CNN and isomaltitol were produced by Hayashibara Co. Ltd (Okayama, Japan). D-(+)-mannose, D-(+)-glucosamine, hydrochloride theophylline, ammonium chloride (NH4Cl), and L-DOPA (3-(3,4-dihydroxyphenyl)-L-alanine were purchased from Wako Pure Chemical Industries, Ltd. (Osaka, Japan). LY294002 was obtained from Calbiochem (Darmstadt, Germany). α-melanocyte-stimulating hormone (α-MSH) was purchased from Sigma Aldrich (St. Louis, MO). Kojic acid (5-hydroxy -2-(hydroxymethyl)-4H-pyran-4-one) was purchased from Tokyo Chemical Industry Co., Ltd. (Tokyo, Japan). Rabbit anti-tyrosinase, rabbit anti-TRP1, rabbit anti-TRP-2, and rat anti-LAMP-1 antibodies were purchased from Santa Cruz (Dallas, Texas). Rabbit anti-Pmel17(gp100) antibody was purchased from Abcam (Cambridge, UK). Mouse anti-Pmel17(HMB45) antibody and horseradish peroxidase (HRP)-conjugated secondary antibodies were purchased from Dako (Glostrup, Denmark). Mouse anti-MITF antibody was purchased from Exalpha Biologicals (Shirley, MA). Mouse anti-actin antibody was purchased from EMD Millipore (Temecula, CA). Alexa Fluor 594- and Alexa Fluor 488-conjugated secondary antibodies were purchased from Life Technologies (Carlsbad, CA). Leupeptin and pepstatin were obtained from Peptide Institute, Inc. (Osaka, Japan). Complete EDTA-free Protease Inhibitor Cocktail was purchased from Roche Diagnostics (Basel, Switzerland).
D mannose
Manufactured by Fujifilm
Sourced in Japan
D-mannose is a type of sugar that is found naturally in various plants and fruits. It is used as a laboratory reagent for various applications, such as in the analysis and detection of carbohydrates and glycoproteins.
Automatically generated - may contain errors
Lab products found in correlation
D glucose, by Fujifilm (5 mentions)
D galactose, by Fujifilm (5 mentions)
D fructose, by Fujifilm (3 mentions)
D xylose, by Fujifilm (3 mentions)
Horseradish peroxidase hrp conjugated secondary antibody, by Agilent Technologies (1 mentions)
Ammonium chloride nh4cl, by Fujifilm (1 mentions)
α melanocyte stimulating hormone α msh, by Merck Group (1 mentions)
Rabbit anti trp1, by Santa Cruz Biotechnology (1 mentions)
Rat anti lamp 1, by Santa Cruz Biotechnology (1 mentions)
Leupeptin, by Peptide Institute (1 mentions)
Pepstatin, by Peptide Institute (1 mentions)
Complete edta free protease inhibitor cocktail, by Roche (1 mentions)
Mouse anti actin antibody, by Merck Group (1 mentions)
Alexa fluor 488 conjugated secondary antibody, by Thermo Fisher Scientific (1 mentions)
Sodium chloride (nacl), by Fujifilm (1 mentions)
D ribose, by Fujifilm (1 mentions)
Sodium carbonate, by Fujifilm (1 mentions)
Disodium hydrogen phosphate, by Fujifilm (1 mentions)
Sodium hydrogen carbonate, by Fujifilm (1 mentions)
Hydrogen peroxide, by Fujifilm (1 mentions)
8 protocols using d mannose
1
Melanogenesis Regulation Pathway Analysis
2
Synthesis and Characterization of Cyclodextrin Derivatives
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FPB-βCyD, PB-βCyD, and 1 were synthesised according to our previous reports.5–7 (link) Dimethyl sulfoxide (DMSO, Luminasol®, Dojindo Laboratories), sodium chloride (Fujifilm Wako Chemicals), disodium hydrogen phosphate (Fujifilm Wako Chemicals), sodium hydrogen carbonate (Fujifilm Wako Chemicals), sodium carbonate (Fujifilm Wako Chemicals), d -fructose (Fujifilm Wako Chemicals), d -glucose (Fujifilm Wako Chemicals), d -galactose (Fujifilm Wako Chemicals), d -mannose (Fujifilm Wako Chemicals), d -ribose (Fujifilm Wako Chemicals), d -xylose (Fujifilm Wako Chemicals), hydrogen chloride aq. (Fujifilm Wako Chemicals), 50% sodium hydroxide solution (super special grade, Fujifilm Wako Chemicals), and Milli-Q water were used for spectroscopic measurements.
