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Sampleprep

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SamplePrep is a laboratory equipment designed for the preparation of samples prior to analysis. It provides a consistent and reliable method for sample homogenization, extraction, and purification. The core function of SamplePrep is to ensure sample integrity and optimize the performance of analytical instruments.

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Lab products found in correlation

Superase in, by Thermo Fisher Scientific (2 mentions) Rnase 1, by Thermo Fisher Scientific (2 mentions) Nicolet 6700 spectrometer, by Thermo Fisher Scientific (2 mentions) Omnic program, by Thermo Fisher Scientific (2 mentions) Cryomicrotome, by Thermo Fisher Scientific (2 mentions) Nextseq platform, by Illumina (1 mentions) Cryostat, by Leica (1 mentions) 1600 minig, by SPEX (1 mentions) Bovine serum albumin (bsa), by Euromedex (1 mentions) Deuterated water, by Merck Group (1 mentions) Human serum albumin (hsa), by Merck Group (1 mentions) Anti flag agarose resin, by Merck Group (1 mentions) Nupage gel, by Thermo Fisher Scientific (1 mentions) 3xflag peptide, by Merck Group (1 mentions) Anti c myc 9e10, by Santa Cruz Biotechnology (1 mentions) Ultrospec 10 cell density meter, by Cytiva (1 mentions) Miseq platform, by Illumina (1 mentions) Speedvac, by Thermo Fisher Scientific (1 mentions) Flag peptide, by Merck Group (1 mentions) M2 beads, by Merck Group (1 mentions)

Close spelling variants of this product

SamplePrep 6770 (9 citations) SamplePrep 6870 Freezer/Mill (5 citations) SamplePrep 2010 Geno/Grinder (5 citations) SamplePrep 6870 (5 citations) SamplePrep 6770 Freezer/Mill (4 citations) SamplePrep Freezer/Mill (3 citations) SamplePrep 1600 MiniG (2 citations) SamplePrep 8000 (2 citations) SPEX SamplePrep 8000 M Mixer (1 citations)

28 protocols using sampleprep

1

Plant Tissue Sampling for Microbiome Analysis

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Plants were harvested in a single day to avoid batch effects. A 10 cm section of stalk was cut from the plant 20 cm off the ground using sterilized razor blades and gloves. Plants were dug up around the roots, and roots were removed from the center of the root ball and placed into a clean falcon tube for root and rhizosphere samples.
The outer portions of stalks were removed with a sterile razor blade, and the inner tissues (protected from contamination and external microbes) were cut into 1–3 mm pieces and loaded into a 2 mL conical tube for GenoGrinding (SPEX SamplePrep). Root samples were vortexed at the max setting for 15 s in deionized water to separate the rhizosphere from the root. This wash was then centrifuged at 4500× g for 10 min in preparation for DNA extraction. Roots were then thoroughly cleaned with deionized water to remove any residual rhizosphere. Then, 2–3 cm of roots were chopped up with a sterile razor blade and loaded into a 2 mL conical tube for GenoGrinding (SPEX SamplePrep, Metuchen, NJ, USA).
Schultz C.R., Johnson M, & Wallace J.G. (2023). Effects of Inbreeding on Microbial Community Diversity of Zea mays. Microorganisms, 11(4), 879.
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2

