Structured Review

Millipore acrylamide
<t>Acrylamide-induced</t> quenching of intrinsic fluorescence of GGBP/H152C. Modified according Equation (12), Stern-Volmer dependences of the GGBP/H152C fluorescence intensity on acrylamide concentration in the solutions without denaturant (black curve) and in the presence of 0.1 M GdnHCl (red curve). The excitation wavelength was 297 nm.
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Images

1) Product Images from "Osmolyte-Like Stabilizing Effects of Low GdnHCl Concentrations on d-Glucose/d-Galactose-Binding Protein"

Article Title: Osmolyte-Like Stabilizing Effects of Low GdnHCl Concentrations on d-Glucose/d-Galactose-Binding Protein

Journal: International Journal of Molecular Sciences

doi: 10.3390/ijms18092008

Acrylamide-induced quenching of intrinsic fluorescence of GGBP/H152C. Modified according Equation (12), Stern-Volmer dependences of the GGBP/H152C fluorescence intensity on acrylamide concentration in the solutions without denaturant (black curve) and in the presence of 0.1 M GdnHCl (red curve). The excitation wavelength was 297 nm.
Figure Legend Snippet: Acrylamide-induced quenching of intrinsic fluorescence of GGBP/H152C. Modified according Equation (12), Stern-Volmer dependences of the GGBP/H152C fluorescence intensity on acrylamide concentration in the solutions without denaturant (black curve) and in the presence of 0.1 M GdnHCl (red curve). The excitation wavelength was 297 nm.

Techniques Used: Fluorescence, Modification, Concentration Assay

2) Product Images from "Substrate stiffness regulates extracellular matrix deposition by alveolar epithelial cells"

Article Title: Substrate stiffness regulates extracellular matrix deposition by alveolar epithelial cells

Journal: Research and reports in biology

doi: 10.2147/RRB.S13178

Characterization of polyacrylamide gel stiffness with mol% acrylamide:bis-acrylamide composition of 7.5%:0.2% (low), 7.5%:0.35% (medium), and 12%:0.6% (high). A ) Elastic moduli as function of bis-acrylamide cross-linker concentration for polyacrylamide
Figure Legend Snippet: Characterization of polyacrylamide gel stiffness with mol% acrylamide:bis-acrylamide composition of 7.5%:0.2% (low), 7.5%:0.35% (medium), and 12%:0.6% (high). A ) Elastic moduli as function of bis-acrylamide cross-linker concentration for polyacrylamide

Techniques Used: Concentration Assay

3) Product Images from "Use of high-refractive index hydrogels and tissue clearing for large biological sample imaging"

Article Title: Use of high-refractive index hydrogels and tissue clearing for large biological sample imaging

Journal: bioRxiv

doi: 10.1101/2020.01.22.905695

Physical description of high refractive index hydrogels. The chemical structures of acrylamide ( A ), methacrylamide ( B ) and tri(ethlene glycol) dimethacrylate ( C ) are shown. Changes in hydrogel size following synthesis and immersion in PBS for 24 hours were measured ( n=8 ) ( D ), together with the water content of high refractive index hydrogels ( n=8 ) ( E ). Histograms ( D and E ) representing the mean ± sd and results were analysed by one-way ANOVA with Dunn’s multiple comparison’s test. *p
Figure Legend Snippet: Physical description of high refractive index hydrogels. The chemical structures of acrylamide ( A ), methacrylamide ( B ) and tri(ethlene glycol) dimethacrylate ( C ) are shown. Changes in hydrogel size following synthesis and immersion in PBS for 24 hours were measured ( n=8 ) ( D ), together with the water content of high refractive index hydrogels ( n=8 ) ( E ). Histograms ( D and E ) representing the mean ± sd and results were analysed by one-way ANOVA with Dunn’s multiple comparison’s test. *p

Techniques Used:

4) Product Images from "Large-scale curvature sensing by epithelial monolayers depends on active cell mechanics and nuclear mechanoadaptation"

Article Title: Large-scale curvature sensing by epithelial monolayers depends on active cell mechanics and nuclear mechanoadaptation

Journal: bioRxiv

doi: 10.1101/2020.07.04.187468

Formation of wavy epithelial monolayers on corrugated polyacrylamide hydrogels. (A) UV-Induced radical photo-polymerization of hydroxypolyacrylamide (hydroxy-PAAm) hydrogels. The radical polymerization of acrylamide (AAm, in black), bis-acrylamide (bis-acrylamide, in red) and N-hydroxyethylacrylamide (HEA, in blue) is amorced by the photoinitiator Iragure 2959 under UV exposure at 360 nm and leads to an acrylamide hydrogel with hydroxyl groups (hydroxy-PAAm). (B) Schematic representation of the UV photo-polymerization of hydroxy-PAAm hydrogels through an optical photomask. Typical atomic force microscopy (AFM) topography images of corrugated hydrogels of (C) 20 μm (P20, left) and (D) 30 μm (P30, right) wavelength. Image area is 100 μm × 100 μm for both. 3D rendering of tapping-mode topography images of (E) P20 (left) and (F) P30 (right) hydrogels. Schematic representation (side view) of (G) P20 and (H) P30 profiles with wavelengths (λ), amplitudes (A) and the radius (R) of curvature for concave (−) and convex (+) topologies. Confocal volume rendering of a MDCK epithelial monolayer grown on (I) P20 and (J) P30 corrugated hydrogels and stained for actin (in green) and DNA (in blue). (K) Maximum intensity projection and confocal orthogonal projections at (L) basal and (M) apical planes of an epithelial monolayer grown on a P30 hydrogel and stained for F-actin (in green) and nuclei (in blue). Scale bars are 30 μm. (N) Total actin intensity in epithelial tissues grown on flat (black), P20 (grey) and P30 (red) hydrogels. n=8 (flat in black), n=10 (P20 in grey) and n=12 (P30 in red). (O) Maximum intensity projection and confocal orthogonal projections at (P) the basal and (Q) the apical planes of an epithelial tissue grown on a P30 hydrogel and stained for β-catenin (red) and nucleus (blue). Total ß-catenin intensity in epithelial tissues grown on flat (black), P20 (grey) and P30 (red) hydrogels. n=10 (flat in black), n=9 (P20 in grey) and n=13 (P30 in red). n.s. is not significant.
Figure Legend Snippet: Formation of wavy epithelial monolayers on corrugated polyacrylamide hydrogels. (A) UV-Induced radical photo-polymerization of hydroxypolyacrylamide (hydroxy-PAAm) hydrogels. The radical polymerization of acrylamide (AAm, in black), bis-acrylamide (bis-acrylamide, in red) and N-hydroxyethylacrylamide (HEA, in blue) is amorced by the photoinitiator Iragure 2959 under UV exposure at 360 nm and leads to an acrylamide hydrogel with hydroxyl groups (hydroxy-PAAm). (B) Schematic representation of the UV photo-polymerization of hydroxy-PAAm hydrogels through an optical photomask. Typical atomic force microscopy (AFM) topography images of corrugated hydrogels of (C) 20 μm (P20, left) and (D) 30 μm (P30, right) wavelength. Image area is 100 μm × 100 μm for both. 3D rendering of tapping-mode topography images of (E) P20 (left) and (F) P30 (right) hydrogels. Schematic representation (side view) of (G) P20 and (H) P30 profiles with wavelengths (λ), amplitudes (A) and the radius (R) of curvature for concave (−) and convex (+) topologies. Confocal volume rendering of a MDCK epithelial monolayer grown on (I) P20 and (J) P30 corrugated hydrogels and stained for actin (in green) and DNA (in blue). (K) Maximum intensity projection and confocal orthogonal projections at (L) basal and (M) apical planes of an epithelial monolayer grown on a P30 hydrogel and stained for F-actin (in green) and nuclei (in blue). Scale bars are 30 μm. (N) Total actin intensity in epithelial tissues grown on flat (black), P20 (grey) and P30 (red) hydrogels. n=8 (flat in black), n=10 (P20 in grey) and n=12 (P30 in red). (O) Maximum intensity projection and confocal orthogonal projections at (P) the basal and (Q) the apical planes of an epithelial tissue grown on a P30 hydrogel and stained for β-catenin (red) and nucleus (blue). Total ß-catenin intensity in epithelial tissues grown on flat (black), P20 (grey) and P30 (red) hydrogels. n=10 (flat in black), n=9 (P20 in grey) and n=13 (P30 in red). n.s. is not significant.

