2 2 6 6 tetramethylpiperidine 1 oxyl tempo
2,2,6,6-tetramethylpiperidine-1-oxyl (TEMPO) is a stable nitroxyl radical compound. It is a versatile reagent used in organic synthesis and analysis.
Lab products found in correlation
9 protocols using 2 2 6 6 tetramethylpiperidine 1 oxyl tempo
Synthesis of Functional Magnetic Nanoparticles
Preparation and Quantification of Singlet Oxygen Precursors
Tuning PEG Fusion Temperatures
of a given molecular mass (Mn, g/mol)
were selected for tuning the fusion temperature, namely, PEG600 (Mn 600, fusion at 17–22 °C), PEG1000
(Mn 950–1050, fusion at 37 °C),
PEG4000 (Mn 4000, fusion at 48–55
°C), PEG6000 (Mn 6000, fusion at
58–60 °C), and PEG8000 (Mn 8000, fusion 58–60 °C). The chemicals used for the CNF
preparation, including NaOH, NaClO, and 2,2,6,6-tetramethylpiperidine-1-oxyl
(TEMPO), were all purchased from Sigma-Aldrich.
Raloxifene-loaded Biocomposite Scaffold
Human cells of bone osteosarcoma (Saos-2) with American type ATCC were obtained from Vacsera, Egypt. Sodium pyruvate and McCoy’s 5a Medium supplemented with L-glutamine, penicillin G sodium, amphotericin B, streptomycin sulphate and fetal bovine serum were procured from Thermo Fisher Scientific, USA. Alkaline Phosphatase Assay Kit (Catalog Number, ab83369) was bought from Abcam, Cambridge, UK.
All other reagents were of analytical grade and the utilized water was distilled, deionized water.
Nanofibrillated Cellulose Synthesis and Characterization
Bleached Bagasse Pulp Functionalization
Cellulose Nanofibers from Diverse Pulp Sources
Arabinoxylan Characterization and Oxidation
TEMPO-Oxidized Cellulose Nanofibrils Production
Potato starch (food grade, applied for food market) was provided by Avebe, Veendam, The Netherlands and used, without any prior purification, as biodegradable polymer matrix. Glycerol (95% purity) was provided by Scharlau, Barcelona, Spain and added as a plasticizer.
α-amylase (Aquazym 480L, declared activity 480 KNU-B/g) was kindly provided by Novozymes, Baggsværd, Denmark and used as received to perform the enzymatic hydrolytic study.
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