Spd speedvac

Manufactured by Thermo Fisher Scientific

Sourced in United States

The SPD SpeedVac is a laboratory equipment designed for the rapid evaporation and concentration of liquid samples. It uses a combination of vacuum and controlled heating to efficiently remove solvents from a wide range of sample types.

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Lab products found in correlation

Trypsin, by Merck Group (1 mentions) Urea, by Merck Group (1 mentions) Tris glycine sds, by Bio-Rad (1 mentions) Sinapinic acid, by Merck Group (1 mentions) Spectra multicolor low range protein ladder, by Thermo Fisher Scientific (1 mentions) Temed, by Bio-Rad (1 mentions) Ammonium persulfate, by Bio-Rad (1 mentions) Mini protean tetra vertical electrophoresis system, by Bio-Rad (1 mentions) Powerpac universal, by Bio-Rad (1 mentions)

Spelling variants of this product

SpeedVac (526 citations) Savant SPD 2010 SpeedVac Concentrator (7 citations) Savant SPD 111V SpeedVac Concentrator (7 citations) SpeedVac SPD 300DDA (3 citations) SpeedVac SPD 111V P1 (2 citations) Savant SPD 2010 SpeedVac (2 citations)

5 protocols using spd speedvac

In Situ Tryptic Digestion and MALDI MS

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Hydrogels (1 mm diameter)
were rehydrated for 15 min using 20 μL of 1 μg/mL trypsin
(in 100 mM ammonium bicarbonate) and then placed over the tissue region
of interest (brain thalamic region) onto the whole tissue surface
guided by the histological features on corresponding serial H&E
stained tissue section. The tissue sections were incubated in a microwave
oven (1.65 kW) for 2 min set at 10% of the power, to accelerate protein
digestion. Each hydrogel disc was removed from the tissue section
and placed in separate eppendorf tubes. Peptides imbibed into the
microwell hydrogels were extracted by organic (50% acetonitrile/5%
formic acid) and aqueous (100 mM ammonium bicarbonate) solvents, a
process that was repeated three times. The supernatants collected
from each extraction were combined and dried in a centrifugal vacuum
concentrator (SPD Speedvac, Thermo Scientific, Waltham, MA, USA).
The reconstituted extracts (20 μL, 0.1% formic acid) were spotted
for matrix assisted laser desorption/ionization mass spectrometry
(MALDI MS) analysis, mixed with CHCA, 10 mg/mL in 50% acetonitrile,
0.5% TFA, and then stored at −20 °C until LC-MS/MS analysis
was performed.

Taverna D., Norris J.L, & Caprioli R.M. (2014). Histology-Directed Microwave Assisted Enzymatic Protein Digestion for MALDI MS Analysis of Mammalian Tissue. Analytical Chemistry, 87(1), 670-676.

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Thymidine Derivatization and Analysis

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Six μL of CAX-B solution (CAX-B at 1 mg/mL and Et₃N at 10 μL/mL in 50% ACN) was added to a vial containing 160 amol of evaporated thymidine, and the vial was kept for 16 h at 38°C. The solution was dried in a SPD Spee d Vac (Thermo Scientific), redissolved in 5 μL of 0.1% TFA in 2% ACN, and injected into a Micro-HPLC system (Agilent 1100, Dionex PepMap 100 C18 column, 1 × 250 mm, 5 μm). Flow rate: 50 μL/minute. Mobile phase: 12% ACN with 0.1% TFA for 4 min, then 12-90% ACN in 40 min. The eluted sample was collected in the 8 to 17 min time-window. The dried sample was re-injected into a nano-LC (Eksigent Tempo LC MALDI System (AB SCIEX), Dionex PepMap 100 C18 column, 0.075 × 150 mm, 3 μm) at 300 nL/min with an immediate gradient of 12 to 90% ACN with 0.1% TFA in 50 min with collection of 3 droplets/min onto a MALDI plate with online matrix addition (CCA matrix: 2.5 mg/mL, 0.5 mL/min syringe pump flow), followed by MALDI-TOF/TOF-MS.