Techniques Used: Microscopy, Staining

5) Product Images from "Exploiting luminescence spectroscopy to elucidate the interaction between sugar and a tryptophan residue in the lactose permease of Escherichia coli"

Article Title: Exploiting luminescence spectroscopy to elucidate the interaction between sugar and a tryptophan residue in the lactose permease of Escherichia coli

Journal: Proceedings of the National Academy of Sciences of the United States of America

doi: 10.1073/pnas.1835645100

The effect of sugar on collisional quenching of Trp-151 fluorescence. Stern–Volmer plots of Trp-151 fluorescence quenching by Cs + (Cesium) ( A ), I – (Iodide) ( B ), or acrylamide ( C ) in the absence (filled circles) or presence (open circles) of 15 mM TDG are shown. Purified detergent-solubilized single-W151/C154G LacY (5 μM) was titrated with small aliquots of stock solutions of 5 M CsCl, KI, or acrylamide. The data were fit to linear Stern–Volmer plots (see Experimental Procedures ), and K SV values were calculated from the slope of the plots. Fluorescence spectra were recorded as described previously.
Figure Legend Snippet: The effect of sugar on collisional quenching of Trp-151 fluorescence. Stern–Volmer plots of Trp-151 fluorescence quenching by Cs + (Cesium) ( A ), I – (Iodide) ( B ), or acrylamide ( C ) in the absence (filled circles) or presence (open circles) of 15 mM TDG are shown. Purified detergent-solubilized single-W151/C154G LacY (5 μM) was titrated with small aliquots of stock solutions of 5 M CsCl, KI, or acrylamide. The data were fit to linear Stern–Volmer plots (see Experimental Procedures ), and K SV values were calculated from the slope of the plots. Fluorescence spectra were recorded as described previously.

Techniques Used: Fluorescence, Purification

6) Product Images from "Myricitrin Inhibits Acrylamide-Mediated Cytotoxicity in Human Caco-2 Cells by Preventing Oxidative Stress"

Article Title: Myricitrin Inhibits Acrylamide-Mediated Cytotoxicity in Human Caco-2 Cells by Preventing Oxidative Stress

Journal: BioMed Research International

doi: 10.1155/2013/724183

Effect of myricitrin on acrylamide-induced cytotoxity in human Caco-2 cells. The Caco-2 cells were exposed to 5 mM acrylamide for 48 h in the presence or absence of myricitrin; cell viability was detected using MTT method. Data of column represent means ± SD of three independent experiments (* P
Figure Legend Snippet: Effect of myricitrin on acrylamide-induced cytotoxity in human Caco-2 cells. The Caco-2 cells were exposed to 5 mM acrylamide for 48 h in the presence or absence of myricitrin; cell viability was detected using MTT method. Data of column represent means ± SD of three independent experiments (* P

Techniques Used: MTT Assay

Effect of water extract of bayberry on ROS production in acrylamide-treated Caco-2 cells. (a) After treatment with 5 mM acrylamide in the presence or absence of myricitrin for 0–48 h, Caco-2 cells were incubated with 10 μ M DCFH-DA for 30 min and then immediately subjected to fluorescence microscope analysis. (b) The quantitative data of panel (a) and results were expressed as mean DCF fluorescence intensity (means ± SD of three independent experiments). * P value represents significant difference between conditions, where P
Figure Legend Snippet: Effect of water extract of bayberry on ROS production in acrylamide-treated Caco-2 cells. (a) After treatment with 5 mM acrylamide in the presence or absence of myricitrin for 0–48 h, Caco-2 cells were incubated with 10 μ M DCFH-DA for 30 min and then immediately subjected to fluorescence microscope analysis. (b) The quantitative data of panel (a) and results were expressed as mean DCF fluorescence intensity (means ± SD of three independent experiments). * P value represents significant difference between conditions, where P

Techniques Used: Incubation, Fluorescence, Microscopy

7) Product Images from "Effects of Acrylamide on the Activity and Structure of Human Brain Creatine Kinase"

Article Title: Effects of Acrylamide on the Activity and Structure of Human Brain Creatine Kinase

Journal: International Journal of Molecular Sciences

doi: 10.3390/ijms10104210

Effect of acrylamide on the activity of HBCK. The residual activity was measured after 2 h incubation of HBCK in 50 mM Tris-HCl buffer, pH 8.0, with the addition of various concentrations of acrylamide at 25 °C. The final enzyme concentration was 2 μM. The data are presented as average ± standard errors for three repetitions.
Figure Legend Snippet: Effect of acrylamide on the activity of HBCK. The residual activity was measured after 2 h incubation of HBCK in 50 mM Tris-HCl buffer, pH 8.0, with the addition of various concentrations of acrylamide at 25 °C. The final enzyme concentration was 2 μM. The data are presented as average ± standard errors for three repetitions.

