MEF and HT1080 cells were maintained in our laboratory. These cells were cultured in DMEM medium (8122292, Gibco, Billings, MT, USA) supplemented with 10% fetal bovine serum (SH30406, Hyclone, Logan, UT, USA) and 1% penicillin/streptomycin (SV30010, Hyclone), and placed in a humidified incubator with 5% CO2 at 37 °C. In the case of arginine deprivation, cells were grown in DMEM/F-12 medium without L-arginine, L-leucine, and L-lysine (D9811-15D, US Biological, Salem, MA, USA) supplemented with 10% fetal bovine serum, 1% penicillin/streptomycin as well as 59.05 mg/L L-leucine (61-90-5, Sigma, St. Louis, MO, USA) and 91.25 mg/L L-lysine (657-27-2, Sigma). In the case of the control group with the complete medium, 59.05 mg/L L-leucine, 91.25 mg/L L-lysine, and 147.5 mg/L L-arginine (1119-34-2, Sigma) were added to the DMEM/F-12 medium without L-arginine, L-leucine, and L-lysine.
L lysine
Manufactured by Merck Group
Sourced in United States, Germany, United Kingdom, Israel, China, Macao
L-lysine is an essential amino acid that is commonly used in various lab equipment and applications. It serves as a building block for proteins and plays a crucial role in various biological processes. The core function of L-lysine is to provide the necessary amino acid for protein synthesis and maintenance.
Automatically generated - may contain errors
Lab products found in correlation
L arginine, by Merck Group (68 mentions)
L histidine, by Merck Group (44 mentions)
L phenylalanine, by Merck Group (40 mentions)
L leucine, by Merck Group (38 mentions)
L methionine, by Merck Group (36 mentions)
L tyrosine, by Merck Group (31 mentions)
L threonine, by Merck Group (29 mentions)
L tryptophan, by Merck Group (29 mentions)
L glutamic acid, by Merck Group (29 mentions)
L valine, by Merck Group (28 mentions)
L isoleucine, by Merck Group (28 mentions)
L serine, by Merck Group (27 mentions)
L aspartic acid, by Merck Group (25 mentions)
L proline, by Merck Group (24 mentions)
L alanine, by Merck Group (22 mentions)
L glutamine, by Merck Group (22 mentions)
L cysteine, by Merck Group (19 mentions)
L asparagine, by Merck Group (19 mentions)
Glycine, by Merck Group (18 mentions)
D glucose, by Merck Group (13 mentions)
207 protocols using l lysine
1
Nutrient Deprivation in Cell Culture
2
Poly(ε-caprolactone) Composite with Apatite Whiskers
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The poly(ε-caprolactone) used in this research work was CAPA 6800 (high-molecular-weight linear polyester, Mw: ~80,000 g/mol), purchased from Perstorp (Malmö, Sweden). Apatite whiskers (HAP) obtained as multiphasic calcium phosphate were prepared using a methodology described earlier [9 (link),24 (link),36 (link)]. L-Lysine (crystallized, >98%) was purchased from Sigma-Aldrich (St. Louis, MO, USA). Sodium chloride and 1,4-dioxane were supplied by POCH (Gliwice, Poland). The standards of L-Lysine, hydrochloride, ammonia formate, formic acid, and acetonitrile (HPLC-grade) were purchased from Sigma-Aldrich. All aqueous solutions were prepared using Milli-Q water (Millipore, Bedford, MA, USA).
3
Modulating Pancreatitis in Mice
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Forty male mice weighing 40–60 g were used in this study. They were housed under standard conditions and allowed access to water and a standard diet ad libitum. The animal protocol was approved by the King AbdulAziz University Animal Ethics committee. The animals were divided into four groups with 10 animals in each group. Group I animals served as controls. Animals in groups II–IV were i.p. injected with L-arginine hydrochloride (400 mg/100 g bw, dissolved in saline, pH 7) for 3 days to induce pancreatitis as described by Tani etal [9 (link)]. Group III animals were orally pre-treated with L-lysine (10 mg/kg bw) (Sigma-Aldrich, StLouis, MO), whereas group IV animals were post-treated orally with L-lysine (10 mg/kg bw). After 15 days, the animals were anesthetized with 10 % thiopental. Blood was collected without anticoagulation, and serum was separated by centrifugation at 4000x g for 15 min. The pancreas was excised immediately and homogenized in ice-cold 0.1 M Tris-HCl. The pancreatic homogenate was used to measure oxidative stress markers.
