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Human corneal epithelial cell viability after insult with 6 <t>mmol/L</t> <t>NaOH,</t> or 6 mmol/L NaOH followed by RP-220 or scrambled peptide for rescue Plot shows the MTT assay results denoted with average absorbance values at 540 nm after treatment. Error bars indicate standard error of the mean of each group ( n =4). a P
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Images

1) Product Images from "Rescue of human corneal epithelial cells after alkaline insult using renalase derived peptide, RP-220"

Article Title: Rescue of human corneal epithelial cells after alkaline insult using renalase derived peptide, RP-220

Journal: International Journal of Ophthalmology

doi: 10.18240/ijo.2019.11.01

Human corneal epithelial cell viability after insult with 6 mmol/L NaOH, or 6 mmol/L NaOH followed by RP-220 or scrambled peptide for rescue Plot shows the MTT assay results denoted with average absorbance values at 540 nm after treatment. Error bars indicate standard error of the mean of each group ( n =4). a P
Figure Legend Snippet: Human corneal epithelial cell viability after insult with 6 mmol/L NaOH, or 6 mmol/L NaOH followed by RP-220 or scrambled peptide for rescue Plot shows the MTT assay results denoted with average absorbance values at 540 nm after treatment. Error bars indicate standard error of the mean of each group ( n =4). a P

Techniques Used: MTT Assay

2) Product Images from "Rescue of human corneal epithelial cells after alkaline insult using renalase derived peptide, RP-220"

Article Title: Rescue of human corneal epithelial cells after alkaline insult using renalase derived peptide, RP-220

Journal: International Journal of Ophthalmology

doi: 10.18240/ijo.2019.11.01

Human corneal epithelial cell viability after insult with 6 mmol/L NaOH, or 6 mmol/L NaOH followed by RP-220 or scrambled peptide for rescue Plot shows the MTT assay results denoted with average absorbance values at 540 nm after treatment. Error bars indicate standard error of the mean of each group ( n =4). a P
Figure Legend Snippet: Human corneal epithelial cell viability after insult with 6 mmol/L NaOH, or 6 mmol/L NaOH followed by RP-220 or scrambled peptide for rescue Plot shows the MTT assay results denoted with average absorbance values at 540 nm after treatment. Error bars indicate standard error of the mean of each group ( n =4). a P

Techniques Used: MTT Assay

3) Product Images from "Low Temperature Characteristics of Hydrogen Storage Alloy LaMm-Ni4.1Al0.3Mn0.4Co0.45 for Ni-MH Batteries"

Article Title: Low Temperature Characteristics of Hydrogen Storage Alloy LaMm-Ni4.1Al0.3Mn0.4Co0.45 for Ni-MH Batteries

Journal: Materials

doi: 10.3390/ma12244220

Electrochemical capacity of LaMm–Ni 4.1 Al 0.3 Mn 0.4 Co 0.45 alloy at 6M KOH electrolyte and 6M mixed alkali metal hydroxide electrolytes (LiOH/KOH, NaOH/KOH, RbOH/KOH, CsOH/KOH) at decreasing temperatures. Sequence of temperature changes: +20 °C (activation), +40 °C, +30 °C, +20 °C, +10 °C, 0 °C, −10 °C, −20 °C, −30 °C, +20 °C (reference measurement).
Figure Legend Snippet: Electrochemical capacity of LaMm–Ni 4.1 Al 0.3 Mn 0.4 Co 0.45 alloy at 6M KOH electrolyte and 6M mixed alkali metal hydroxide electrolytes (LiOH/KOH, NaOH/KOH, RbOH/KOH, CsOH/KOH) at decreasing temperatures. Sequence of temperature changes: +20 °C (activation), +40 °C, +30 °C, +20 °C, +10 °C, 0 °C, −10 °C, −20 °C, −30 °C, +20 °C (reference measurement).

Techniques Used: Sequencing, Activation Assay

Hydrogen diffusion coefficient in LaMm–Ni 4.1 Al 0.3 Mn 0.4 Co 0.45 alloy as a function of a composition of 1M alkali metal electrolytes (LiOH, NaOH, KOH, RbOH, CsOH), 6M alkali metal electrolytes (NaOH, KOH, RbOH, CsOH) and binary mixed 6M alkali metal hydroxide electrolytes (LiOH/KOH, NaOH/KOH, RbOH/KOH, CsOH/KOH), determined in chronopotentiometric tests. Temperature 20 °C, SOC = 1.
Figure Legend Snippet: Hydrogen diffusion coefficient in LaMm–Ni 4.1 Al 0.3 Mn 0.4 Co 0.45 alloy as a function of a composition of 1M alkali metal electrolytes (LiOH, NaOH, KOH, RbOH, CsOH), 6M alkali metal electrolytes (NaOH, KOH, RbOH, CsOH) and binary mixed 6M alkali metal hydroxide electrolytes (LiOH/KOH, NaOH/KOH, RbOH/KOH, CsOH/KOH), determined in chronopotentiometric tests. Temperature 20 °C, SOC = 1.

Techniques Used: Diffusion-based Assay

4) Product Images from "Corrosion of Hydrogen Storage Metal Alloy LaMm-Ni4.1Al0.3Mn0.4Co0.45 in the Aqueous Solutions of Alkali Metal Hydroxides"

Article Title: Corrosion of Hydrogen Storage Metal Alloy LaMm-Ni4.1Al0.3Mn0.4Co0.45 in the Aqueous Solutions of Alkali Metal Hydroxides

Journal: Materials

doi: 10.3390/ma11122423

SEM images of a surface of LaMm-Ni 4.1 Al 0.3 Mn 0.4 Co 0.45 alloy not subjected to any treatment ( A ), and after electrochemical treatment in 1 M LiOH ( B ), 1 M NaOH ( C ), and 1 M KOH ( D ).
Figure Legend Snippet: SEM images of a surface of LaMm-Ni 4.1 Al 0.3 Mn 0.4 Co 0.45 alloy not subjected to any treatment ( A ), and after electrochemical treatment in 1 M LiOH ( B ), 1 M NaOH ( C ), and 1 M KOH ( D ).

Techniques Used:

SEM images of a surface of LaMm-Ni 4.1 Al 0.3 Mn 0.4 Co 0.45 alloy not subjected to any treatment ( A ), and after electrochemical treatment at 6 M electrolytes: 6 M LiOH/KOH ( B ), 6 M NaOH/KOH ( C ), 6 M KOH ( D ), 6 M RbOH/KOH ( E ), and 6 M CsOH/KOH ( F ).
Figure Legend Snippet: SEM images of a surface of LaMm-Ni 4.1 Al 0.3 Mn 0.4 Co 0.45 alloy not subjected to any treatment ( A ), and after electrochemical treatment at 6 M electrolytes: 6 M LiOH/KOH ( B ), 6 M NaOH/KOH ( C ), 6 M KOH ( D ), 6 M RbOH/KOH ( E ), and 6 M CsOH/KOH ( F ).

Techniques Used:

5) Product Images from "Extension of the ‘Inorganic Gel Casting’ Process to the Manufacturing of Boro-Alumino-Silicate Glass Foams"

Article Title: Extension of the ‘Inorganic Gel Casting’ Process to the Manufacturing of Boro-Alumino-Silicate Glass Foams

Journal: Materials

doi: 10.3390/ma11122545

27 Al ( a ) and 11 B ( b ) Nuclear magnetic resonance (NMR) studies BSG glass in the as received state, after alkali activation (in ‘green’ foams, NaOH/KOH activation) and after firing (in final foams).
Figure Legend Snippet: 27 Al ( a ) and 11 B ( b ) Nuclear magnetic resonance (NMR) studies BSG glass in the as received state, after alkali activation (in ‘green’ foams, NaOH/KOH activation) and after firing (in final foams).