Techniques Used: Activity Assay, Incubation, Concentration Assay

Inactivation kinetics of HBCK by various concentrations of acrylamide ranging from 0 to 800 mM. The enzyme solutions were mixed with various concentrations of acrylamide, and aliquots were taken at the indicated time points. Then the residual activity was measured using the standard activity assay, and the data were normalized by taking the activity recorded at 0 min as 100%. The data were fitted by a biphasic process, and the fitted data are presented as solid lines. The rate constants are presented in Table 1 .
Figure Legend Snippet: Inactivation kinetics of HBCK by various concentrations of acrylamide ranging from 0 to 800 mM. The enzyme solutions were mixed with various concentrations of acrylamide, and aliquots were taken at the indicated time points. Then the residual activity was measured using the standard activity assay, and the data were normalized by taking the activity recorded at 0 min as 100%. The data were fitted by a biphasic process, and the fitted data are presented as solid lines. The rate constants are presented in Table 1 .

Techniques Used: Activity Assay

Effect of acrylamide on the ANS fluorescence of HBCK. The enzyme solutions were mixed with various concentrations of acrylamide and equilibrated for 2 h. The final concentration of ANS was 40 μM, and the solutions were incubated at ambient temperature for 30 min in the dark before measurements. The final enzyme concentration was 2 μM. The presented spectra were obtained by subtracting the spectra of ANS in the same buffer.
Figure Legend Snippet: Effect of acrylamide on the ANS fluorescence of HBCK. The enzyme solutions were mixed with various concentrations of acrylamide and equilibrated for 2 h. The final concentration of ANS was 40 μM, and the solutions were incubated at ambient temperature for 30 min in the dark before measurements. The final enzyme concentration was 2 μM. The presented spectra were obtained by subtracting the spectra of ANS in the same buffer.

Techniques Used: Fluorescence, Concentration Assay, Incubation

Native-PAGE analysis of the tertiary structural changes of HBCK induced by acrylamide. The protein was dissolved in 50 mM Tris-HCl buffer, pH 8.0, in the presence of various concentrations of acrylamide. Lanes 1–6 indicate the protein incubated in the buffer with the addition of 0, 50, 100, 200, 400 and 800 mM acrylamide, respectively.
Figure Legend Snippet: Native-PAGE analysis of the tertiary structural changes of HBCK induced by acrylamide. The protein was dissolved in 50 mM Tris-HCl buffer, pH 8.0, in the presence of various concentrations of acrylamide. Lanes 1–6 indicate the protein incubated in the buffer with the addition of 0, 50, 100, 200, 400 and 800 mM acrylamide, respectively.

Techniques Used: Clear Native PAGE, Incubation

The surface of HBCK (A and B) and acrylamide binding sites predicted by Autodock (C and D) and Fred (E and F). (A and B) The surface of the HBCK molecule. The yellow parts indicated the position of the cleft or pocket between the two domains of HBCK. Panel (B) shows the top view of the structure shown in panel (A). (C-F) The residues forming the binding site are shown by a line model, the acrylamide molecule is presented by a space-filling model, while Glu232 is highlighted by a stick model.
Figure Legend Snippet: The surface of HBCK (A and B) and acrylamide binding sites predicted by Autodock (C and D) and Fred (E and F). (A and B) The surface of the HBCK molecule. The yellow parts indicated the position of the cleft or pocket between the two domains of HBCK. Panel (B) shows the top view of the structure shown in panel (A). (C-F) The residues forming the binding site are shown by a line model, the acrylamide molecule is presented by a space-filling model, while Glu232 is highlighted by a stick model.

Techniques Used: Binding Assay

8) Product Images from "Increased Collagen Turnover Impairs Tendon Microstructure and Stability in Integrin α2β1-Deficient Mice"

Article Title: Increased Collagen Turnover Impairs Tendon Microstructure and Stability in Integrin α2β1-Deficient Mice

Journal: International Journal of Molecular Sciences

doi: 10.3390/ijms21082835

Resident MMP-2 activity is increased in integrin α2β1-deficient tendons. Gelatin zymography of 30-µg tendon lysate. Quantification of the MMP-2-activity signal ( A ). Zymography gel 10% acrylamide with polymerized gelatin. The arrows depict the pro and active forms of MMP-9 and MMP-2, respectively ( B ). C-terminal fragments (CTX) ELISA quantification of soluble collagen fragments in the tendon ( C ) (N = 5). Mann-Whitney U test was used for statistical testing (** p
Figure Legend Snippet: Resident MMP-2 activity is increased in integrin α2β1-deficient tendons. Gelatin zymography of 30-µg tendon lysate. Quantification of the MMP-2-activity signal ( A ). Zymography gel 10% acrylamide with polymerized gelatin. The arrows depict the pro and active forms of MMP-9 and MMP-2, respectively ( B ). C-terminal fragments (CTX) ELISA quantification of soluble collagen fragments in the tendon ( C ) (N = 5). Mann-Whitney U test was used for statistical testing (** p

Techniques Used: Activity Assay, Zymography, Enzyme-linked Immunosorbent Assay, MANN-WHITNEY

9) Product Images from "Vitamin A and E Homologues Impacting the Fate of Acrylamide in Equimolar Asparagine-Glucose Model System"

Article Title: Vitamin A and E Homologues Impacting the Fate of Acrylamide in Equimolar Asparagine-Glucose Model System

Journal: Antioxidants

doi: 10.3390/antiox10070993

Rate of acrylamide promotion for different Vitamin A and E homologues at 1 and 10 µmol. Value are the means ± SD of duplicate experiments with duplicate determinations.
Figure Legend Snippet: Rate of acrylamide promotion for different Vitamin A and E homologues at 1 and 10 µmol. Value are the means ± SD of duplicate experiments with duplicate determinations.

Techniques Used:

10) Product Images from "Effect of Acrylamide Supplementation on the Population of Vasoactive Intestinal Peptide (VIP)-Like Immunoreactive Neurons in the Porcine Small Intestine"

Article Title: Effect of Acrylamide Supplementation on the Population of Vasoactive Intestinal Peptide (VIP)-Like Immunoreactive Neurons in the Porcine Small Intestine