3
Catalytic valorization of biomass-derived compounds
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d (+)‐glucose (98 %, Kishida), d (−)‐fructose (99 %, Wako), d (+)‐mannose (99 %, Wako), d (+)‐xylose (99 %, Wako), dl ‐glycelaldehyde (>90 %, Sigma‐Aldrich), glycolic acid (97 %, Wako), formic acid (98 %, Wako), hydrogen peroxide (30 %, Wako), and benzoic acid (99.5 %, Wako) were used for the reactions and the analysis. Calcium oxide (CaO, 99.9 %, Wako), hydroxide (Ca(OH)2, 90 %, Kishida), carbonate (CaCO3, 99.95 %, Wako), and phosphate (Ca3(PO4)2, 98 %, Wako) were used as catalysts. Other metal oxides, MgO (99.9 %, Wako), SrO (95 %, Kishida), BaO (90 %, Wako), Sc2O3 (99.9 %, Kojundo), Y2O3 (99.99 %, Wako), La2O3 (99.99 %, Wako), CeO2 (99.9 %, Wako), TiO2 (anatase, 98.5 %, Wako), Nb2O5 (99.9 %, Kojundo), Ta2O5 (99.9 %, Wako), Cr2O3 (Wako), SnO2 (98 %, Wako) and ZnO (99.9 %, Wako) were also used as catalysts. Mg‐Al hydrotalcite (Mg/Al=3) was prepared by a conventional coprecipitation method[39] using Mg(NO3)2 ⋅ 6H2O (99 %, Wako), Al(NO3)3 ⋅ 9H2O (98 %, Wako), Na2CO3 (99.5 %, Kishida) and NaOH (98 %, Kishida).
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4
Quantifying Biomass Content via Acid Hydrolysis
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The neutral sugar content was
determined using the two-stage sulfuric acid hydrolysis method28 with slight modifications.29 (link) For neutral sugar analysis, approximately 0.25 g of each
dried sample was dissolved in 1 mL of 72% sulfuric acid for 1 h in
a 30 °C water bath. Each mixture was quantitatively diluted by
adding 28 mL of distilled water (final sulfuric acid concentration,
4%), and each solution was incubated for 1 h at 121 °C. The resulting
hydrolysate was filtered through a 0.2 μm high-performance liquid
chromatography (HPLC)-certified filter (GE Healthcare, Little Chalfont,
UK). The neutral sugars obtained via acid hydrolysis were analyzed
by HPLC (Prominence, Shimadzu Corporation, Kyoto, Japan) on SP0810
columns (Showa Denko K. K., Kanagawa, Japan), with a charged aerosol
detector (Corona Veo RS; Thermo Fisher Scientific, Waltham, MA, USA).
Neutral sugars were eluted with acetonitrile/water 13.0/87.0 (v/v)
at a flow rate of 0.5 mL min–1. Analytical gradel -arabinose, d -galactose, d -glucose, d -mannose (Wako Pure Chemical Industries, Ltd., Osaka, Japan), and d -xylose (Tokyo Chemical Industry Co., Ltd., Tokyo, Japan) were
used as standards to quantify the neutral sugars. Since a coal sample
does not contain neutral sugar and only a biomass sample contains
neutral sugar, the content of biomass in the mixture can be estimated
from the following equation.
determined using the two-stage sulfuric acid hydrolysis method28 with slight modifications.29 (link) For neutral sugar analysis, approximately 0.25 g of each
dried sample was dissolved in 1 mL of 72% sulfuric acid for 1 h in
a 30 °C water bath. Each mixture was quantitatively diluted by
adding 28 mL of distilled water (final sulfuric acid concentration,
4%), and each solution was incubated for 1 h at 121 °C. The resulting
hydrolysate was filtered through a 0.2 μm high-performance liquid
chromatography (HPLC)-certified filter (GE Healthcare, Little Chalfont,
UK). The neutral sugars obtained via acid hydrolysis were analyzed
by HPLC (Prominence, Shimadzu Corporation, Kyoto, Japan) on SP0810
columns (Showa Denko K. K., Kanagawa, Japan), with a charged aerosol
detector (Corona Veo RS; Thermo Fisher Scientific, Waltham, MA, USA).
Neutral sugars were eluted with acetonitrile/water 13.0/87.0 (v/v)
at a flow rate of 0.5 mL min–1. Analytical grade
used as standards to quantify the neutral sugars. Since a coal sample
does not contain neutral sugar and only a biomass sample contains
neutral sugar, the content of biomass in the mixture can be estimated
from the following equation.