Techniques Used: Nuclear Magnetic Resonance, Activation Assay

29 Si NMR studies of BSG glass: ( a ) comparison of spectra in the as received state, after alkali activation (in ‘green’ foams, NaOH/KOH activation) and after firing (in final foams); ( b ) deconvolution analysis: blue lines, from experimental spectra, overlap with fitted curves, in red.
Figure Legend Snippet: 29 Si NMR studies of BSG glass: ( a ) comparison of spectra in the as received state, after alkali activation (in ‘green’ foams, NaOH/KOH activation) and after firing (in final foams); ( b ) deconvolution analysis: blue lines, from experimental spectra, overlap with fitted curves, in red.

Techniques Used: Nuclear Magnetic Resonance, Activation Assay

Fourier transform infrared (FTIR) analysis of boro-alumino-silicated glass (BSG) in the as received state, after alkali activation (in ‘green’ foams, NaOH/KOH activation) and after firing (in final foams)
Figure Legend Snippet: Fourier transform infrared (FTIR) analysis of boro-alumino-silicated glass (BSG) in the as received state, after alkali activation (in ‘green’ foams, NaOH/KOH activation) and after firing (in final foams)

Techniques Used: Activation Assay

Morphology of foams in the ‘green’ state (before firing): ( a ) NaOH/KOH activation; ( b ) KOH activation.
Figure Legend Snippet: Morphology of foams in the ‘green’ state (before firing): ( a ) NaOH/KOH activation; ( b ) KOH activation.

Techniques Used: Activation Assay

6) Product Images from "Rescue of human corneal epithelial cells after alkaline insult using renalase derived peptide, RP-220"

Article Title: Rescue of human corneal epithelial cells after alkaline insult using renalase derived peptide, RP-220

Journal: International Journal of Ophthalmology

doi: 10.18240/ijo.2019.11.01

Human corneal epithelial cell viability after insult with 6 mmol/L NaOH, or 6 mmol/L NaOH followed by RP-220 or scrambled peptide for rescue Plot shows the MTT assay results denoted with average absorbance values at 540 nm after treatment. Error bars indicate standard error of the mean of each group ( n =4). a P
Figure Legend Snippet: Human corneal epithelial cell viability after insult with 6 mmol/L NaOH, or 6 mmol/L NaOH followed by RP-220 or scrambled peptide for rescue Plot shows the MTT assay results denoted with average absorbance values at 540 nm after treatment. Error bars indicate standard error of the mean of each group ( n =4). a P

Techniques Used: MTT Assay

7) Product Images from "High-affinity Anticalins with aggregation-blocking activity directed against the Alzheimer β-amyloid peptide"

Article Title: High-affinity Anticalins with aggregation-blocking activity directed against the Alzheimer β-amyloid peptide

Journal: Biochemical Journal

doi: 10.1042/BCJ20160114

Effect of Anticalins on Aβ42 fibril formation and neuronal cytotoxicity ( A ) Macromolecular fibril formation was monitored via TEM starting from Aβ42 dissolved at 200 μM (0.9 mg/ml) in 5 mM NaOH. Subsequently, 1 volume of 20 mM Tris/HCl, pH 6.8 was added by vortex-mixing. The solution was then incubated at 4°C for 6 h without agitation, prior to dilution in RPMI-1640 cell culture medium to a final concentration of 10 μM. Aβ42 alone or in combination with equimolar concentrations of wtLcn2 (negative control), MAb 6E10 (positive control) or the Aβ-specific Anticalins S1A4, H1G1 and H1GA were incubated at 37°C for 72 h and then subjected to TEM. ( B , C ) The toxicity of Aβ42 alone or in combination with Anticalins on NGF-β differentiated PC12 cells was analysed in an MTT reduction assay. ( B ) Aβ42 was preincubated at 4°C for 6 h in a mixture of 1 volume 5 mM NaOH and 1 volume 20 mM Tris/HCl, pH 6.8 and then added at a concentration of 10 μM alone or in combination with equimolar concentrations of the Lcn2 variants to the cells. wtLcn2, S1A4 and H1G1 alone (without Aβ42) showed only minor cytotoxicity (see Figure S5C in the supplementary data section). ( C ) Anticalins with promising effects (H1GA not shown) were further analysed for their potential to support cell viability up to stoichiometric ratios in the presence of 10 μM Aβ42 (measured as in B). For each experiment, measurements of replicates were derived from different wells ( n =4–8) of a single 96-well plate from which the median was calculated. Several plates were measured on different days as independent experiments for cell viability ( n ≥ 3) from which the mean was calculated. Error bars represent standard deviations of the means.
Figure Legend Snippet: Effect of Anticalins on Aβ42 fibril formation and neuronal cytotoxicity ( A ) Macromolecular fibril formation was monitored via TEM starting from Aβ42 dissolved at 200 μM (0.9 mg/ml) in 5 mM NaOH. Subsequently, 1 volume of 20 mM Tris/HCl, pH 6.8 was added by vortex-mixing. The solution was then incubated at 4°C for 6 h without agitation, prior to dilution in RPMI-1640 cell culture medium to a final concentration of 10 μM. Aβ42 alone or in combination with equimolar concentrations of wtLcn2 (negative control), MAb 6E10 (positive control) or the Aβ-specific Anticalins S1A4, H1G1 and H1GA were incubated at 37°C for 72 h and then subjected to TEM. ( B , C ) The toxicity of Aβ42 alone or in combination with Anticalins on NGF-β differentiated PC12 cells was analysed in an MTT reduction assay. ( B ) Aβ42 was preincubated at 4°C for 6 h in a mixture of 1 volume 5 mM NaOH and 1 volume 20 mM Tris/HCl, pH 6.8 and then added at a concentration of 10 μM alone or in combination with equimolar concentrations of the Lcn2 variants to the cells. wtLcn2, S1A4 and H1G1 alone (without Aβ42) showed only minor cytotoxicity (see Figure S5C in the supplementary data section). ( C ) Anticalins with promising effects (H1GA not shown) were further analysed for their potential to support cell viability up to stoichiometric ratios in the presence of 10 μM Aβ42 (measured as in B). For each experiment, measurements of replicates were derived from different wells ( n =4–8) of a single 96-well plate from which the median was calculated. Several plates were measured on different days as independent experiments for cell viability ( n ≥ 3) from which the mean was calculated. Error bars represent standard deviations of the means.

Techniques Used: Transmission Electron Microscopy, Incubation, Cell Culture, Concentration Assay, Negative Control, Positive Control, MTT Assay, Derivative Assay

8) Product Images from "Oxygen Reduction Reaction at Penta-Coordinated Co Phthalocyanines"

Article Title: Oxygen Reduction Reaction at Penta-Coordinated Co Phthalocyanines

Journal: Frontiers in Chemistry

doi: 10.3389/fchem.2020.00022

Cyclic voltammetry of (A) 8(2-Et-C 6 H 11 O)CoPc-Py-CNT, (B) CoPc-Py-CNT, (C) 16(F)CoPc-Py-CNT at 25, 50, 75, 100, 150, and 200 mV/s in N 2 saturated NaOH 0.1 M. Linear sweep voltammetry of rotating ring disk electrodes at various rotating speeds (i.e., 200, 400, 800, 1,200, 1600 rpm) of (D) 8(2-Et-C 6 H 11 O)CoPc-Py-CNT, (E) CoPc-Py-CNT, (F) 16(F)CoPc-Py-CNT. Inset: oxidative current produce at the Pt ring electrode during the linear sweep voltammetry at the various rotation speeds. Conditions: potential scan rate of linear sweep experiments was 5 mV/s, Pt ring polarized at 0.6 V during chronoamperometry, O 2 saturated NaOH 0.1 M.
Figure Legend Snippet: Cyclic voltammetry of (A) 8(2-Et-C 6 H 11 O)CoPc-Py-CNT, (B) CoPc-Py-CNT, (C) 16(F)CoPc-Py-CNT at 25, 50, 75, 100, 150, and 200 mV/s in N 2 saturated NaOH 0.1 M. Linear sweep voltammetry of rotating ring disk electrodes at various rotating speeds (i.e., 200, 400, 800, 1,200, 1600 rpm) of (D) 8(2-Et-C 6 H 11 O)CoPc-Py-CNT, (E) CoPc-Py-CNT, (F) 16(F)CoPc-Py-CNT. Inset: oxidative current produce at the Pt ring electrode during the linear sweep voltammetry at the various rotation speeds. Conditions: potential scan rate of linear sweep experiments was 5 mV/s, Pt ring polarized at 0.6 V during chronoamperometry, O 2 saturated NaOH 0.1 M.