Journal: International Journal of Molecular Sciences

doi: 10.3390/ijms21249691

The ratio of co-localization of VIP with CART in intramural neurons in each part of the porcine small intestine (duodenum, jejunum, and ileum) in control animals (grey bars), after low (white bars) and high dose (black bars) of acrylamide supplementation ( A – C ) and the most representative images showing VIP-LI neurons simultaneously immunoreactive to CART in animals from control ( D , G , J ), LD ( E , H , K ), HD ( F , I , L ) group. ( A ) Mean (±SEM) percentage of VIP+/CART+ neurons in the myenteric plexus (MP), outer submucous plexus (OSP), and inner submucous plexus (ISP) within the porcine duodenum; ( B ) Mean (±SEM) percentage of VIP+/CART+ neurons in the myenteric plexus (MP), outer submucous plexus (OSP), and inner submucous plexus (ISP) within the porcine jejunum; ( C ) Mean (±SEM) percentage of VIP+/CART+ neurons in the myenteric plexus (MP), outer submucous plexus (OSP), and inner submucous plexus (ISP) within the porcine ileum; ( D ) VIP+/CART+ neurons in the myenteric plexus of the porcine duodenum in animals from control group; ( E ) VIP+/CART+ neurons in the myenteric plexus of the porcine duodenum in animals from LD group; ( F ) VIP+/CART+ neurons in the myenteric plexus of the porcine duodenum in animals from HD group; ( G ) VIP+/CART+ neurons in the outer submucous plexus (OSP) of the porcine jejunum in animals from control group; ( H ) VIP+/CART+ neurons in the outer submucous plexus (OSP) of the porcine jejunum in animals from LD group; ( I ) VIP+/CART+ neurons in the outer submucous plexus (OSP) of the porcine jejunum in animals from HD group; ( J ) VIP+/CART+ neurons in the inner submucous plexus (ISP) of the porcine ileum in animals from control group; ( K ) VIP+/CART+ neurons in the inner submucous plexus (ISP) of the porcine ileum in animals from LD group; ( L ) VIP+/CART+ neurons in the inner submucous plexus (ISP) of the porcine ileum in animals from HD group. All images were created by digital superimposition of two color channels (green for VIP and red for CART). Intramural neurons immunopositive to VIP and CART are indicated with arrows. Significant differences were assessed with one-way analysis of variance (ANOVA) with Dunnett’s test (* p
Figure Legend Snippet: The ratio of co-localization of VIP with CART in intramural neurons in each part of the porcine small intestine (duodenum, jejunum, and ileum) in control animals (grey bars), after low (white bars) and high dose (black bars) of acrylamide supplementation ( A – C ) and the most representative images showing VIP-LI neurons simultaneously immunoreactive to CART in animals from control ( D , G , J ), LD ( E , H , K ), HD ( F , I , L ) group. ( A ) Mean (±SEM) percentage of VIP+/CART+ neurons in the myenteric plexus (MP), outer submucous plexus (OSP), and inner submucous plexus (ISP) within the porcine duodenum; ( B ) Mean (±SEM) percentage of VIP+/CART+ neurons in the myenteric plexus (MP), outer submucous plexus (OSP), and inner submucous plexus (ISP) within the porcine jejunum; ( C ) Mean (±SEM) percentage of VIP+/CART+ neurons in the myenteric plexus (MP), outer submucous plexus (OSP), and inner submucous plexus (ISP) within the porcine ileum; ( D ) VIP+/CART+ neurons in the myenteric plexus of the porcine duodenum in animals from control group; ( E ) VIP+/CART+ neurons in the myenteric plexus of the porcine duodenum in animals from LD group; ( F ) VIP+/CART+ neurons in the myenteric plexus of the porcine duodenum in animals from HD group; ( G ) VIP+/CART+ neurons in the outer submucous plexus (OSP) of the porcine jejunum in animals from control group; ( H ) VIP+/CART+ neurons in the outer submucous plexus (OSP) of the porcine jejunum in animals from LD group; ( I ) VIP+/CART+ neurons in the outer submucous plexus (OSP) of the porcine jejunum in animals from HD group; ( J ) VIP+/CART+ neurons in the inner submucous plexus (ISP) of the porcine ileum in animals from control group; ( K ) VIP+/CART+ neurons in the inner submucous plexus (ISP) of the porcine ileum in animals from LD group; ( L ) VIP+/CART+ neurons in the inner submucous plexus (ISP) of the porcine ileum in animals from HD group. All images were created by digital superimposition of two color channels (green for VIP and red for CART). Intramural neurons immunopositive to VIP and CART are indicated with arrows. Significant differences were assessed with one-way analysis of variance (ANOVA) with Dunnett’s test (* p

Techniques Used:

The ratio of co-localization of VIP with nNOS in intramural neurons in each part of the porcine small intestine (duodenum, jejunum and ileum) in control animals (grey bars), after low (white bars) and high doses (black bars) of acrylamide supplementation ( A – C ) and the most representative images showing VIP-LI neurons simultaneously immunoreactive to nNOS in animals from control ( D , G , J ), LD ( E , H , K ) and HD ( F , I , L ) group. ( A ) Mean (±SEM) percentage of VIP+/nNOS+ neurons in the myenteric plexus (MP), outer submucous plexus (OSP), and inner submucous plexus (ISP) within the porcine duodenum; ( B ) Mean (±SEM) percentage of VIP+/nNOS+ neurons in the myenteric plexus (MP), outer submucous plexus (OSP), and inner submucous plexus (ISP) within the porcine jejunum; ( C ) Mean (±SEM) percentage of VIP+/nNOS+ neurons in the myenteric plexus (MP), outer submucous plexus (OSP), and inner submucous plexus (ISP) within the porcine ileum; ( D ) VIP+/nNOS+ neurons in the myenteric plexus of the porcine ileum in animals from control group; ( E ) VIP+/nNOS+ neurons in the myenteric plexus (MP) of the porcine ileum in animals from LD group; ( F ) VIP+/nNOS+ neurons in the myenteric plexus (MP) of the porcine ileum in animals from HD group; ( G ) VIP+/nNOS+ neurons in the outer submucous plexus (OSP) of the porcine jejunum in animals from control group; ( H ) VIP+/nNOS+ neurons in the outer submucous plexus (OSP) of the porcine jejunum in animals from LD group; ( I ) VIP+/nNOS+ neurons in the outer submucous plexus (OSP) of the porcine jejunum in animals from HD group; ( J ) VIP+/nNOS+ neurons in the inner submucous plexus (ISP) of the porcine jejunum in animals from control group; ( K ) VIP+/nNOS+ neurons in the inner submucous plexus (ISP) of the porcine jejunum in animals from LD group; ( L ) VIP+/nNOS+ neurons in the inner submucous plexus (ISP) of the porcine jejunum in animals from control group. All images were created by digital superimposition of two color channels (green for VIP and red for nNOS). Intramural neurons immunopositive to VIP and nNOS are indicated with arrows. Significant differences were assessed with one-way analysis of variance (ANOVA) with Dunnett’s test (* p
Figure Legend Snippet: The ratio of co-localization of VIP with nNOS in intramural neurons in each part of the porcine small intestine (duodenum, jejunum and ileum) in control animals (grey bars), after low (white bars) and high doses (black bars) of acrylamide supplementation ( A – C ) and the most representative images showing VIP-LI neurons simultaneously immunoreactive to nNOS in animals from control ( D , G , J ), LD ( E , H , K ) and HD ( F , I , L ) group. ( A ) Mean (±SEM) percentage of VIP+/nNOS+ neurons in the myenteric plexus (MP), outer submucous plexus (OSP), and inner submucous plexus (ISP) within the porcine duodenum; ( B ) Mean (±SEM) percentage of VIP+/nNOS+ neurons in the myenteric plexus (MP), outer submucous plexus (OSP), and inner submucous plexus (ISP) within the porcine jejunum; ( C ) Mean (±SEM) percentage of VIP+/nNOS+ neurons in the myenteric plexus (MP), outer submucous plexus (OSP), and inner submucous plexus (ISP) within the porcine ileum; ( D ) VIP+/nNOS+ neurons in the myenteric plexus of the porcine ileum in animals from control group; ( E ) VIP+/nNOS+ neurons in the myenteric plexus (MP) of the porcine ileum in animals from LD group; ( F ) VIP+/nNOS+ neurons in the myenteric plexus (MP) of the porcine ileum in animals from HD group; ( G ) VIP+/nNOS+ neurons in the outer submucous plexus (OSP) of the porcine jejunum in animals from control group; ( H ) VIP+/nNOS+ neurons in the outer submucous plexus (OSP) of the porcine jejunum in animals from LD group; ( I ) VIP+/nNOS+ neurons in the outer submucous plexus (OSP) of the porcine jejunum in animals from HD group; ( J ) VIP+/nNOS+ neurons in the inner submucous plexus (ISP) of the porcine jejunum in animals from control group; ( K ) VIP+/nNOS+ neurons in the inner submucous plexus (ISP) of the porcine jejunum in animals from LD group; ( L ) VIP+/nNOS+ neurons in the inner submucous plexus (ISP) of the porcine jejunum in animals from control group. All images were created by digital superimposition of two color channels (green for VIP and red for nNOS). Intramural neurons immunopositive to VIP and nNOS are indicated with arrows. Significant differences were assessed with one-way analysis of variance (ANOVA) with Dunnett’s test (* p

