, & Baum J. (2023). A novel class of sulphonamides potently block malaria transmission by targeting a Plasmodium vacuole membrane protein. Disease Models & Mechanisms, 16(2), dmm049950.

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Purification of Crude Peptides using C-18 Columns

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Sometimes the synthesis can yield products of up to 90% purity, but if it is necessary to have a product with higher purity, the crude peptides are fractionated using preparative Clean-Up^® CEC18153 C-18 extraction columns (UCT, Bristol, PA, USA). Columns were washed twice with 2 mL of methanol and twice with 2 mL of milliQ water. 5–7 mg of the crude peptide was dissolved in milliQ water and loaded onto the column, then the flow-through was collected and reloaded thrice. Elution of the peptide was carried out by adding 0.9–1 mL of successive solutions of water/acetonitrile with concentrations between 0% and 60% (%v/v), collecting each eluent fraction. Finally, the column was washed twice with 1 mL of acetonitrile and twice with 1 mL of methanol, and the eluent was collected. Acetonitrile was evaporated using a Savant SPD 1010 SpeedVac Concentrator (Thermo Fisher Scientific, Asheville, NC, USA) and the aqueous remnant was frozen at −80 °C to be lyophilized. Fractions were evaluated by HPLC and ESI-MS, to determine the main fraction containing the expected peptide.

Guzmán F., Gauna A., Roman T., Luna O., Álvarez C., Pareja-Barrueto C., Mercado L., Albericio F, & Cárdenas C. (2021). Tea Bags for Fmoc Solid-Phase Peptide Synthesis: An Example of Circular Economy. Molecules, 26(16), 5035.

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Bacterial Culture Filtrate Preparation

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Bacterial strains are listed in Table 1. Pseudomonas fluorescens and Pantoea ananatis strains were inoculated into either 60 ml or 5 ml of Pseudomonas Minimal Salts Medium (PMS) [6 ] in a 125-ml Wheaton bottle or 20-ml test tube, respectively. The cultures were grown at 28 °C with shaking for either seven (60-ml cultures) or two days (5-ml cultures). Subsequently, cells were removed from the filtrate by centrifugation (3000 x g for 15 min) and filter sterilized (Millipore GP express Steritop, 0.22-μm pore size (EMD Millipore, Billerica, MA, USA) or 25-mm Pall Acrodisc with 0.22-μm pore size Supor membrane (Pall Corporation, Port Washington, NY, USA), respectively). The dilution series was prepared by concentrating the culture filtrate in a Savant SPD1010 SpeedVac Concentrator (Thermo Scientific, Waltham, MA, USA) without heat (2X), or by diluting (0.3X, 0.1X, 0.03X, 0.01X) culture filtrate with PMS media. As a positive control, a sample enriched in FVG was prepared by extraction with 90% ethanol as described in [9 ].

Okrent R.A., Trippe K.M., Manning V.A, & Walsh C.M. (2018). Detection of 4-formylaminooxyvinylglycine in culture filtrates of Pseudomonas fluorescens WH6 and Pantoea ananatis BRT175 by laser ablation electrospray ionization-mass spectrometry. PLoS ONE, 13(7), e0200481.

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High-pH Reversed-Phase Fractionation Protocol

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Eluted samples were evaporated in a SAVANT SPD1010 SpeedVac Concentrator (Thermo Fisher Scientific, USA), and resuspended in 0.1% formic acid (v/v) to a concentration of 1 μg/μL for high-pH reversed-phase fractionation following a previous workflow^{15 (link)}, with minor adaptations: 30 μL sample were loaded to a ZORBAX Bonus-RP column (with 3.5 µm C18 resins, ID 2.1 mm, length 50 mm; Agilent Technologies, USA), and fractionated with an Agilent 1200 series HPLC System (Agilent Technologies, Germany). A 60 min gradient consisting of 5–35% buffer B (v/v) in 1–42 min, and 35–50% buffer B in 42–45 min at a flow rate of 100 μL/min was used for the fractionation. Here, 10 mM ammonium formate was used as buffer A, and 10 mM ammonium formate with 90% acetonitrile (v/v) was used as buffer B. Ammonium hydroxide was used to adjust the pH of both buffers A and B to 10. Sample fractions were continuously collected into 96 well plates by an Agilent 1100 Series Micro-FC G1364D micro fraction collector (Agilent Technologies, Germany). For each sample, 48 fractions were collected into different wells at 1 min intervals over the first 48 min. The samples were then pooled by combining four fractions at an interval of 12 wells, resulting in 12 fractionated samples per individual microbiome (Fig. 1a).

Li L., Wang T., Ning Z., Zhang X., Butcher J., Serrana J.M., Simopoulos C.M., Mayne J., Stintzi A., Mack D.R., Liu Y.Y, & Figeys D. (2023). Revealing proteome-level functional redundancy in the human gut microbiome using ultra-deep metaproteomics. Nature Communications, 14, 3428.

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HPLC Quantification of Drug in Serum and Lymph

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To a 100 μL serum or lymph sample (except 0 h), 10 μM of the internal standard (duanorubicin) was added then vortexed for 30 s (Vortex Genie–2, VWR Scientific, West Chester, PA, USA). One milliliter of cold HPLC grade acetonitrile (pre-stored at −20 °C) was added to the precipitate proteins, vortexed for 2 min (Vortex Genie–2, VWR Scientific, West Chester, PA, USA), and centrifuged at 15,000 rpm for 5 min; the supernatant was transferred to new, labeled 2 mL centrifuge tubes. The samples were evaporated to dryness using a Savant SPD1010 SpeedVac Concentrator (Thermo Fisher Scientific, Inc., Asheville, NC, USA). The residue was reconstituted with 100 μL of mobile phase, vortexed for 1 min, and centrifuged at 15,000 rpm for 5 min; the supernatant was transferred to HPLC vials and 100 μL were injected into the HPLC system.

Alrushaid S., Sayre C.L., Yáñez J.A., Forrest M.L., Senadheera S.N., Burczynski F.J., Löbenberg R, & Davies N.M. (2017). Pharmacokinetic and Toxicodynamic Characterization of a Novel Doxorubicin Derivative. Pharmaceutics, 9(3), 35.

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