Wang P., Zhang Q., Yao Y, & Giese R.W. (2015). Cationic Xylene Tag for Increasing Sensitivity in Mass Spectrometry. Journal of the American Society for Mass Spectrometry, 26(10), 1713-1721.

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MALDI-TOF MS Protein Profiling

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Urea, NaNC, dithiothreitol, acetonitrile, 3-[(3-cholamidopropyl) dimethylammonio)-1-propanesulfonate, trifluoroacetic acid, sinapinic acid and trypsin were purchased from Sigma (St. Louis, MO, USA). Spectra Multicolor Low Range Protein Ladder and SPD SpeedVac were purchased from Thermo Fisher Scientific (Waltham, MA, USA). PBSII SELDI-TOF MS and the WCX2 protein chip were purchased from Ciphergen Biosystems Inc. (Fremont, CA, USA). Ammonium persulfate, 2X/4X Laemmli Sample Buffer, 10X Tris/Glycine/SDS, TEMED, Powerpac Universal and Mini-PROTEAN Tetra vertical electrophoresis system were purchased from Bio-Rad (Berkeley, CA, USA). Matrix-assisted laser desorption ionization/time-of-flight mass spectrometry (MALDI-TOF MS) was purchased from Kratos Analytica Inc. (Spring Valley, NY, USA). Uhraflex III MALDI-TOF/TOF MS were purchased from Bruker Corp. (Bremen, Germany).

Yan Z., Meng Q., Yang J., Zhang J., Zhao W., Guo F., Song D., Zhan Y., Fan D., Zhou R., Zuo S., Wang Z., Yu J., Zheng S, & Wang J. (2016). Identification of proteins associated with pediatric bilateral Wilms tumor. Oncology Letters, 12(6), 5075-5079.

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Amino Acid Analysis via Acid Hydrolysis

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All samples were subjected to acid hydrolysis prior to amino acid analysis. For that, 5 mg of dry substance was mixed with 2 mL of 6 M hydrochloric acid in screw-cap tubes and incubated in a drying chamber at 110 °C for 23 h. An aliquot of 300 µL of the hydrolysates was dried afterwards in a vacuum centrifuge (SPD Speed Vac; Thermo Fischer Scientific, Karlsruhe, Germany). The dry residues were dissolved in 600 µL of loading buffer (0.12 N lithium citrate, pH 2.20), membrane filtered (0.45 µm) and subjected to amino acid analysis. Quantification of amino acids was performed with the amino acid analyzer S 433 (Sykam, Fürstenfeldbruck, Germany). The injection volume was between 10 and 100 µL, and a PEEK column filled with the cation exchange resin LCA K07/Li (150 mm × 4.6 mm, 7 µM) was used for separation according to a custom gradient program. Loading and running buffers were purchased from Sykam. Post-column derivatization with ninhydrin was applied, followed by VIS detection with an integrated two-channel photometer at 440 and 570 nm. External calibration was performed with commercial amino acid standards (Sigma-Aldrich, Steinheim, Germany).

Sajapin J, & Hellwig M. (2020). Studies on the synthesis and stability of α-ketoacyl peptides. Amino Acids, 52(10), 1425-1438.

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Rhodamine-PE Reconstitution and Concentration

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(1,2-dimyristoyl-sn-glycero-3phosphoethanolamine-N-(lissamine rhodamine B sulfonyl), Avanti Polar Lipids, 810157) in 100% chloroform is evaporated with a SpeedVac (SPD SpeedVac, rotor RH64-11, ThermoScientific) for 15 min at room temperature. The pellet of RhodaminePE is suspended in 20 mM HEPES-Na pH 7.5, 100 mM NaCl, 0.035% DDM, to a final concentration of 500 mM. This solution is then diluted to 5 mM of RhodaminePE to a buffer containing Ovalbumin (Ovalbumin 1 mM is solubilized in 20 mM HEPES-Na pH7.5, 100 mM NaCl, 0.035% DDM) and concentrated at 20 C as described below. 15 ml of solution were concentrated.

Gobet A., Zampieri V., Magnard S., Pebay-Peyroula E., Falson P, & Chaptal V. (2023). The non-Newtonian behavior of detergents during concentration is increased by macromolecules, in trans, and results in their over-concentration. Biochimie, 205.

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