Techniques Used:

The ratio of co-localization of VIP with SP in intramural neurons in each part of the porcine small intestine (duodenum, jejunum, and ileum) in control animals (grey bars), after low (white bars) and high doses (black bars) of acrylamide supplementation ( A – C ) and the most representative images showing VIP-LI neurons simultaneously immunoreactive to substance P (SP) in animals from control ( D , G , J ), LD ( E , H , K ), HD ( F , I , L ) group. ( A ) Mean (±SEM) percentage of VIP+/SP+ neurons in the myenteric plexus (MP), outer submucous plexus (OSP), and inner submucous plexus (ISP) within the porcine duodenum; ( B ) Mean (±SEM) percentage of VIP+/SP+ neurons in the myenteric plexus (MP), outer submucous plexus (OSP), and inner submucous plexus (ISP) within the porcine jejunum; ( C ) Mean (±SEM) percentage of VIP+/SP+ neurons in the myenteric plexus (MP), outer submucous plexus (OSP), and inner submucous plexus (ISP) within the porcine ileum; ( D ) VIP+/SP+ neurons in the myenteric plexus of the porcine jejunum in animals from control group; ( E ) VIP+/SP+ neurons in the myenteric plexus of the porcine jejunum in animals from LD group; ( F ) VIP+/SP+ neurons in the myenteric plexus of the porcine jejunum in animals from HD group; ( G ) VIP+/SP+ neurons in the outer submucous plexus (OSP) of the porcine duodenum in animals from control group; ( H ) VIP+/SP+ neurons in the outer submucous plexus (OSP) of the porcine duodenum in animals from LD group; ( I ) VIP+/SP+ neurons in the outer submucous plexus (OSP) of the porcine duodenum in animals from HD group; ( J ) VIP+/SP+ neurons in the inner submucous plexus (ISP) of the porcine duodenum in animals from control group; ( K ) VIP+/SP+ neurons in the inner submucous plexus (ISP) of the porcine duodenum in animals from LD group; ( L ) VIP+/SP+ neurons in the inner submucous plexus (ISP) of the porcine duodenum in animals from HD group. All images were created by digital superimposition of two color channels (green for VIP and red for SP). Intramural neurons immunopositive to VIP and SP are indicated with arrows. Significant differences were assessed with one-way analysis of variance (ANOVA) with Dunnett’s test (* p
Figure Legend Snippet: The ratio of co-localization of VIP with SP in intramural neurons in each part of the porcine small intestine (duodenum, jejunum, and ileum) in control animals (grey bars), after low (white bars) and high doses (black bars) of acrylamide supplementation ( A – C ) and the most representative images showing VIP-LI neurons simultaneously immunoreactive to substance P (SP) in animals from control ( D , G , J ), LD ( E , H , K ), HD ( F , I , L ) group. ( A ) Mean (±SEM) percentage of VIP+/SP+ neurons in the myenteric plexus (MP), outer submucous plexus (OSP), and inner submucous plexus (ISP) within the porcine duodenum; ( B ) Mean (±SEM) percentage of VIP+/SP+ neurons in the myenteric plexus (MP), outer submucous plexus (OSP), and inner submucous plexus (ISP) within the porcine jejunum; ( C ) Mean (±SEM) percentage of VIP+/SP+ neurons in the myenteric plexus (MP), outer submucous plexus (OSP), and inner submucous plexus (ISP) within the porcine ileum; ( D ) VIP+/SP+ neurons in the myenteric plexus of the porcine jejunum in animals from control group; ( E ) VIP+/SP+ neurons in the myenteric plexus of the porcine jejunum in animals from LD group; ( F ) VIP+/SP+ neurons in the myenteric plexus of the porcine jejunum in animals from HD group; ( G ) VIP+/SP+ neurons in the outer submucous plexus (OSP) of the porcine duodenum in animals from control group; ( H ) VIP+/SP+ neurons in the outer submucous plexus (OSP) of the porcine duodenum in animals from LD group; ( I ) VIP+/SP+ neurons in the outer submucous plexus (OSP) of the porcine duodenum in animals from HD group; ( J ) VIP+/SP+ neurons in the inner submucous plexus (ISP) of the porcine duodenum in animals from control group; ( K ) VIP+/SP+ neurons in the inner submucous plexus (ISP) of the porcine duodenum in animals from LD group; ( L ) VIP+/SP+ neurons in the inner submucous plexus (ISP) of the porcine duodenum in animals from HD group. All images were created by digital superimposition of two color channels (green for VIP and red for SP). Intramural neurons immunopositive to VIP and SP are indicated with arrows. Significant differences were assessed with one-way analysis of variance (ANOVA) with Dunnett’s test (* p

Techniques Used:

11) Product Images from "Capture of circulating tumor cells using photoacoustic flowmetry and two phase flow"