Techniques Used:

(A) Koutecky–Levich plots for O 2 reduction for 8(2-Et-C 6 H 11 O)CoPc-Py-CNT (Blue), CoPc-Py-CNT (Black), and 16(F)CoPc-Py-CNT (red). (B) Tafel plots for O 2 reduction for 8(2-Et-C 6 H 11 O)CoPc-Py-CNT (Blue), CoPc-Py-CNT (Black), and 16(F)CoPc-Py-CNT (red). (C) Linear sweep voltammetry comparison between 8(2-Et-C 6 H 11 O)CoPc-Py-CNT (Blue), CoPc-Py-CNT (Black), and 16(F)CoPc-Py-CNT (Red) during ORR at 800 rpm, scan rate 5 mv/s, O 2 saturated NaOH 0.1 M.
Figure Legend Snippet: (A) Koutecky–Levich plots for O 2 reduction for 8(2-Et-C 6 H 11 O)CoPc-Py-CNT (Blue), CoPc-Py-CNT (Black), and 16(F)CoPc-Py-CNT (red). (B) Tafel plots for O 2 reduction for 8(2-Et-C 6 H 11 O)CoPc-Py-CNT (Blue), CoPc-Py-CNT (Black), and 16(F)CoPc-Py-CNT (red). (C) Linear sweep voltammetry comparison between 8(2-Et-C 6 H 11 O)CoPc-Py-CNT (Blue), CoPc-Py-CNT (Black), and 16(F)CoPc-Py-CNT (Red) during ORR at 800 rpm, scan rate 5 mv/s, O 2 saturated NaOH 0.1 M.

Techniques Used:

9) Product Images from "Biostimulant Action of Dissolved Humic Substances From a Conventionally and an Organically Managed Soil on Nitrate Acquisition in Maize Plants"

Article Title: Biostimulant Action of Dissolved Humic Substances From a Conventionally and an Organically Managed Soil on Nitrate Acquisition in Maize Plants

Journal: Frontiers in Plant Science

doi: 10.3389/fpls.2019.01652

E 465 / E 665 ratios of organic farming (OF) and conventional farming (CF) fractions (A) and density of carboxylic groups in dissolved humic substances (DHS) obtained by titration with NaOH 0.1 M (B) . White bar refers to water-extractable humic substances (WEHS); dark gray bars refer to DHS isolated from OF soils; light gray bars refer to DHS isolated from CF soils (data shown are means plus standard deviation). OF1 and CF1 were sampled in November; OF2, OF-P2, CF2, and CF-P2 were sampled in April; OF3, OF-P3, CF3, and CF-P3 were sampled in June. OF1, OF2, OF3 and CF1, CF2, CF3 refer to leachates collected from bare soil columns. OF-P2, OF-P3 and CF-P2, CF-P3 refer to leachates collected from planted soil columns.
Figure Legend Snippet: E 465 / E 665 ratios of organic farming (OF) and conventional farming (CF) fractions (A) and density of carboxylic groups in dissolved humic substances (DHS) obtained by titration with NaOH 0.1 M (B) . White bar refers to water-extractable humic substances (WEHS); dark gray bars refer to DHS isolated from OF soils; light gray bars refer to DHS isolated from CF soils (data shown are means plus standard deviation). OF1 and CF1 were sampled in November; OF2, OF-P2, CF2, and CF-P2 were sampled in April; OF3, OF-P3, CF3, and CF-P3 were sampled in June. OF1, OF2, OF3 and CF1, CF2, CF3 refer to leachates collected from bare soil columns. OF-P2, OF-P3 and CF-P2, CF-P3 refer to leachates collected from planted soil columns.

Techniques Used: Titration, Isolation, Standard Deviation

10) Product Images from "Synthesis, Characterization and the Solvent Effects on Interfacial Phenomena of Jatropha Curcas Oil Based Non-Isocyanate Polyurethane"

Article Title: Synthesis, Characterization and the Solvent Effects on Interfacial Phenomena of Jatropha Curcas Oil Based Non-Isocyanate Polyurethane

Journal: Polymers

doi: 10.3390/polym9050162

Swelling-time diagrams of CJCO and CJCO/CC-AR blends in ( a ) dilute 10% HCl solution; ( b ) 10% NaCl solution; ( c ) 5% NaOH solution.
Figure Legend Snippet: Swelling-time diagrams of CJCO and CJCO/CC-AR blends in ( a ) dilute 10% HCl solution; ( b ) 10% NaCl solution; ( c ) 5% NaOH solution.

Techniques Used:

FESEM images of the CJCO/CC-AR blend (ratio 1:3) based NIPU with IPDA: ( A ) before solvent treatment; ( B ), ( C ), and ( D ) after solvent treatment. Interfacial surface of the NIPU: ( a ) after being treated with MEK; ( b ) after being treated with 10% NaCl; ( c ) after being treated with 5% NaOH; ( d ) the optimum Hartee-Fock structure of the solvation shell of the hydroxide anion [ 1 ].
Figure Legend Snippet: FESEM images of the CJCO/CC-AR blend (ratio 1:3) based NIPU with IPDA: ( A ) before solvent treatment; ( B ), ( C ), and ( D ) after solvent treatment. Interfacial surface of the NIPU: ( a ) after being treated with MEK; ( b ) after being treated with 10% NaCl; ( c ) after being treated with 5% NaOH; ( d ) the optimum Hartee-Fock structure of the solvation shell of the hydroxide anion [ 1 ].

Techniques Used:

11) Product Images from "Isolation and Culture of a Marine Bacterium Degrading the Sulfated Fucans from Marine Brown Algae"

Article Title: Isolation and Culture of a Marine Bacterium Degrading the Sulfated Fucans from Marine Brown Algae

Journal: Marine Biotechnology (New York, N.y.)

doi: 10.1007/s10126-005-5107-0

Purification of the end-products of the hydrolysis of Pelvetia canaliculata fucoidan (FS28) by the SW5 ammonium sulfate fucanase fraction. (A) Fractionation of the hydrolysate (OF fraction) from P. canaliculata fucan on DEAE Sepharose. The OF fraction (250 mg) was chromatographed on DEAE Sepharose CL6B with a 0 to 2 M NaCl gradient, eluted fractions were assayed for total sugars, and carbohydrate-containing fractions (fractions 85 to 100) were collected. (B) Fractions 85 to 100 were pooled and then chromatographed on Biogel P6 using 50 mM NaNO3 as eluent. The four peaks resolved as fractions 1 to 4 were collected. (C) HPAEC elution profiles of peaks 1 to 4 from fractions 85 to 100 on Biogel P6 chromatography. Fractions were desalted on Sephadex G10 and injected at 250 μg/ml on an AS11A anion-exchange column, using a NaOH linear gradient and conductivity detection.
Figure Legend Snippet: Purification of the end-products of the hydrolysis of Pelvetia canaliculata fucoidan (FS28) by the SW5 ammonium sulfate fucanase fraction. (A) Fractionation of the hydrolysate (OF fraction) from P. canaliculata fucan on DEAE Sepharose. The OF fraction (250 mg) was chromatographed on DEAE Sepharose CL6B with a 0 to 2 M NaCl gradient, eluted fractions were assayed for total sugars, and carbohydrate-containing fractions (fractions 85 to 100) were collected. (B) Fractions 85 to 100 were pooled and then chromatographed on Biogel P6 using 50 mM NaNO3 as eluent. The four peaks resolved as fractions 1 to 4 were collected. (C) HPAEC elution profiles of peaks 1 to 4 from fractions 85 to 100 on Biogel P6 chromatography. Fractions were desalted on Sephadex G10 and injected at 250 μg/ml on an AS11A anion-exchange column, using a NaOH linear gradient and conductivity detection.

