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Phenylalanine

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Phenylalanine is a lab equipment product that functions as an essential amino acid. It is a colorless, crystalline solid with a specific chemical structure and properties. The core function of Phenylalanine is to serve as a building block for proteins in biological systems.

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Lab products found in correlation

Pierce bca protein assay kit, by Thermo Fisher Scientific (2 mentions) L methyl 3h methionine, by PerkinElmer (1 mentions) Tri carb 2910tr liquid scintillation analyzer, by PerkinElmer (1 mentions) 14c phenylalanine, by PerkinElmer (1 mentions)

3 protocols using phenylalanine

1

In Vivo Substrate Transport Assays

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In vivo transport assays were performed as previously described [62 (link)]. The radioactive substrates used were L-(14C(U))-phenylalanine, L-(14C(U))-lysine and L-(methyl-3H)-methionine (PerkinElmer, USA) and L-(14C(U))-alanine (Amersham Biosciences, Little Chalfont, Buckinghamshire, UK). Transport was assayed at the following concentrations: 50 μM lysine with and without 100 mM of histidine or ornithine, 500 μM alanine or methionine, and 2.5 mM phenylalanine.
Ruiz S.J., van ’t Klooster J.S., Bianchi F, & Poolman B. (2020). Growth Inhibition by Amino Acids in Saccharomyces cerevisiae. Microorganisms, 9(1), 7.
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2

Measuring Proteasomal Protein Degradation in Jurkat Cells

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The rate of proteasomal protein degradation in Jurkat T-ALL cells was measured using a pulse-chase experiment using tritiated phenylalanine as described (Sha et al., 2018 (link)). Briefly, Jurkat cells (0.5 million/ml) were subjected to a 20-hour pulse of 5 µCi/ml tritiated phenylalanine (Perkin Elmer Cat#NET1122001MC), followed by a chase in medium containing 2 mM nonradioactive phenylalanine for 2 hrs. At time 0 and all subsequent points, an identical volume of media was collected, and samples were centrifuged to pellet cells. Radioactivity in the cell pellet at time 0 was measured. Radioactivity in the supernatant was then measured at each subsequent timepoint after TCA precipitation, which precipitates proteins but not amino acids, so that TCA-soluble radioactivity in the supernatant reflects radiolabeled phenylalanine generated by protein degradation. The percentage of the initial radioactivity released into the medium at each timepoint was calculated relative to radioactivity in the cell pellet at time 0, as described (Sha et al., 2018 (link)). Radioactivity was measured using a Perkin Elmer Tri-Carb 2910TR Liquid Scintillation Analyzer.
Hinze L., Schreek S., Zeug A., Ibrahim N.K., Fehlhaber B., Loxha L., Cinar B., Ponimaskin E., Degar J., McGuckin C., Chiosis G., Eckert C., Cario G., Bornhauser B., Bourquin J.P., Stanulla M, & Gutierrez A. (2022). Supramolecular Assembly of GSK3α as a Cellular Response to Amino Acid Starvation. Molecular cell, 82(15), 2858-2870.e8.
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3

Phenylalanine Incorporation Assay in Myotubes

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Differentiated myotubes were incubated with 425 μmol/l phenylalanine and 0.4 μCi/mL of [ 14 C] phenylalanine (Perkin Elmer, Waltham, MA, US) in DMEM (1 g/l glucose) for 6 h at 37°C and 7.5% CO 2 . The cells were then washed in ice cold PBS and lysed in 0.03% SDS for 1 hour at room temperature. The total amount of protein per well was determined by the Pierce BCA protein assay kit (Thermo Fischer Scientific). Protein from the cell lysates was precipitated in 50% TCA with 1% BSA, overnight at -20°C. The samples were centrifuged at 12000 g for 10 minutes at 4°C. The protein pellet was then washed in acetone, dissolved in 0.5 mol/l NaOH and the amount of [ 14 C] determined by scintillation counting (WinSpectral 1414 Liquid Scintillation Counter; Wallac, Turku, Finland). Counts per minute were normalized to the total amount of protein per well, and the amount of phenylalanine incorporated into protein is presented as pmol/mg/hour.
Lundell L.S., Savikj M., Kostovski E., Iversen P.O., Zierath J.R., Krook A., Chibalin A.V, & Widegren U. (2018). Protein translation, proteolysis and autophagy in human skeletal muscle atrophy after spinal cord injury. Acta physiologica (Oxford, England), 223(3).
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