Article Title: Capture of circulating tumor cells using photoacoustic flowmetry and two phase flow

Journal: Journal of Biomedical Optics

doi: 10.1117/1.JBO.17.6.061221

The flow chamber for the photoacoustic flowmeter consists of a flow path in an acrylamide mold that allows cell suspensions to be irradiated by laser pulses. Subsequent photoacoustic waves are sensed by a transducer element. Here, water droplets are dyed
Figure Legend Snippet: The flow chamber for the photoacoustic flowmeter consists of a flow path in an acrylamide mold that allows cell suspensions to be irradiated by laser pulses. Subsequent photoacoustic waves are sensed by a transducer element. Here, water droplets are dyed

Techniques Used: Flow Cytometry, Irradiation

12) Product Images from "Minocycline protects against acrylamide-induced neurotoxicity and testicular damage in Sprague-Dawley rats"

Article Title: Minocycline protects against acrylamide-induced neurotoxicity and testicular damage in Sprague-Dawley rats

Journal: Journal of Toxicologic Pathology

doi: 10.1293/tox.2019-0066

Representative micrographs of the testes from vehicle-, acrylamide (ACR)-, and ACR+minocycline (MIN)-treated rats. A) Seminiferous tubules from vehicle-treated rats showing normal spermatogenic cell layers including fibroblasts (1), Sertoli cells (2), spermatogonia (3), spermatocytes (4), spermatids (5), spermatozoa (6) (stages I–VIII), and normal Leydig cells (arrows). B) Seminiferous tubules from ACR-treated rats showing depletion of seminiferous tubular cells (asterisks) and formation of spermatid giant cells (arrows) in the lumen (stages I–VI). Damaged Leydig cells (thin arrows). C) Seminiferous tubules from ACR+MIN-treated rats showing restored seminiferous tubular epithelium including myofibroblasts (1), Sertoli cells (2), spermatogonia (3), spermatocytes (4), and spermatids (5) (stages I–VIII).
Figure Legend Snippet: Representative micrographs of the testes from vehicle-, acrylamide (ACR)-, and ACR+minocycline (MIN)-treated rats. A) Seminiferous tubules from vehicle-treated rats showing normal spermatogenic cell layers including fibroblasts (1), Sertoli cells (2), spermatogonia (3), spermatocytes (4), spermatids (5), spermatozoa (6) (stages I–VIII), and normal Leydig cells (arrows). B) Seminiferous tubules from ACR-treated rats showing depletion of seminiferous tubular cells (asterisks) and formation of spermatid giant cells (arrows) in the lumen (stages I–VI). Damaged Leydig cells (thin arrows). C) Seminiferous tubules from ACR+MIN-treated rats showing restored seminiferous tubular epithelium including myofibroblasts (1), Sertoli cells (2), spermatogonia (3), spermatocytes (4), and spermatids (5) (stages I–VIII).

Techniques Used:

Representative ultrastructural micrographs of normal, acrylamide (ACR)-treated, and ACR-minocycline (MIN) treated rats. A) Normal seminiferous tubular epithelium showing a normal Sertoli cell resting on the basement membrane (asterisk), spermatogonia (thin arrow), and spermatocytes (thick arrows) showing a regular nuclear membrane with dispersed chromatin in the nucleus. The basement membrane is indicated by arrowheads. B) ACR-treated rats with cytoplasmic vacuolation (small asterisk) and presence of electron-dense bodies in spermatogonia (thin arrows). Spermatocytes showing an irregular nuclear membrane and mitochondrial swelling (thick arrows). The basement membrane is indicated by arrowheads. C) Treatment of ACR-exposed rats with MIN decreased the intensity of ultrastructural changes. The basement membrane is indicated by arrowheads, Sertoli cells by asterisks, spermatogonia by thick arrows, and spermatocytes by thick arrows.
Figure Legend Snippet: Representative ultrastructural micrographs of normal, acrylamide (ACR)-treated, and ACR-minocycline (MIN) treated rats. A) Normal seminiferous tubular epithelium showing a normal Sertoli cell resting on the basement membrane (asterisk), spermatogonia (thin arrow), and spermatocytes (thick arrows) showing a regular nuclear membrane with dispersed chromatin in the nucleus. The basement membrane is indicated by arrowheads. B) ACR-treated rats with cytoplasmic vacuolation (small asterisk) and presence of electron-dense bodies in spermatogonia (thin arrows). Spermatocytes showing an irregular nuclear membrane and mitochondrial swelling (thick arrows). The basement membrane is indicated by arrowheads. C) Treatment of ACR-exposed rats with MIN decreased the intensity of ultrastructural changes. The basement membrane is indicated by arrowheads, Sertoli cells by asterisks, spermatogonia by thick arrows, and spermatocytes by thick arrows.

Techniques Used:

Representative micrographs of the cerebellum from vehicle-, acrylamide (ACR)-, and ACR+minocycline (MIN)-treated rats. A) A normal cerebellum showing normal architecture with distinct cortical layers: outer molecular (MC) layer, inner granular (GC) layer, and in between the single-cell layer of Purkinje cells. B) A cerebellum from ACR-treated rats showing degenerated Purkinje cells (arrows). C) A cerebellum from ACR+MIN-treated rats showing more or less normal Purkinje cells (arrows).
Figure Legend Snippet: Representative micrographs of the cerebellum from vehicle-, acrylamide (ACR)-, and ACR+minocycline (MIN)-treated rats. A) A normal cerebellum showing normal architecture with distinct cortical layers: outer molecular (MC) layer, inner granular (GC) layer, and in between the single-cell layer of Purkinje cells. B) A cerebellum from ACR-treated rats showing degenerated Purkinje cells (arrows). C) A cerebellum from ACR+MIN-treated rats showing more or less normal Purkinje cells (arrows).

Techniques Used:

Representative micrographs of the hippocampus from vehicle-, acrylamide (ACR)-, and ACR+minocycline (MIN)-treated rats. A) A normal CA1 subdivision of the hippocampus showing intact small pyramidal neurons with vesicular nuclei (arrows). B) A CA1 subdivision of the hippocampus from ACR-treated rats showing degenerated pyramidal neurons (arrows). Degenerated neurons appear shrunken with pyknotic nuclei. C) A CA1 subdivision of the hippocampus from ACR+MIN-treated rats revealing the presence of very few degenerated pyramidal neurons (arrow).
Figure Legend Snippet: Representative micrographs of the hippocampus from vehicle-, acrylamide (ACR)-, and ACR+minocycline (MIN)-treated rats. A) A normal CA1 subdivision of the hippocampus showing intact small pyramidal neurons with vesicular nuclei (arrows). B) A CA1 subdivision of the hippocampus from ACR-treated rats showing degenerated pyramidal neurons (arrows). Degenerated neurons appear shrunken with pyknotic nuclei. C) A CA1 subdivision of the hippocampus from ACR+MIN-treated rats revealing the presence of very few degenerated pyramidal neurons (arrow).