Ribosome Profiling and Transcriptome Analysis

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Cultures were grown in 500 ml of rich media in 1 L Erlenmeyer flasks; we added cyclohexamide (100 µg/ml final concentration) 1 min prior to harvesting the cells. We harvested the yeast cells via vacuum filtration, suspended them in 500 μl of lysis buffer, then flash-froze them with N2(l). For each sample, 2/3 of the harvested cells were reserved for Ribo-Seq and 1/3 for RNA-Seq.Cells were lysed using the freezer/mill method (SPEX SamplePrep); after preliminary preparations, lysates were treated with RNaseI (Ambion), and subsequently with SUPERaseIn (Ambion). Digested extracts were loaded in 7–47% sucrose gradients to evaluate the quality of the samples. Monosomal fractions corresponding to digested polysomes were collected; SDS was added to stop any possible RNAse activity, then samples were flash-frozen with N2(l). RNA was isolated from monosomal fractions using the hot acid phenol method. Ribosome-Protected Fragments (RPFs) were selected by isolating RNA fragments of 28-32 nucleotides (nt) using gel electrophoresis. The protocol described in Ingolia et al. 2012 was used to prepare sequencing libraries for both RPFs and fragmented RNA, with minor modifications73 (link). Sequencing was performed on the Illumina NextSeq platform. We performed strand-specific sequencing, which permits the differentiation between the products of sense and antisense overlapping sequences.
Blevins W.R., Ruiz-Orera J., Messeguer X., Blasco-Moreno B., Villanueva-Cañas J.L., Espinar L., Díez J., Carey L.B, & Albà M.M. (2021). Uncovering de novo gene birth in yeast using deep transcriptomics. Nature Communications, 12, 604.
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3

Cryo-sectioning and X-ray Fluorescence Analysis

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Tissues were fixed in F1-buffer, as described above and cryo-sectioned using a Leica cryostat to 10 μm sections. The tissues sections were melted at room temperature onto ultralene film (SPEX SamplePrep, Metuchen NJ) then transferred to sample mounts for XFM. X-ray fluorescence experiments were conducted on the 2-ID-E and 2-ID-D beamlines at the Advanced Photo Source, Argonne National Labs (Argonne, IL). Samples were visualized by light microscopy and tissue regions were selected for element measurement. XFM sample mounting, data collection, and data processing were conducted as described previously21 (link).
Pierson H., Muchenditsi A., Kim B.E., Ralle M., Zachos N., Huster D, & Lutsenko S. (2017). The Function of ATPase Copper Transporter ATP7B in Intestine. Gastroenterology, 154(1), 168-180.e5.
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4

Arabidopsis Seedling Flood Inoculation

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Ten-day-old seedlings were flood-inoculated essentially as in Ishiga et al. (59 (link)). Seedlings were grown in 12-well plates containing 1/2 LS salts and 0.5% (wt/vol) Phytagel solid media. On the day of infection, Pst DC3000 (pVSP61) inoculum was suspended in sterile water with 0.025% (vol/vol) Silwet L-77 (Lehle Seeds) to an OD595nm = 0.01 (∼8.0 × 106 CFU/mL of bacteria) and 3 mL of inoculum was added to each well for 3 min, decanted, and tissue harvested from 5 to 10 seedlings per biological replicate at 1 and 3 DPI. After harvesting, tissue fresh weight was measured, and the samples were surface-sterilized with 5% (vol/vol) H2O2 for 5 min and rinsed three times with sterile water. Tissue was placed in 1.5-mL microfuge tubes and macerated in sterile water for 5 min in a 1600 miniG (Spex SamplePrep) set at 1,000 strokes per minute. Macerated tissue was serially diluted in sterile water and spread onto LB plates containing 25 µM rifampicin. Colonies per plate were counted after incubating at 28 °C for 48 h.
Hilleary R., Paez-Valencia J., Vens C., Toyota M., Palmgren M, & Gilroy S. (2020). Tonoplast-localized Ca2+ pumps regulate Ca2+ signals during pattern-triggered immunity in Arabidopsis thaliana. Proceedings of the National Academy of Sciences of the United States of America, 117(31), 18849-18857.
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5