Techniques Used: Purification, Fractionation, Chromatography, Injection

12) Product Images from "Isolation and Culture of a Marine Bacterium Degrading the Sulfated Fucans from Marine Brown Algae"

Article Title: Isolation and Culture of a Marine Bacterium Degrading the Sulfated Fucans from Marine Brown Algae

Journal: Marine Biotechnology (New York, N.y.)

doi: 10.1007/s10126-005-5107-0

Purification of the end-products of the hydrolysis of Pelvetia canaliculata fucoidan (FS28) by the SW5 ammonium sulfate fucanase fraction. (A) Fractionation of the hydrolysate (OF fraction) from P. canaliculata fucan on DEAE Sepharose. The OF fraction (250 mg) was chromatographed on DEAE Sepharose CL6B with a 0 to 2 M NaCl gradient, eluted fractions were assayed for total sugars, and carbohydrate-containing fractions (fractions 85 to 100) were collected. (B) Fractions 85 to 100 were pooled and then chromatographed on Biogel P6 using 50 mM NaNO3 as eluent. The four peaks resolved as fractions 1 to 4 were collected. (C) HPAEC elution profiles of peaks 1 to 4 from fractions 85 to 100 on Biogel P6 chromatography. Fractions were desalted on Sephadex G10 and injected at 250 μg/ml on an AS11A anion-exchange column, using a NaOH linear gradient and conductivity detection.
Figure Legend Snippet: Purification of the end-products of the hydrolysis of Pelvetia canaliculata fucoidan (FS28) by the SW5 ammonium sulfate fucanase fraction. (A) Fractionation of the hydrolysate (OF fraction) from P. canaliculata fucan on DEAE Sepharose. The OF fraction (250 mg) was chromatographed on DEAE Sepharose CL6B with a 0 to 2 M NaCl gradient, eluted fractions were assayed for total sugars, and carbohydrate-containing fractions (fractions 85 to 100) were collected. (B) Fractions 85 to 100 were pooled and then chromatographed on Biogel P6 using 50 mM NaNO3 as eluent. The four peaks resolved as fractions 1 to 4 were collected. (C) HPAEC elution profiles of peaks 1 to 4 from fractions 85 to 100 on Biogel P6 chromatography. Fractions were desalted on Sephadex G10 and injected at 250 μg/ml on an AS11A anion-exchange column, using a NaOH linear gradient and conductivity detection.

Techniques Used: Purification, Fractionation, Chromatography, Injection

13) Product Images from "Lactosylceramide promotes hypertrophy through ROS generation and activation of ERK1/2 in cardiomyocytes"

Article Title: Lactosylceramide promotes hypertrophy through ROS generation and activation of ERK1/2 in cardiomyocytes

Journal: Glycobiology

doi: 10.1093/glycob/cwu020

LacCer significantly upregulated [ 3 H]-leucine incorporation in H9c2 cells: H9c2 cells were plated (10 5 per well) in 24-well plates and allowed to proliferate in growth medium composed of DMEM supplemented with 10% fetal bovine serum. When cells had reached near confluence, growth medium was replaced with differentiation medium (DMEM containing 2% horse serum) for 48 h to induce differentiation of H9c2 myoblasts into myotubes. Cells were then stimulated for 48 h with a single dose of 100 µM PE and different glycolipids (as shown above, 100 µM each). [ 3 H]-Leucine (5 Ci or 142 Ci/mmol) was included per well. At the end of the incubation period, cells were washed twice in PBS and proteins were subsequently precipitated with ice-cold 10% trichloroacetic acid. After dissolving the precipitates in 0.5 mol/L NaOH, 5 mL scintillation cocktail was added, and radioactivity was measured by liquid scintillation spectroscopy. [ 3 H]-Leucine incorporation experiments were repeated five times with triplicate measurements for each experiment. LacCer upregulated protein synthesis in H9c2 cells significantly. * P
Figure Legend Snippet: LacCer significantly upregulated [ 3 H]-leucine incorporation in H9c2 cells: H9c2 cells were plated (10 5 per well) in 24-well plates and allowed to proliferate in growth medium composed of DMEM supplemented with 10% fetal bovine serum. When cells had reached near confluence, growth medium was replaced with differentiation medium (DMEM containing 2% horse serum) for 48 h to induce differentiation of H9c2 myoblasts into myotubes. Cells were then stimulated for 48 h with a single dose of 100 µM PE and different glycolipids (as shown above, 100 µM each). [ 3 H]-Leucine (5 Ci or 142 Ci/mmol) was included per well. At the end of the incubation period, cells were washed twice in PBS and proteins were subsequently precipitated with ice-cold 10% trichloroacetic acid. After dissolving the precipitates in 0.5 mol/L NaOH, 5 mL scintillation cocktail was added, and radioactivity was measured by liquid scintillation spectroscopy. [ 3 H]-Leucine incorporation experiments were repeated five times with triplicate measurements for each experiment. LacCer upregulated protein synthesis in H9c2 cells significantly. * P

Techniques Used: Incubation, Radioactivity, Spectroscopy

14) Product Images from "Improving Morphological Quality and Uniformity of Hydrothermally Grown ZnO Nanowires by Surface Activation of Catalyst Layer"

Article Title: Improving Morphological Quality and Uniformity of Hydrothermally Grown ZnO Nanowires by Surface Activation of Catalyst Layer

Journal: Nanoscale Research Letters

doi: 10.1186/s11671-017-1838-x

SEM images of resulting grown NWs. SEM images of 1-year-old substrates after activating for 10 min with solutions of a H 2 O 2 :KOH [1:2], b H 2 O 2 :KOH [1:3], c H 2 O 2 :NaOH [1:3], and d without any cleaning
Figure Legend Snippet: SEM images of resulting grown NWs. SEM images of 1-year-old substrates after activating for 10 min with solutions of a H 2 O 2 :KOH [1:2], b H 2 O 2 :KOH [1:3], c H 2 O 2 :NaOH [1:3], and d without any cleaning

Techniques Used:

AFM images of sample surfaces. AFM images of the surface after 10-min activation by different cleaning solutions: a H 2 O 2 :KOH [1:2], b H 2 O 2 :KOH [1:3], c H 2 O 2 :NaOH [1:2]. Images of sample surfaces before cleaning: d uncleaned, 1-year-old gold layer; e uncleaned, 2-month-old gold layer
Figure Legend Snippet: AFM images of sample surfaces. AFM images of the surface after 10-min activation by different cleaning solutions: a H 2 O 2 :KOH [1:2], b H 2 O 2 :KOH [1:3], c H 2 O 2 :NaOH [1:2]. Images of sample surfaces before cleaning: d uncleaned, 1-year-old gold layer; e uncleaned, 2-month-old gold layer

Techniques Used: Activation Assay

15) Product Images from "In vitro model to study the effects of matrix stiffening on Ca2+ handling and myofilament function in isolated adult rat cardiomyocytes"

Article Title: In vitro model to study the effects of matrix stiffening on Ca2+ handling and myofilament function in isolated adult rat cardiomyocytes

Journal: The Journal of Physiology

doi: 10.1113/JP274460

Preparation of gels of tuneable stiffness in a culture dish and experimental timeline A , 24 mm coverslips were treated with NaOH, APTES and Gluth (glutaraldehyde). Polyacrylamide gels were polymerized between a glue‐rimmed 30 mm coverslip and the treated side of the 24 mm coverslip. After polymerization the 24 mm coverslip, to which the gel was now attached, was turned. Subsequently, the gel was treated with the cross‐linker Sulpho SANPAH under UV light and coated with laminin. B , timeline of the cardiomyocyte culturing and detachment‐protocol. C , timeline of the cardiomyocyte transfer protocol.
Figure Legend Snippet: Preparation of gels of tuneable stiffness in a culture dish and experimental timeline A , 24 mm coverslips were treated with NaOH, APTES and Gluth (glutaraldehyde). Polyacrylamide gels were polymerized between a glue‐rimmed 30 mm coverslip and the treated side of the 24 mm coverslip. After polymerization the 24 mm coverslip, to which the gel was now attached, was turned. Subsequently, the gel was treated with the cross‐linker Sulpho SANPAH under UV light and coated with laminin. B , timeline of the cardiomyocyte culturing and detachment‐protocol. C , timeline of the cardiomyocyte transfer protocol.