Techniques Used:

Malondialdehyde (MDA) measurement in the brains and testes of vehicle-, acrylamide (ACR)-, ACR+minocycline (MIN)-, ACR+saline-, and MIN-treated rats. MDA concentrations are expressed as means ± standard error of the mean (SEM) (nmol/g tissue) (*p
Figure Legend Snippet: Malondialdehyde (MDA) measurement in the brains and testes of vehicle-, acrylamide (ACR)-, ACR+minocycline (MIN)-, ACR+saline-, and MIN-treated rats. MDA concentrations are expressed as means ± standard error of the mean (SEM) (nmol/g tissue) (*p

Techniques Used: Multiple Displacement Amplification

13) Product Images from "Protective effect of l-carnitine against acrylamide-induced DNA damage in somatic and germ cells of mice"

Article Title: Protective effect of l-carnitine against acrylamide-induced DNA damage in somatic and germ cells of mice

Journal: Saudi Journal of Biological Sciences

doi: 10.1016/j.sjbs.2010.07.004

Metaphases from mouse bone marrow cells treated with acrylamide showing: (A) normal, (B) break, (C) fragment, (D) gap, (E) deletion and gap, (F) polyploidy.
Figure Legend Snippet: Metaphases from mouse bone marrow cells treated with acrylamide showing: (A) normal, (B) break, (C) fragment, (D) gap, (E) deletion and gap, (F) polyploidy.

Techniques Used:

Microphotograph shows polychromatic erythrocyte with Micronuclei(black arrow) from mouse bone marrow cells treated with acrylamide.
Figure Legend Snippet: Microphotograph shows polychromatic erythrocyte with Micronuclei(black arrow) from mouse bone marrow cells treated with acrylamide.

Techniques Used:

Sperm abnormalities induced in male mice orally treated with acrylamide showing: (A) normal, (B) amorphous, (C) triangular, (D) without hook, (E) banana (F) big head, (G) small head and (H) coiled tail.
Figure Legend Snippet: Sperm abnormalities induced in male mice orally treated with acrylamide showing: (A) normal, (B) amorphous, (C) triangular, (D) without hook, (E) banana (F) big head, (G) small head and (H) coiled tail.

Techniques Used: Mouse Assay

14) Product Images from "The effects of anthracycline drugs on the conformational distribution of mouse P-glycoprotein explains their transport rate differences"

Article Title: The effects of anthracycline drugs on the conformational distribution of mouse P-glycoprotein explains their transport rate differences

Journal: Biochemical pharmacology

doi: 10.1016/j.bcp.2020.113813

Acrylamide quenching of Pgp in the presence of DNR and DOX. (A) Acrylamide quenching of 67 μM Phe and 36 μM Tyr (Phe+Tyr) (a), 11 μM NATA (NATA) (b), and a combination of (a) and (b), or NATA+Phe+Tyr (c) in the absence (closed columns) and presence of 530 mM acrylamide (open columns). The relative fluorescence units (RFUs) are shown on the y-axis. (B) The Stern-Volmer plot of NATA+Phe+Tyr (open circles), Pgp in the absence of ligands (apoPgp, open diamonds), Pgp with 3.2 mM AMPPNP (AMPPNP, open triangles) with a range of acrylamide concentrations. Stern-Volmer plots of Pgp in the presence of 16 μM (open circles) and 500 μM (open squares) for (C) DNR and (D) DOX. The data points represent the average of at least three experiments, and the error bars are the standard deviation. The Stern-Volmer curves for apoPgp and AMPPNP are shown as gray and black dashed lines, respectively, for comparison.
Figure Legend Snippet: Acrylamide quenching of Pgp in the presence of DNR and DOX. (A) Acrylamide quenching of 67 μM Phe and 36 μM Tyr (Phe+Tyr) (a), 11 μM NATA (NATA) (b), and a combination of (a) and (b), or NATA+Phe+Tyr (c) in the absence (closed columns) and presence of 530 mM acrylamide (open columns). The relative fluorescence units (RFUs) are shown on the y-axis. (B) The Stern-Volmer plot of NATA+Phe+Tyr (open circles), Pgp in the absence of ligands (apoPgp, open diamonds), Pgp with 3.2 mM AMPPNP (AMPPNP, open triangles) with a range of acrylamide concentrations. Stern-Volmer plots of Pgp in the presence of 16 μM (open circles) and 500 μM (open squares) for (C) DNR and (D) DOX. The data points represent the average of at least three experiments, and the error bars are the standard deviation. The Stern-Volmer curves for apoPgp and AMPPNP are shown as gray and black dashed lines, respectively, for comparison.

Techniques Used: Fluorescence, Standard Deviation

15) Product Images from "Probing Conformational Stability and Dynamics of Erythroid and Nonerythroid Spectrin: Effects of Urea and Guanidine Hydrochloride"

Article Title: Probing Conformational Stability and Dynamics of Erythroid and Nonerythroid Spectrin: Effects of Urea and Guanidine Hydrochloride

Journal: PLoS ONE

doi: 10.1371/journal.pone.0116991

Acrylamide quenching of spectrin tryptophans showing plots of Stern Volmer constant (K SV ) versus denaturant concentrations for (A) erythroid spectrin and (B) nonerythroid spectrin. Changes in bimolecular quenching rate constants (k q ) versus denaturant concentrations are shown in (C) for erythroid and (D) for nonerythroid spectrin.
Figure Legend Snippet: Acrylamide quenching of spectrin tryptophans showing plots of Stern Volmer constant (K SV ) versus denaturant concentrations for (A) erythroid spectrin and (B) nonerythroid spectrin. Changes in bimolecular quenching rate constants (k q ) versus denaturant concentrations are shown in (C) for erythroid and (D) for nonerythroid spectrin.