Purification and Preparation of Myoglobin

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Horse heart Myoglobin (Met-Myoglobin, metMb) was purchased from Sigma-Aldrich (purity ≥ 90%). It was purified before use, following the procedure described below. Deuterated water (Sigma-Aldrich, 99.9% isotopic purity) and glutaraldehyde (TCI, 50% in water w/w) were kept under nitrogen atmosphere to avoid contamination by water vapor after first opening. Polypropylene sheets (4.75 µm  ±  3%, Spex Sample Prep) and steel foil (5 µm) were used for protein hydrogel preparation and irradiation. Bovine serum albumin (Euromedex, > 98%), Human serum albumin (Sigma-Aldrich), and β-lactoglobulin from bovine milk (Sigma-Aldrich, ≥ 90%, mixture of 2 variants) were used after similar purification to that described for myoglobin.
Ludwig N., Galindo C., Witjaksono C., Danvin A., Peaupardin P., Muller D., Kusumoto T., Kodaira S., Barillon R, & Raffy Q. (2024). Radiolysis of myoglobin concentrated gels by protons: specific changes in secondary structure and production of carbon monoxide. Scientific Reports, 14, 8625.
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6

Trace Metal Mapping in Cryosectioned Samples

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A 10 μm cryosection was placed between two pieces of a 4 μm thin ultralene foil (Spex SamplePrep) and mounted on custom-made sample holders. Micro x-ray-fluorescence (μXRF) cartography was performed at the microXAS beamline of the Swiss Light Source (Paul Scherrer Institute). In brief, monochromatic excitation radiation of 9.8 keV (above Zn K-edge) was selected using a double crystal monochromator (DCM) equipped with Si(111) crystals. The primary beam was focused by two orthogonal reflective mirrors ('KB-geometry') down to a spot size of 1 μm × 2 μm (h x v). XRF spectra were collected using Silicon Drift Diode (SDD) detector systems. Chemical images were recorded in ‘on-the-fly’ mode, typically with a pixel size of 8 μm × 8 μm based on the required large field of view. XRF spectra obtained for each individual pixel were deconvoluted using the software PyMCA [29 (link),30 ].
Zimmerer A., Schulze F., Gebhardt S., Huesker K., Stobbe D., Grolimund D., Hesse B., Wassilew G.I, & Schoon J. (2024). Impact of gadolinium-based MRI contrast agent and local anesthetics co-administration on chondrogenic gadolinium uptake and cytotoxicity. Heliyon, 10(8), e29719.
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7

Galvanostatic Cycling of Li-FSI-Ethylcellulose Li/S Battery

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Example 7

FIG. 7 shows the galvanostatic cycling performance of the Li—FSI-ethylcellulose cell in a Li/S battery system at a c-rate of C/20, and at temperature of 70° C. Cells were assembled with lithium foil as anode and the cathode was prepared using 35% of sulphur, 15% of Ketjen black (Ckj-600, AkzoNobel), 15% Li(FSI-ethylcellulose) and 35% of PEO as binder. Sulphur was dry ball milled in an 8000M mixer/mill (© SPEX SamplePrep) for min with carbon black prior to the cathode slurry preparation. The PEO was dissolved in acetonitrile, while the Li(FSI-ethylcellulose) was dissolved in ethanol and was added and the resulting mixture was wet ball milled for 30 min at RT. Initial cycles showed a discharge capacity of approximately 350 mAh/g at a C-rate of C/20. FIG. 8 shows the typical formation of higher and lower order polysulphides during discharge (reduction) followed by the oxidation of lower order polysulphides that takes place in Li/S batteries.

US10892521B2. Solid polymer electrolyte based on modified cellulose and its use in lithium or sodium secondary batteries (2021-01-12). Fundacion Centro de Investigacion Cooperativa de Energias Alternativas CIC Energigune Fundazioa [ES]. Inventors: Hicham Ben Youcef [ES], Michel Armand [ES], Brahim Orayech [ES], Damien Saurel [ES], Devaraj Shanmukaraj [ES], Teofilo Rojo [ES].
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8