5
Electrochemical Glucose Sensing in Human Serum
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A gold disk, Pt wire, and Ag|AgCl|saturated KCl electrodes were purchased from Bioanalytical Systems Inc. (West Lafayette, IN, USA). D-glucose, D-galactose, D-mannose, D-fructose, ascorbic acid, and dialysis membrane (size 36) were obtained from FUJIFILM Wako Pure Chemical Co. (Osaka, Japan). Human serum was purchased from Sigma-Aldrich (St. Louis, MO, USA). All reagents were of the best available grade and were used as received with no further purification. All solutions were prepared with purified water (Millipore, 18 MΩ cm−1).
6
Enzymatic Characterization of Sucrose Phosphorylase
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d -Allose, d -glucose, α-Glc1P, d -gluconic acid, lactose, d -mannose, and d -xylose were purchased from Fujifilm Wako Pure Chemical (Osaka, Japan); N-acetyl-d -glucosamine, d -galactose, and sucrose were purchased from Nacalai Tesque (Kyoto, Japan); d -glucosamine was purchased from Tokyo Chemical Industry (Tokyo, Japan); cellobiose, d -galacturonic acid, and d -glucuronic acid were purchased from Sigma (St. Louis, MO, USA). β-(1 → 4)-Mannobiose was prepared as previously described29 (link). Lactoless L3 (β-galactosidase) was provided by Daiwa Kasei (Shiga, Japan). SP from Bifidobacterium longum was prepared according to the method described by Nishimoto and Kitaoka5 (link). One unit of SP was defined as the amount of enzyme required to phosphorolyze 1 μmol of sucrose in 1 min. SP activity was measured as follows: a reaction mixture (50 μL) containing appropriate concentration of enzyme, 20 mM sucrose, 40 mM sodium phosphate, 100 mM 4-(2-hydroxyethyl)-1-piperazineethanesulfonic acid (HEPES)-NaOH buffer (pH 7.0), and 0.2 mg/mL bovine serum albumin (BSA, Nacalai Tesque) was incubated at 37 °C for 10 min. The enzymatic reaction was terminated by incubating the sample at 80 °C for 3 min, and the liberated d -fructose was measured using a d -Fructose/d -Glucose Assay Kit (Megazyme, Brey, Ireland).
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7
Phagocytosis Inhibition Assay with Carbohydrates
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Phagocytosis inhibition assay was performed by dispensing mouse BMDCs into 24-well plates at a concentration of 2.5 × 105 cells/well and incubating with 1 mg/mL mannan from Saccharomyces cerevisiae (Sigma-Aldrich), 1 mg/mL d (+)-mannose (FUJIFILM Wako Pure Chemical), 1 mg/mL laminarin (Nacalai Tesque, Kyoto, Japan), 1 mg/mL dextran from Leuconostoc spp. (Mr 450000–650000; Sigma-Aldrich), 1 mg/mL d (+)-galactose (FUJIFILM Wako Pure Chemical), 1 mg/mL N-acetyl-d (+)-glucosamine (FUJIFILM Wako Pure Chemical), or PBS at 37°C under an atmosphere of 5% CO2 for 30 min, followed by addition of CFW-labeled rLdpA–chitin complex (rLdpA, 1 μg/mL, chitin, 50 μg/mL). After 4-h incubation, the MFI of rLdpA–chitin complex-phagocytosed cells was measured by flow cytometry (BD FACSVerse; BD Biosciences). Data were analyzed using FlowJo version 10 (BD Biosciences).
8
Sugars Influence Larval Settlement
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Larvae were immersed in millipore-filtered seawater (0.22 µm) containing graded concentrations (10−10, 10−8, 10−6, 10−4 M) of dissolved sugars for 2 h [3 (link)] relative to those recorded in previous studies [3 (link),4 (link),5 (link),6 (link)]. Monosaccharides (D-arabinose, D-fructose, D-galactose, D-glucose, D-mannose, D-xylose, N-acetylglucosamine (GlcNAc), N-acetylneuraminic acid (Sialic acid or Neu5Ac), α-methyl-D-mannoside) and Disaccharides (lactose, maltose, sucrose) were used (Nacalai Tesque, Kyoto, Japan except for D-galactose (Wako Pure Chemical Co., Osaka, Japan)). After 2 h immersion into the sugar solutions, the sugar treated larvae were washed 3 times in 1 L FSW. Ten sugar treated larvae were introduced into 6-well plates coated with CgSE and to 10 mL FSW. The CgSE-coated surfaces were prepared by inoculating the 6-well plates with CgSE at a protein concentration of 50 µg mL−1. Untreated larvae were also released into the well plates containing CgSE-coated surfaces and FSW as the control. The 24 h larval settlement assays were repeated twice using different batches of larvae with three replicates at each trial (n = 6).
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