Techniques Used:

16) Product Images from "The Interpretation of Current-Clamp Recordings in the Cell-Attached Patch-Clamp Configuration"

Article Title: The Interpretation of Current-Clamp Recordings in the Cell-Attached Patch-Clamp Configuration

Journal: Biophysical Journal

doi: 10.1529/biophysj.104.049866

The detection of single-channel events in RBL-1 cells before the measurement of membrane potential across the cell-attached patch. ( A ) Single-channel events from cell-attached patches were recorded during 950-ms ramps from +140 to −60 mV applied pipette potential from a pipette holding potential of +40 mV. Ramps were applied every 3 s. The cell was superfused with an external solution containing (in mM) 145 NaCl, 5 KCl, 1 CaCl 2 , 1 MgCl 2 , 10 Hepes, 10 D-glucose, pH 7.35 with NaOH. The pipette solution had the following composition (in mM): 150 KCl, 0.15 EGTA, 2 MgCl 2 , 10 Hepes, pH 7.3 with KOH. ( B ) After collection of single-channel data the amplifier was placed in current-clamp mode and membrane potential was recorded. Where indicated, an extracellular solution containing 154 mM K + was superfused into the experimental chamber.
Figure Legend Snippet: The detection of single-channel events in RBL-1 cells before the measurement of membrane potential across the cell-attached patch. ( A ) Single-channel events from cell-attached patches were recorded during 950-ms ramps from +140 to −60 mV applied pipette potential from a pipette holding potential of +40 mV. Ramps were applied every 3 s. The cell was superfused with an external solution containing (in mM) 145 NaCl, 5 KCl, 1 CaCl 2 , 1 MgCl 2 , 10 Hepes, 10 D-glucose, pH 7.35 with NaOH. The pipette solution had the following composition (in mM): 150 KCl, 0.15 EGTA, 2 MgCl 2 , 10 Hepes, pH 7.3 with KOH. ( B ) After collection of single-channel data the amplifier was placed in current-clamp mode and membrane potential was recorded. Where indicated, an extracellular solution containing 154 mM K + was superfused into the experimental chamber.

Techniques Used: Mass Spectrometry, Transferring

Simultaneous cell-attached current-clamp and whole-cell voltage-clamp recordings in a rat megakaryocyte. ( Upper panel ) Membrane currents recorded under whole-cell voltage-clamp during superfusion with normal saline solution: 145 NaCl, 5 KCl, 1 CaCl 2 , 1 MgCl 2 , 10 Hepes, 10 D-glucose, pH 7.35 with NaOH. The pipette contained (in mM) 150 KCl, 0.1 EGTA, 0.05 fura-2 penta K + salt, 0.05 Na 2 GTP, 2 MgCl 2 , 10 Hepes, pH 7.3 with KOH. ( Middle panel ) Holding potential set by whole-cell voltage-clamp ( VC ). Where indicated the cell was placed in current-clamp ( CC ) and membrane potential was recorded. Where noted, a seal test was performed and the capacitative transients were adjusted. ( Bottom panel ) Simultaneous current-clamp recording ( CC ) of membrane potential measured across an intact cell-attached patch in the same cell. The pipette contained the same internal as used for the whole-cell recordings.
Figure Legend Snippet: Simultaneous cell-attached current-clamp and whole-cell voltage-clamp recordings in a rat megakaryocyte. ( Upper panel ) Membrane currents recorded under whole-cell voltage-clamp during superfusion with normal saline solution: 145 NaCl, 5 KCl, 1 CaCl 2 , 1 MgCl 2 , 10 Hepes, 10 D-glucose, pH 7.35 with NaOH. The pipette contained (in mM) 150 KCl, 0.1 EGTA, 0.05 fura-2 penta K + salt, 0.05 Na 2 GTP, 2 MgCl 2 , 10 Hepes, pH 7.3 with KOH. ( Middle panel ) Holding potential set by whole-cell voltage-clamp ( VC ). Where indicated the cell was placed in current-clamp ( CC ) and membrane potential was recorded. Where noted, a seal test was performed and the capacitative transients were adjusted. ( Bottom panel ) Simultaneous current-clamp recording ( CC ) of membrane potential measured across an intact cell-attached patch in the same cell. The pipette contained the same internal as used for the whole-cell recordings.

Techniques Used: Transferring

Cell-attached current-clamp measurements of membrane potential in response to ADP application. Where indicated, the cell was superfused with 1 μ M ADP in saline containing (in mM) 145 NaCl, 5 KCl, 1 CaCl 2 , 1 MgCl 2 , 10 Hepes, 10 D-glucose, pH 7.35 with NaOH. The pipette contained (in mM) 150 KCl, 0.1 EGTA, 0.05 fura-2 penta K + salt, 0.05 Na 2 GTP, 2 MgCl 2 , 10 Hepes, pH 7.3 with KOH.
Figure Legend Snippet: Cell-attached current-clamp measurements of membrane potential in response to ADP application. Where indicated, the cell was superfused with 1 μ M ADP in saline containing (in mM) 145 NaCl, 5 KCl, 1 CaCl 2 , 1 MgCl 2 , 10 Hepes, 10 D-glucose, pH 7.35 with NaOH. The pipette contained (in mM) 150 KCl, 0.1 EGTA, 0.05 fura-2 penta K + salt, 0.05 Na 2 GTP, 2 MgCl 2 , 10 Hepes, pH 7.3 with KOH.

Techniques Used: Transferring

Whole-cell ramp currents recorded in an RBL-1 cell during application of high-K + solution. The whole-cell voltage-clamp configuration was obtained using a KCl-based pipette solution (in mM): 150 KCl, 2 EGTA, 1 CaCl 2 , 10 Hepes, pH 7.3 with KOH. Ramps of 200-ms duration from −140 to +60 mV were applied at 1-s intervals from a holding potential of −40 mV while the cell was superfused with normal saline (in mM): 145 NaCl, 5 KCl, 1 CaCl 2 , 1 MgCl 2 , 10 Hepes, 10 D-glucose, pH 7.35 with NaOH. The current record, labeled Pre-KCl , is the average of 16 ramps taken immediately before the first change in null current potential recorded during superfusion with 154 mM KCl solution. Whole-cell currents are shown 2, 5, 10, and 21 s after superfusion of high-K + solution.
Figure Legend Snippet: Whole-cell ramp currents recorded in an RBL-1 cell during application of high-K + solution. The whole-cell voltage-clamp configuration was obtained using a KCl-based pipette solution (in mM): 150 KCl, 2 EGTA, 1 CaCl 2 , 10 Hepes, pH 7.3 with KOH. Ramps of 200-ms duration from −140 to +60 mV were applied at 1-s intervals from a holding potential of −40 mV while the cell was superfused with normal saline (in mM): 145 NaCl, 5 KCl, 1 CaCl 2 , 1 MgCl 2 , 10 Hepes, 10 D-glucose, pH 7.35 with NaOH. The current record, labeled Pre-KCl , is the average of 16 ramps taken immediately before the first change in null current potential recorded during superfusion with 154 mM KCl solution. Whole-cell currents are shown 2, 5, 10, and 21 s after superfusion of high-K + solution.