Isolation of Rad9-3FLAG Protein Complexes

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For Rad93FLAG IPs cell extracts were prepared from 200 OD yeast cells treated as above for cell cycle arrest and DNA damage. Cells were harvested, washed in ice-cold sorbitol buffer (1 M sorbitol, 25 mM Hepes pH 7.6), and resuspended in a 1:1 ratio with lysis buffer supplemented with protease and phosphatase inhibitors (100 mM Hepes, 200 mM KOAc, 0.1% NP-40, 10% glycerol, 2 mM β-mecaptoethanol, 100 nM okadaic acid, 10 mM NaF, 20 mM β-glycerophosphate, 400 μM PMSF, 4 μM aprotinin, 4 mM benzamidin, 400 μM leupeptin, 300 μM pepstatin A), snap-frozen to liquid nitrogen and lysed using a Spex Sample Prep cryo mill. The extracts were cleared by centrifugation and incubated with anti‐FLAG agarose resin (Sigma) for 1 hour (4 °C, rotation). After five washes with lysis buffer, Rad93FLAG was eluted twice with 0.5 mg/ml 3xFLAG peptide (Sigma). The elutions were pooled and proteins were precipitated with TCA prior to analysis on 4–12% NuPAGE gels (Invitrogen) and standard western blotting.
di Cicco G., Bantele S.C., Reusswig K.U, & Pfander B. (2017). A cell cycle-independent mode of the Rad9-Dpb11 interaction is induced by DNA damage. Scientific Reports, 7, 11650.
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9

Fission Yeast Telomerase Purification

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S. pombe cultures (1.5 l) were collected at 5 × 106 cells ml–1, washed in TMG(300) (10 mM Tris-HCl buffer, pH 8.0, 1 mM magnesium acetate, 10% (v/v) glycerol, 300 mM sodium acetate), resuspended in one packed cell volume TMG(300) plus supplements (5 μg ml–1 chymostatin, 5 μg ml–1 leupeptin, 1 μg ml–1 pepstatin, 1 mM benzamidine, 1 mM DTT, 1 mM EDTA and 0.5 mM phenylmethylsulphonyl fluoride) and quick-frozen by dripping into liquid nitrogen. Cells were lysed in a 6,850 Freezer mill (SPEX SamplePrep) using six cycles (2 min) at a rate of 10 per second with 2 min cooling time between cycles. After thawing on ice, two packed cell volumes of TMG(300) plus supplements were added. All subsequent steps were perfomed at 4 °C. Extracts were cleared by two rounds of centrifugation at 14,000g for 10 min and frozen in liquid nitrogen for storage at –80 °C. Telomerase was enriched on agarose beads coated with anti-c-Myc (9E10, Santa Cruz), and telomerase activity assays contained 10 μl of beads in 10 μl of 50 mM Tris-acetate, pH 8.0, 100 mM potassium acetate, 1 mM magnesium acetate, 5% (v/v) glycerol, 1 mM spermidine, 1 mM DTT, 0.2 mM dATP, dCTP and dTTP, 2 μM [α-32P]dGTP (500 Ci mmol–1) and 5 μM primer (PBoli14, 5′- TGTGGTGTGTGGGTGTG -3′). Reactions were incubated at 30 °C for 90 min and reaction products analysed on a 10% polyacryl amide gel.
Kannan R., Helston R.M., Dannebaum R.O, & Baumann P. (2015). Diverse mechanisms for spliceosome-mediated 3′ end processing of telomerase RNA. Nature Communications, 6, 6104.
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10

FTIR Spectroscopy of Lyophilized Samples

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Lyophilized samples were mixed with KBr at a 1:50 mass ratio, ground by mortar and pestle to homogenize, and pressed into 13-mm-diameter pellets (Spex SamplePrep) for mid-range FTIR spectroscopy (Nicolet 6700 spectrometer, Thermo). Transmission FTIR spectra were collected over the region of 400–4000 cm−1 using a CO2-free purge gas generator and a deuterated triglycine sulfate (DTGS) detector with 32 interferograms averaged for each spectrum. Data collection and spectral processing, including background subtraction and baseline correction, were performed using the OMNIC program (Thermo Nicolet, Co.).
Wang D., Root R.A, & Chorover J. (2021). Biochar-templated surface precipitation and inner-sphere complexation effectively removes arsenic from acid mine drainage. Environmental Science and Pollution Research International, 28(33), 45519-45533.
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