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Alpha 1 4 ld

Manufactured by Martin Christ
Sourced in Germany

The Alpha 1-4 LD is a laboratory freeze dryer manufactured by Martin Christ. It is designed to efficiently dehydrate samples through the process of lyophilization. The core function of this equipment is to remove water from frozen samples under vacuum conditions, preserving the structure and composition of the original material.

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9 protocols using alpha 1 4 ld

1

Chromatin Characterization by FTIR and Fluorescence

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The IS-RDV3 temperature controlled shaker (crystal, USA) was used in EtBr removal assays. Freeze centrifuge (Sigma, Germany) was used in all centrifugation steps. Chromatin was dried in Alpha 1-4 LD plus freeze dryer (Christ, Germany). The concentration of EtBr was converted by Cary-60 UV-Spectrometer (Agilent Technology, USA). Chromatin before and after treatment with EtBr were characterized by FTIR spectroscopy (Spectrum Two, PerkinElmer). The fluorescence observations of csDNA, chromatin and magnetic beads were carried out with DM4B fluorescence microscope (Leica, Germany).
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2

Blueberry Pomace Production and Characterization

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In this work, fresh blueberries were treated with a juicer (mechanical force) to mimic the processing of crushing, pressing, and filtration of industrial juice production. After treatment, the juice was filtered, and the remaining blueberry pomace from the juicer was collected as pomace samples. The resultant blueberry pomace was freeze-dried using an Alpha 1-4 LD lyophiliser (Martin Christ, Osterode, Germany) at –50 °C for about 48 h. The freeze-dried powder was milled into particles smaller than 0.180 mm (No. 80 mesh), sealed, and stored at 4 °C.
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3

Protein Extraction from N. benthamiana Leaves

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Agroinfiltrated N. benthamiana leaves were harvested at various days post-infiltration (dpi), frozen at −80 °C, lyophilized using a freeze dryer system (Alpha 1–4 LD; Martin Christ GmbH, Osterode, Germany), and pulverized using a mixer. Small-scale protein extraction was performed to evaluate the protein expression and accumulation. Total soluble protein (TSP) was extracted from 25 mg of lyophilized leaf material, homogenized in 500 µL cold protein extraction buffer (100 mM NaCl, 10 mM KCl, 6.5 mM Na2HPO4, 2 mM KH2PO4, pH 7.2) plus complete protease inhibitor cocktail (Roche Diagnostics GmbH, Mannheim, Germany), using a Precellys 24 homogenizer (Bertin Instruments, France), and incubated for 30 min on ice. Clarified extract was obtained via repeated centrifugation at 15000 × g for 15 min at 4°C. Then, protein concentration of the supernatant was measured using the Pierce Coomassie Plus (Bradford) assay kit (Thermo Fisher Scientific) with bovine serum albumin (BSA) (Thermo Fisher Scientific) as the standard.
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4

Freeze-Drying Protocol for Sample Preservation

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This was performed using a small‐scale freeze‐drier (Alpha1‐4 LD plus‐Martin Christ Model‐101541; Germany). Samples slices were placed in airtight ziplock bags and frozen in a deep freezer at −21°C for 72 hr. The ziplock bags were pierced with several holes and placed in the freeze‐drier. The holes allowed good balance of pressure and temperature inside and outside the ziplock bags during drying. Initial drying was carried out at −41°C and 0.11 mbar, while final drying was carried out at −47°C and 0.055 mbar. In total, the freeze‐drying was carried out for a period of 72 hr. The temperature and pressure conditions used are a recommendation by the drier manufacturer.
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5

Morphology of Juvenile Crabs

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The general anatomical structures of the juvenile crab were observed under the stereomicroscope (Olympus, Tokyo, Japan). Scanning electron microscope (SEM) (Hitachi, Tokyo, Japan) was used to obtain micrographs of juvenile crabs. The juvenile crabs’ samples were prepared by the standard process described by Zhu et al. [40 (link)]. The samples for observation were prepared through ethanol gradient dehydration and tert-butyl alcohol replacement. After being frozen for 20 h at −20 °C, the samples were dried for 24 h in the Martin Christ Alpha 1—4LD plus freeze dryer (Martin Christ, Osterode am Harz, Germany) before being sprayed with gold by a Hitachi E-1010 ion sputtering device (Hitachi, Japan). The length of male penis was obtained by the software Image J and converted according to the scale of SEM images.
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6

Synthesis of Shiny Silver Nanoparticles

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The silver nanoparticle solution was centrifuged for 20 min at 10,000 rpm (centrifugation machine, Sigma 3K30). The resulting pellet was washed with distilled water to wash off impurities. The resulting solution was lyophilized (lyophilizer: Christ Alpha 1-4 LD) to get powdered shiny silver nanoparticles.
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7

Liposome Structural Analysis by XRD

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X-ray diffraction patterns of the liposomes were analyzed between 2θ = 4 and 2θ = 60°with a step size 2θ = 0.02°in an X-ray diffraction instrument (Bruker D8 Discover, USA). The samples were freeze-dried before analysis (Freeze dryer Christ Alpha 1-4 LD, Martin Christ, Germany).
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8

Liposome Functional Group Analysis

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To determine the functional groups of liposomes, FTIR analysis were carried out in Attenuated Total Reflectance mode (ATR) between 500 and 4000 cm -1 , using 16 scans at a resolution of 4 cm -1 (Perkin-Elmer 16 PC spectrometer, Boston, USA). Before analysis, an open bean background spectrum of clean crystal was recorded. The samples were freeze-dried before analysis (Freeze dryer Christ Alpha 1-4 LD, Martin Christ, Germany).
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9

Thermal Analysis of Freeze-Dried Samples

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DSC measurements were performed in a PerkinElmer DSC 6000 equipment (Perkin Elmer, USA). About 10 mg of sample were placed in aluminium DSC pans and heated from 20 to 250 °C at a heating rate of 30 °C min -1 under nitrogen atmosphere. Two replicates were performed for each sample. The samples were freeze-dried before analysis (Freeze dryer Christ Alpha 1-4 LD, Martin Christ, Germany).
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