Techniques Used: Transferring, Mass Spectrometry, Labeling

Cell-attached and whole-cell recording of membrane potential in partially depolarized RBL-1 cells during exposure to high K + . ( A ) An RBL-1 cell was superfused with normal external saline (in mM): 145 NaCl, 5 KCl, 1 CaCl 2 , 1 MgCl 2 , 10 Hepes, 10 D-glucose, pH 7.35 with NaOH, and membrane potential was recorded across a cell-attached patch using a K-glutamate-based internal (in mM): 150 K-glutamate, 2 EGTA, 1 CaCl 2 , 10 Hepes, pH 7.3 with KOH. Where indicated, a high K + -based external saline (154 mM K + ) was superfused into the chamber. The inset shows the initial response to application of high K + at higher temporal resolution. Data are corrected for a +13 mV liquid junction potential. ( B ) A different RBL-1 cell was superfused with normal external saline (in mM): 145 NaCl, 5 KCl, 1 CaCl 2 , 1 MgCl 2 , 10 Hepes, 10 D-glucose, pH 7.35 with NaOH, and membrane potential was recorded under current-clamp in the whole-cell configuration using a KCl-based pipette internal (in mM): 150 KCl, 0.15 EGTA, 2 MgCl 2 , 10 Hepes, pH 7.3 with KOH. Where indicated a high K + -based external saline (154 mM K + ) was superfused into the chamber. The inset shows the initial response to application of high K + at higher temporal resolution.
Figure Legend Snippet: Cell-attached and whole-cell recording of membrane potential in partially depolarized RBL-1 cells during exposure to high K + . ( A ) An RBL-1 cell was superfused with normal external saline (in mM): 145 NaCl, 5 KCl, 1 CaCl 2 , 1 MgCl 2 , 10 Hepes, 10 D-glucose, pH 7.35 with NaOH, and membrane potential was recorded across a cell-attached patch using a K-glutamate-based internal (in mM): 150 K-glutamate, 2 EGTA, 1 CaCl 2 , 10 Hepes, pH 7.3 with KOH. Where indicated, a high K + -based external saline (154 mM K + ) was superfused into the chamber. The inset shows the initial response to application of high K + at higher temporal resolution. Data are corrected for a +13 mV liquid junction potential. ( B ) A different RBL-1 cell was superfused with normal external saline (in mM): 145 NaCl, 5 KCl, 1 CaCl 2 , 1 MgCl 2 , 10 Hepes, 10 D-glucose, pH 7.35 with NaOH, and membrane potential was recorded under current-clamp in the whole-cell configuration using a KCl-based pipette internal (in mM): 150 KCl, 0.15 EGTA, 2 MgCl 2 , 10 Hepes, pH 7.3 with KOH. Where indicated a high K + -based external saline (154 mM K + ) was superfused into the chamber. The inset shows the initial response to application of high K + at higher temporal resolution.

Techniques Used: Transferring

17) Product Images from "Safe decontamination of cytostatics from the nitrogen mustards family. Part one: cyclophosphamide and ifosfamide"

Article Title: Safe decontamination of cytostatics from the nitrogen mustards family. Part one: cyclophosphamide and ifosfamide

Journal: International Journal of Nanomedicine

doi: 10.2147/IJN.S159328

Transformation products formed during IFOS degradation plotted as a function of the normalized concentration ( C / C 0 ) of IFOS decay. Note: Transformation products formed during the decontamination time (minutes) in the presence of ( A ) 5% NaClO agent, ( B ) 0.01 M NaOH agent, and ( C ) TiO 2 . Abbreviations: IFOS, ifosfamide; IFOS-TP1-OH, ifosforamide mustard.
Figure Legend Snippet: Transformation products formed during IFOS degradation plotted as a function of the normalized concentration ( C / C 0 ) of IFOS decay. Note: Transformation products formed during the decontamination time (minutes) in the presence of ( A ) 5% NaClO agent, ( B ) 0.01 M NaOH agent, and ( C ) TiO 2 . Abbreviations: IFOS, ifosfamide; IFOS-TP1-OH, ifosforamide mustard.

Techniques Used: Transformation Assay, Concentration Assay

Transformation products formed during CP degradation plotted as a function of the normalized concentration ( C / C 0 ) of cyclophosphamide decay. Note: Transformation products formed during the decontamination time (minutes) in the presence of ( A ) 5% NaClO agent, ( B ) 0.01 M NaOH agent, and ( C ) TiO 2 . Abbreviations: CP, cyclophosphamide; CP-TP1-OCl, 4-hydroxy-cyclophosphamide; CP-TP2-OCl, ifosfamide.
Figure Legend Snippet: Transformation products formed during CP degradation plotted as a function of the normalized concentration ( C / C 0 ) of cyclophosphamide decay. Note: Transformation products formed during the decontamination time (minutes) in the presence of ( A ) 5% NaClO agent, ( B ) 0.01 M NaOH agent, and ( C ) TiO 2 . Abbreviations: CP, cyclophosphamide; CP-TP1-OCl, 4-hydroxy-cyclophosphamide; CP-TP2-OCl, ifosfamide.

Techniques Used: Transformation Assay, Concentration Assay

18) Product Images from "Safe decontamination of cytostatics from the nitrogen mustards family. Part one: cyclophosphamide and ifosfamide"

Article Title: Safe decontamination of cytostatics from the nitrogen mustards family. Part one: cyclophosphamide and ifosfamide

Journal: International Journal of Nanomedicine

doi: 10.2147/IJN.S159328

Transformation products formed during IFOS degradation plotted as a function of the normalized concentration ( C / C 0 ) of IFOS decay. Note: Transformation products formed during the decontamination time (minutes) in the presence of ( A ) 5% NaClO agent, ( B ) 0.01 M NaOH agent, and ( C ) TiO 2 . Abbreviations: IFOS, ifosfamide; IFOS-TP1-OH, ifosforamide mustard.
Figure Legend Snippet: Transformation products formed during IFOS degradation plotted as a function of the normalized concentration ( C / C 0 ) of IFOS decay. Note: Transformation products formed during the decontamination time (minutes) in the presence of ( A ) 5% NaClO agent, ( B ) 0.01 M NaOH agent, and ( C ) TiO 2 . Abbreviations: IFOS, ifosfamide; IFOS-TP1-OH, ifosforamide mustard.

Techniques Used: Transformation Assay, Concentration Assay

Transformation products formed during CP degradation plotted as a function of the normalized concentration ( C / C 0 ) of cyclophosphamide decay. Note: Transformation products formed during the decontamination time (minutes) in the presence of ( A ) 5% NaClO agent, ( B ) 0.01 M NaOH agent, and ( C ) TiO 2 . Abbreviations: CP, cyclophosphamide; CP-TP1-OCl, 4-hydroxy-cyclophosphamide; CP-TP2-OCl, ifosfamide.
Figure Legend Snippet: Transformation products formed during CP degradation plotted as a function of the normalized concentration ( C / C 0 ) of cyclophosphamide decay. Note: Transformation products formed during the decontamination time (minutes) in the presence of ( A ) 5% NaClO agent, ( B ) 0.01 M NaOH agent, and ( C ) TiO 2 . Abbreviations: CP, cyclophosphamide; CP-TP1-OCl, 4-hydroxy-cyclophosphamide; CP-TP2-OCl, ifosfamide.