4
Synthetic Complete Medium Preparation
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A total of 1.7 g yeast basic nitrogen source (YNB without amino acids and ammonium sulfate, BD), 5 g ammonium sulfate (VETECTM, Merck), 20 g d -glucose, 0.1 g l -arginine, 0.1 g l -cysteine, 0.1 g l -lysine, 0.1 g l -threonine, 0.05 g l -aspartic acid, 0.05 g l -Isoleucine, 0.05 g l -phenylalanine, 0.05 g l -proline, 0.05 g l -serine, 0.05 g l -tyrosine, 0.05 g l -valine, 0.05 g l- methionine, 0.1 g l -tryptophan, 0.05 g l -histidine, 0.1 g l -uracil, 0.1 g l- leucine, 0.1 g l- adenine were added to 1 L deionized H2O. All amino acids were purchased from Sigma-Aldrich. After autoclaving for 45 min, the SC medium was stored at room temperature. In all, 2% (m/v) glucose was supplemented to the medium before use.
5
Amino Acid Decarboxylase Activity Assay
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Petri dishes containing YPD agar supplemented with 1% (w/v) of the tested amino acid and 0.006% (w/v) bromocresol purple (Sigma-Aldrich) were prepared [15 (link)]. The amino acids analysed, L-ornithine (Panreac), L-lysine (Merck, Darmstadt, Germany), L-leucine (Merck), L-histidine (Panreac), L-phenylalanine (Panreac), L-arginine (Sigma-Aldrich), L-tryptophan (Merck) and S-tyrosine (Merck) were dissolved in water. Each prepared amino acid solution was mixed with the remaining fraction of medium, and pH was adjusted to 6.0. A single colony was spread onto the plates and was incubated at 25 °C for 7–14 days. The basis for the detection of the decarboxylase activity was the same as described for HCDC activity.
6
Renal Proximal Tubule Cell Assay
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Human serum albumin (HSA) was purchased from Bio Verde (Kyoto, Japan). l -Lysine was purchased from Merck (Darmstadt, Germany). d -Glucose was purchased from Wako (Osaka, Japan). QuantiTect Primer Assay (SLC47A1 and GAPDH) was purchased from Qiagen (Venlo, the Netherlands). Power SYBR Green Cell to Cell kit™ was purchased from Life Technologies (Carlsbad, CA, USA). Rabbit antihuman MATE/SLC47A1 polyclonal antibody was purchased from LifeSpan BioSciences (Seattle, WA, USA). Rabbit IgG as an isotype control and Alexa Flour 647™ goat antiRabbit IgG polyclonal antibody were purchased from Invitrogen (Carlsbad, CA, USA). Human renal proximal tubule epithelial cells were purchased from Takara Bio (Otsu, Japan). Renal epithelial cell growth kit and medium were also purchased from Takara Bio. Fetal bovine serum was purchased from Invitrogen. Six- or 96-well plates were purchased from Becton Dickinson (San Jose, CA, USA). Dimethyl sulfoxide was purchased from Sigma (Tokyo, Japan). Cisplatin and carboplatin were purchased from Wako. XTT-kit was purchased from Roche Applied Science (Penzberg, Germany).
7
Arginine and Lysine Metabolism in Cells
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RPMI 1640 medium and fetal calf serum were from Euroclone. RPMI medium without L-Arginine and L-Lysine (cat. n. R1780), L-Lysine, L-Arginine, L-[4,4,5,5-D4]-Lysine and L-[13C615N4]-Arginine were from Merck, Darmstadt, Germany.
Acridine orange, ethidium bromide, Nile red, quercetin, and polyclonal anti-Caprin1 antibody were purchased from Sigma Chemical Co (St. Louis, MO, USA). Stock solution of quercetin was prepared in DMSO. The DMSO concentration in treated cells was less than 0.01% (v/v). Monoclonal anti-actin, anti-tubulin, anti-CTH (F-1), anti-G3BP1 (H-10), anti-cHMGCS (A-6), anti-Annexin I (EH17a), anti-IDI1 (XY-7), anti-TrxR1 (B-2), anti-CD98 (E5), anti-DDX3 (2253C5a) and anti-FASN (A-5) antibodies were purchased from Santa Cruz Biotechnology (Santa Cruz, CA, USA). Peroxidase-conjugated secondary IgG antibodies were from Thermo Scientific Inc. (Hudson, NH). Reagents for enhanced chemiluminescence (ECL) detection were obtained from Advasta. Fluorogenic caspase-3 substrate, acetyl-Asp-Glu-Val-aspaminomethylcoumarin (Ac-DEVD-AMC) was from Alexis Biochemicals (San Diego, CA, USA).