Techniques Used: Transformation Assay, Concentration Assay

19) Product Images from "Extension of the ‘Inorganic Gel Casting’ Process to the Manufacturing of Boro-Alumino-Silicate Glass Foams"

Article Title: Extension of the ‘Inorganic Gel Casting’ Process to the Manufacturing of Boro-Alumino-Silicate Glass Foams

Journal: Materials

doi: 10.3390/ma11122545

27 Al ( a ) and 11 B ( b ) Nuclear magnetic resonance (NMR) studies BSG glass in the as received state, after alkali activation (in ‘green’ foams, NaOH/KOH activation) and after firing (in final foams).
Figure Legend Snippet: 27 Al ( a ) and 11 B ( b ) Nuclear magnetic resonance (NMR) studies BSG glass in the as received state, after alkali activation (in ‘green’ foams, NaOH/KOH activation) and after firing (in final foams).

Techniques Used: Nuclear Magnetic Resonance, Activation Assay

29 Si NMR studies of BSG glass: ( a ) comparison of spectra in the as received state, after alkali activation (in ‘green’ foams, NaOH/KOH activation) and after firing (in final foams); ( b ) deconvolution analysis: blue lines, from experimental spectra, overlap with fitted curves, in red.
Figure Legend Snippet: 29 Si NMR studies of BSG glass: ( a ) comparison of spectra in the as received state, after alkali activation (in ‘green’ foams, NaOH/KOH activation) and after firing (in final foams); ( b ) deconvolution analysis: blue lines, from experimental spectra, overlap with fitted curves, in red.

Techniques Used: Nuclear Magnetic Resonance, Activation Assay

Fourier transform infrared (FTIR) analysis of boro-alumino-silicated glass (BSG) in the as received state, after alkali activation (in ‘green’ foams, NaOH/KOH activation) and after firing (in final foams)
Figure Legend Snippet: Fourier transform infrared (FTIR) analysis of boro-alumino-silicated glass (BSG) in the as received state, after alkali activation (in ‘green’ foams, NaOH/KOH activation) and after firing (in final foams)

Techniques Used: Activation Assay

Morphology of BSG-derived glass foams (surfactant: Triton X-100): ( a , c ) NaOH activation; ( b , d ) NaOH/KOH activation.
Figure Legend Snippet: Morphology of BSG-derived glass foams (surfactant: Triton X-100): ( a , c ) NaOH activation; ( b , d ) NaOH/KOH activation.

Techniques Used: Derivative Assay, Activation Assay

Morphology of foams in the ‘green’ state (before firing): ( a ) NaOH/KOH activation; ( b ) KOH activation.
Figure Legend Snippet: Morphology of foams in the ‘green’ state (before firing): ( a ) NaOH/KOH activation; ( b ) KOH activation.

Techniques Used: Activation Assay

20) Product Images from "Corrosion of Hydrogen Storage Metal Alloy LaMm-Ni4.1Al0.3Mn0.4Co0.45 in the Aqueous Solutions of Alkali Metal Hydroxides"

Article Title: Corrosion of Hydrogen Storage Metal Alloy LaMm-Ni4.1Al0.3Mn0.4Co0.45 in the Aqueous Solutions of Alkali Metal Hydroxides

Journal: Materials

doi: 10.3390/ma11122423

SEM images of a surface of LaMm-Ni 4.1 Al 0.3 Mn 0.4 Co 0.45 alloy not subjected to any treatment ( A ), and after electrochemical treatment in 1 M LiOH ( B ), 1 M NaOH ( C ), and 1 M KOH ( D ).
Figure Legend Snippet: SEM images of a surface of LaMm-Ni 4.1 Al 0.3 Mn 0.4 Co 0.45 alloy not subjected to any treatment ( A ), and after electrochemical treatment in 1 M LiOH ( B ), 1 M NaOH ( C ), and 1 M KOH ( D ).

Techniques Used:

SEM images of a surface of LaMm-Ni 4.1 Al 0.3 Mn 0.4 Co 0.45 alloy not subjected to any treatment ( A ), and after electrochemical treatment at 6 M electrolytes: 6 M LiOH/KOH ( B ), 6 M NaOH/KOH ( C ), 6 M KOH ( D ), 6 M RbOH/KOH ( E ), and 6 M CsOH/KOH ( F ).
Figure Legend Snippet: SEM images of a surface of LaMm-Ni 4.1 Al 0.3 Mn 0.4 Co 0.45 alloy not subjected to any treatment ( A ), and after electrochemical treatment at 6 M electrolytes: 6 M LiOH/KOH ( B ), 6 M NaOH/KOH ( C ), 6 M KOH ( D ), 6 M RbOH/KOH ( E ), and 6 M CsOH/KOH ( F ).

Techniques Used:

Related Articles

Modification:

Article Title: Oxygen Reduction Reaction at Penta-Coordinated Co Phthalocyanines
Article Snippet: .. Modification of Co Phthalocyanines Cobalt phthalocyanine (CoPc), cobalt-hexadecafluorophthalocyanine (16(F)CoPc), and 4-aminopyridine (Py), 2,2-diphenyl-1-picryl- hydrazyl (DPPH), N,N-dimethylformamide (DMF), isopropyl alcohol, NaOH, HCl, K2 HPO4 were obtained from Sigma (St. Louis, USA). .. Cobalt-octaethylhexyloxyphthalocyanine (8(2-Et-C6 H11 O)CoPc), was synthesized according to the literature (Weber and Busch, ).

Electron Microscopy:

Article Title: High-affinity Anticalins with aggregation-blocking activity directed against the Alzheimer β-amyloid peptide
Article Snippet: .. Transmission electron microscopy A 200 μM solution of Aβ42, aged for 6 h at 4°C in a 1:1 mixture of 5 mM NaOH and 20 mM Tris/HCl, pH 6.8, was diluted to 10 μM in RPMI-1640 medium (Sigma) in the presence or absence of equimolar concentrations of Anticalin or MAb 6E10 (Covance). .. After incubation for 72 h at 37°C the mixture was fixed on poly-L -lysine coated copper grids (Plano) and negatively stained with 1% (w/v) uranyl acetate.

other:

Article Title: Rescue of human corneal epithelial cells after alkaline insult using renalase derived peptide, RP-220
Article Snippet: For rescue assays involving RP-220, a 6 mmol/L solution of NaOH was prepared from a stock 10 mol/L NaOH (Sigma) solution, filtered through 0.22 µm filter (Merck Millipore, Cork Ireland).

Transmission Assay:

Article Title: High-affinity Anticalins with aggregation-blocking activity directed against the Alzheimer β-amyloid peptide
Article Snippet: .. Transmission electron microscopy A 200 μM solution of Aβ42, aged for 6 h at 4°C in a 1:1 mixture of 5 mM NaOH and 20 mM Tris/HCl, pH 6.8, was diluted to 10 μM in RPMI-1640 medium (Sigma) in the presence or absence of equimolar concentrations of Anticalin or MAb 6E10 (Covance). .. After incubation for 72 h at 37°C the mixture was fixed on poly-L -lysine coated copper grids (Plano) and negatively stained with 1% (w/v) uranyl acetate.

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  • 91
    Millipore hepes naoh buffer
    The effects of pH and temperature on the activities and stabilities of Teth514_1788 and Teth514_1789. ( A ) The thermal stabilities of 360 n m Teth514_1788 (closed symbols) and 320 n m Teth514_1789 (open symbols) at a temperature range between 30–90°C for 30 min. ( B ) The pH stabilities of 360 n m Teth514_1788 (closed symbols) and 320 n m Teth514_1789 (open symbols) at 4°C for 24 h. ( C ) The pH dependence on the phosphorolytic and synthetic activities of Teth514_1788 (44 n m ) in 40 m m sodium citrate (pH 3.0–5.5), bis(2-hydroxyethyl)iminotris(hydroxymethyl)methane-HCl (pH 5.5–7.0), <t>HEPES-NaOH</t> (pH 7.0–8.5), and glycine-NaOH (pH 8.5–10.5). ( D ) The pH dependence of the phosphorolytic and synthetic activities of Teth514_1789 (32 n m ) in the same buffers listed in Panel C. In Panels C and D, the closed and open symbols represent the synthetic and phosphorolytic activities, respectively.
    Hepes Naoh Buffer, supplied by Millipore, used in various techniques. Bioz Stars score: 91/100, based on 9 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/hepes naoh buffer/product/Millipore
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    Price from $9.99 to $1999.99
    hepes naoh buffer - by Bioz Stars, 2020-09
    91/100 stars
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    88
    Millipore m mops naoh
    pH ( A ) and temperature ( B ) profiles of Cpin_6279rC. The stability ( dashed line ) and optimum ( solid line ) are shown. A, buffers used for incubation and enzymatic reaction were sodium citrate (pH 3.0–5.5, closed circles ), <t>MES-NaOH</t> (pH 5.5–6.5, open circles ), <t>MOPS-NaOH</t> (pH 6.5–7.5, closed triangles ), 2-hydroxy-3-[4-(2-hydroxyethyl)-1-piperazinyl]propanesulfonic acid-NaOH (pH 7.5–8.5, open triangles ), and glycine-NaOH (pH 8.6–10, closed rhombi ). The highest activity was defined as 100% (stability, pH 6.5; and optimum, pH 6.0). B, highest activity was defined as 100% (50 °C). As for the enzymatic reaction at 60 and 70 °C, the data from 0 to 1.5 min were used to calculate the initial velocity.
    M Mops Naoh, supplied by Millipore, used in various techniques. Bioz Stars score: 88/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    93
    Millipore n naoh
    pH ( A ) and temperature ( B ) profiles of Cpin_6279rC. The stability ( dashed line ) and optimum ( solid line ) are shown. A, buffers used for incubation and enzymatic reaction were sodium citrate (pH 3.0–5.5, closed circles ), <t>MES-NaOH</t> (pH 5.5–6.5, open circles ), <t>MOPS-NaOH</t> (pH 6.5–7.5, closed triangles ), 2-hydroxy-3-[4-(2-hydroxyethyl)-1-piperazinyl]propanesulfonic acid-NaOH (pH 7.5–8.5, open triangles ), and glycine-NaOH (pH 8.6–10, closed rhombi ). The highest activity was defined as 100% (stability, pH 6.5; and optimum, pH 6.0). B, highest activity was defined as 100% (50 °C). As for the enzymatic reaction at 60 and 70 °C, the data from 0 to 1.5 min were used to calculate the initial velocity.
    N Naoh, supplied by Millipore, used in various techniques. Bioz Stars score: 93/100, based on 30 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Average 93 stars, based on 30 article reviews
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    Image Search Results


    The effects of pH and temperature on the activities and stabilities of Teth514_1788 and Teth514_1789. ( A ) The thermal stabilities of 360 n m Teth514_1788 (closed symbols) and 320 n m Teth514_1789 (open symbols) at a temperature range between 30–90°C for 30 min. ( B ) The pH stabilities of 360 n m Teth514_1788 (closed symbols) and 320 n m Teth514_1789 (open symbols) at 4°C for 24 h. ( C ) The pH dependence on the phosphorolytic and synthetic activities of Teth514_1788 (44 n m ) in 40 m m sodium citrate (pH 3.0–5.5), bis(2-hydroxyethyl)iminotris(hydroxymethyl)methane-HCl (pH 5.5–7.0), HEPES-NaOH (pH 7.0–8.5), and glycine-NaOH (pH 8.5–10.5). ( D ) The pH dependence of the phosphorolytic and synthetic activities of Teth514_1789 (32 n m ) in the same buffers listed in Panel C. In Panels C and D, the closed and open symbols represent the synthetic and phosphorolytic activities, respectively.

    Journal: PLoS ONE

    Article Title: Discovery of Two β-1,2-Mannoside Phosphorylases Showing Different Chain-Length Specificities from Thermoanaerobacter sp. X-514

    doi: 10.1371/journal.pone.0114882

    Figure Lengend Snippet: The effects of pH and temperature on the activities and stabilities of Teth514_1788 and Teth514_1789. ( A ) The thermal stabilities of 360 n m Teth514_1788 (closed symbols) and 320 n m Teth514_1789 (open symbols) at a temperature range between 30–90°C for 30 min. ( B ) The pH stabilities of 360 n m Teth514_1788 (closed symbols) and 320 n m Teth514_1789 (open symbols) at 4°C for 24 h. ( C ) The pH dependence on the phosphorolytic and synthetic activities of Teth514_1788 (44 n m ) in 40 m m sodium citrate (pH 3.0–5.5), bis(2-hydroxyethyl)iminotris(hydroxymethyl)methane-HCl (pH 5.5–7.0), HEPES-NaOH (pH 7.0–8.5), and glycine-NaOH (pH 8.5–10.5). ( D ) The pH dependence of the phosphorolytic and synthetic activities of Teth514_1789 (32 n m ) in the same buffers listed in Panel C. In Panels C and D, the closed and open symbols represent the synthetic and phosphorolytic activities, respectively.

    Article Snippet: After washing with buffer A containing 22 mm imidazole and subsequently eluting the proteins with a 22–400 mm imidazole linear gradient in buffer A, the fractions containing the recombinant protein were pooled, dialyzed against 10 mm HEPES-NaOH buffer (pH 7.0), and concentrated (AMICON Ultra-15 filter; Millipore, Billerica, MA, USA).

    Techniques:

    pH ( A ) and temperature ( B ) profiles of Cpin_6279rC. The stability ( dashed line ) and optimum ( solid line ) are shown. A, buffers used for incubation and enzymatic reaction were sodium citrate (pH 3.0–5.5, closed circles ), MES-NaOH (pH 5.5–6.5, open circles ), MOPS-NaOH (pH 6.5–7.5, closed triangles ), 2-hydroxy-3-[4-(2-hydroxyethyl)-1-piperazinyl]propanesulfonic acid-NaOH (pH 7.5–8.5, open triangles ), and glycine-NaOH (pH 8.6–10, closed rhombi ). The highest activity was defined as 100% (stability, pH 6.5; and optimum, pH 6.0). B, highest activity was defined as 100% (50 °C). As for the enzymatic reaction at 60 and 70 °C, the data from 0 to 1.5 min were used to calculate the initial velocity.

    Journal: The Journal of Biological Chemistry

    Article Title: Biochemical and structural analyses of a bacterial endo-β-1,2-glucanase reveal a new glycoside hydrolase family

    doi: 10.1074/jbc.M116.762724

    Figure Lengend Snippet: pH ( A ) and temperature ( B ) profiles of Cpin_6279rC. The stability ( dashed line ) and optimum ( solid line ) are shown. A, buffers used for incubation and enzymatic reaction were sodium citrate (pH 3.0–5.5, closed circles ), MES-NaOH (pH 5.5–6.5, open circles ), MOPS-NaOH (pH 6.5–7.5, closed triangles ), 2-hydroxy-3-[4-(2-hydroxyethyl)-1-piperazinyl]propanesulfonic acid-NaOH (pH 7.5–8.5, open triangles ), and glycine-NaOH (pH 8.6–10, closed rhombi ). The highest activity was defined as 100% (stability, pH 6.5; and optimum, pH 6.0). B, highest activity was defined as 100% (50 °C). As for the enzymatic reaction at 60 and 70 °C, the data from 0 to 1.5 min were used to calculate the initial velocity.

    Article Snippet: The enzymatic reaction was conducted by adding 10 μl of 40 μg/ml Cpin_6279rC in 20 m m MOPS-NaOH (pH 6.5) to the substrate solution at 30 °C for 1 h. After the reaction, the reaction mixture was applied to Amicon Ultra 10,000 molecular weight cutoff (Millipore), and the flow-through solution was collected.

    Techniques: Incubation, Activity Assay