All other chemicals were reagent grade.
Acridine orange, ethidium bromide, Nile red, quercetin, and polyclonal anti-Caprin1 antibody were purchased from Sigma Chemical Co (St. Louis, MO, USA). Stock solution of quercetin was prepared in DMSO. The DMSO concentration in treated cells was less than 0.01% (v/v). Monoclonal anti-actin, anti-tubulin, anti-CTH (F-1), anti-G3BP1 (H-10), anti-cHMGCS (A-6), anti-Annexin I (EH17a), anti-IDI1 (XY-7), anti-TrxR1 (B-2), anti-CD98 (E5), anti-DDX3 (2253C5a) and anti-FASN (A-5) antibodies were purchased from Santa Cruz Biotechnology (Santa Cruz, CA, USA). Peroxidase-conjugated secondary IgG antibodies were from Thermo Scientific Inc. (Hudson, NH). Reagents for enhanced chemiluminescence (ECL) detection were obtained from Advasta. Fluorogenic caspase-3 substrate, acetyl-Asp-Glu-Val-aspaminomethylcoumarin (Ac-DEVD-AMC) was from Alexis Biochemicals (San Diego, CA, USA).
All other chemicals were reagent grade.
8
Amino Acid Quantification by HPLC
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Amino acid standards (L-Aspartic acid, L-Glutamic acid, L-Serine, L-Glycine, L-Histidine, L-Arginine, L-Threonine, L-Alanine, L-Proline, L-Tyrosine, L-Valine, L-Methionine, L-Cysteine L-Isoleucine, L-Leucine, L-Phenylalanine, L-Lysine) procured from Merck chemicals, Germany. HPLC grade, the two eluants A (0.05M Ammonium acetate aqueous buffer) and B (60% acetonitrile) purchased from Water Corporation, uSA.
9
Synthesis of Amine-Functionalized Carbon Nanotubes
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The single-walled CNT, lithium
amide (LiNH2),l -lysine, and DMF were procured
from Aldrich and were used without any further purification. The first
step in the process was the preparation of the ACNT or the amine-functionalized
CNT in DMF for 12 h. The prepared solution of LiNH2/DMF
(1 g/10 g) was added to the CNT/DMF (1 g/20 g) solution at 50 °C
and was stirred constantly for 8–12 h until the homogeneous
solution was obtained. The solution was then filtered and washed several
times with DMF to remove unreacted amide molecules. The sample was
dried in a vacuum oven at 100 °C for 6 h. After drying, the sample
of ACNT was taken for the further characterization and analysis.
amide (LiNH2),
from Aldrich and were used without any further purification. The first
step in the process was the preparation of the ACNT or the amine-functionalized
CNT in DMF for 12 h. The prepared solution of LiNH2/DMF
(1 g/10 g) was added to the CNT/DMF (1 g/20 g) solution at 50 °C
and was stirred constantly for 8–12 h until the homogeneous
solution was obtained. The solution was then filtered and washed several
times with DMF to remove unreacted amide molecules. The sample was
dried in a vacuum oven at 100 °C for 6 h. After drying, the sample
of ACNT was taken for the further characterization and analysis.
10
Comprehensive 2D Gel Electrophoresis Protocol
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N-hydroxy succinimide ester Cy2, Cy3 and Cy5, urea, glycerol, mineral oil, immobiline DryStrip gels (18 cm, pH = 3–10, pH = 4–7 and pH = 6–11) and IPG buffer solutions (pH = 3–10, 4–7 and 6–11) were purchased from GE Healthcare (Piscataway, NJ). Acrylamide, DTT, Tris, glycine and SDS were purchased from Bio-Rad (Hercules, CA, USA). Dimethyl formamide (DMF), CHAPS, L-lysine, ammonium persulfate, iodoacetamide, agarose, bromophenol blue and TFA were purchased from Aldrich (Poole, Dorset, UK). Thiourea, TEMED, acetone, acetonitrile (ACN) and ethanol were purchased from Fluka (Buchs, Switzerland). Trypsin (sequencing grade) was purchased from Promega (Madison, WI). All buffers were prepared with Milli-Q water (Millipore, Belford, MA, USA). Imperial Protein Stain solution was purchased from Thermo Scientific (Rockford, IL, USA).
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