Techniques Used:

16) Product Images from "Contrasting Roles of Endosomal pH and the Cytoskeleton in Infection of Human Glial Cells by JC Virus and Simian Virus 40"

Article Title: Contrasting Roles of Endosomal pH and the Cytoskeleton in Infection of Human Glial Cells by JC Virus and Simian Virus 40

Journal: Journal of Virology

doi: 10.1128/JVI.77.2.1347-1356.2003

Intermediate filaments are required for infection by JCV but not by SV40. (A) Untreated SVG-A cells or SVG-A cells treated with 10 mM acrylamide for 6 h at 37°C were stained with antivimentin antibody to detect the disassembly of intermediate filaments. Bar, 40 μm. (B 1 and 4) Uninfected SVG-A cells. (B 2 and 5) SVG-A cells were incubated with JCV or SV40 for 4 h at 37°C, washed, and incubated with medium containing neutralizing JCV or SV40 antiserum. Cells were fixed at 72 h postinfection and stained for V antigen. (B 3 and 6) SVG-A cells were treated for 6 h at 37°C with 10 mM acrylamide, infected with JCV or SV40, fixed, and stained for V antigen. Bar, 200 μm. (C 1) Uninfected CV1 cells. (C 2) Untreated CV1 cells infected with SV40. (C 3) CV1 cells treated for 6 h with 10 mM acrylamide, infected with SV40, fixed, and stained for V antigen. Numbers at the bottom right of each panel refer to the percentage of infected cells per field and represent the mean of at least four different fields of cells from each of three independent experiments.
Figure Legend Snippet: Intermediate filaments are required for infection by JCV but not by SV40. (A) Untreated SVG-A cells or SVG-A cells treated with 10 mM acrylamide for 6 h at 37°C were stained with antivimentin antibody to detect the disassembly of intermediate filaments. Bar, 40 μm. (B 1 and 4) Uninfected SVG-A cells. (B 2 and 5) SVG-A cells were incubated with JCV or SV40 for 4 h at 37°C, washed, and incubated with medium containing neutralizing JCV or SV40 antiserum. Cells were fixed at 72 h postinfection and stained for V antigen. (B 3 and 6) SVG-A cells were treated for 6 h at 37°C with 10 mM acrylamide, infected with JCV or SV40, fixed, and stained for V antigen. Bar, 200 μm. (C 1) Uninfected CV1 cells. (C 2) Untreated CV1 cells infected with SV40. (C 3) CV1 cells treated for 6 h with 10 mM acrylamide, infected with SV40, fixed, and stained for V antigen. Numbers at the bottom right of each panel refer to the percentage of infected cells per field and represent the mean of at least four different fields of cells from each of three independent experiments.

Techniques Used: Infection, Staining, Incubation

17) Product Images from "YscO of Yersinia pestis Is a Mobile Core Component of the Yop Secretion System"

Article Title: YscO of Yersinia pestis Is a Mobile Core Component of the Yop Secretion System

Journal: Journal of Bacteriology

doi:

Secretion profile of Δ yscO Y. pestis grown in the presence or absence of Ca 2+ . Shown is an immunoblot analysis of proteins expressed and secreted from Y. pestis KIM5-3001 (wt); KIM5-3001.16, the yscO mutant (Δ yscO ); and the mutant carrying pYscO.2 or pYscOP.2 in trans (Δ yscO/O and Δ yscO/OP ). Bacteria were grown in TMH with (+) or without (−) Ca 2+ , and proteins from bacterial fractions were separated by SDS-PAGE (A, B, and D, 12% [wt/vol] acrylamide; C, 15% [wt/vol] acrylamide). Proteins from soluble (s), membrane (m), whole-cell (c), and culture medium (e) fractions were visualized with polyclonal antibodies specific to YopE, YopM, V antigen, and YscP and with antibody raised to a mixture of extracellular Yersinia proteins (ECP). The secondary antibody used was conjugated to alkaline phosphatase. Arrows denote the positions of proteins. (A) YopE was visualized with mouse anti-YopE (YopE and its Pla-generated degradation products are enclosed in brackets). (B) YopE was visualized with rabbit anti-YopE. (C) The complexity of the protein pattern reflects degradation products from multiple Yops due to the Pla protease. (D) YscP was visualized with antibody to a GST-YscP fusion protein. Molecular masses (in kilodaltons) of prestained molecular mass standards (Bio-Rad) are denoted to the right in panels A and C.
Figure Legend Snippet: Secretion profile of Δ yscO Y. pestis grown in the presence or absence of Ca 2+ . Shown is an immunoblot analysis of proteins expressed and secreted from Y. pestis KIM5-3001 (wt); KIM5-3001.16, the yscO mutant (Δ yscO ); and the mutant carrying pYscO.2 or pYscOP.2 in trans (Δ yscO/O and Δ yscO/OP ). Bacteria were grown in TMH with (+) or without (−) Ca 2+ , and proteins from bacterial fractions were separated by SDS-PAGE (A, B, and D, 12% [wt/vol] acrylamide; C, 15% [wt/vol] acrylamide). Proteins from soluble (s), membrane (m), whole-cell (c), and culture medium (e) fractions were visualized with polyclonal antibodies specific to YopE, YopM, V antigen, and YscP and with antibody raised to a mixture of extracellular Yersinia proteins (ECP). The secondary antibody used was conjugated to alkaline phosphatase. Arrows denote the positions of proteins. (A) YopE was visualized with mouse anti-YopE (YopE and its Pla-generated degradation products are enclosed in brackets). (B) YopE was visualized with rabbit anti-YopE. (C) The complexity of the protein pattern reflects degradation products from multiple Yops due to the Pla protease. (D) YscP was visualized with antibody to a GST-YscP fusion protein. Molecular masses (in kilodaltons) of prestained molecular mass standards (Bio-Rad) are denoted to the right in panels A and C.

Techniques Used: Mutagenesis, SDS Page, Proximity Ligation Assay, Generated

18) Product Images from "An ultrafast insulin formulation enabled by high-throughput screening of engineered polymeric excipients"

Article Title: An ultrafast insulin formulation enabled by high-throughput screening of engineered polymeric excipients

Journal: Science translational medicine

doi: 10.1126/scitranslmed.aba6676

Scheme of polymer excipient library design. A library of statistical acrylamide copolymers with a target degree of polymerization (DP) of 50 was synthesized through controlled copolymerization using RAFT. Copolymer combinations consist of one carrier monomer: 4-acryloylmorpholine (MORPH), N -(3-methoxypropyl)acrylamide (MPAM), N,N -dimethylacrylamide (DMA), N -hydroxyethyl acrylamide (HEAM), or acrylamide (AM). Each copolymer also contains one dopant monomer: N -[tris(hydroxymethyl)-methyl]acrylamide (TRI), 2-acrylamido-2-methylpropane sulfonic acid (AMP), (3-acrylamidopropyl)trimethylammonium chloride (TMA), N -isopropylacrylamide (NIP), N - tert -butylacrylamide (TBA), or N -phenylacrylamide (PHE). Each carrier-dopant combination was repeated at low, medium, and high dopant loadings: NIP at 6.7, 13.3, and 20 wt.%; TRI at 5, 10, and 15 wt.%; and AMP, TMA, TBA, and PHE at 3.3, 6.7, and 10 wt.%.
Figure Legend Snippet: Scheme of polymer excipient library design. A library of statistical acrylamide copolymers with a target degree of polymerization (DP) of 50 was synthesized through controlled copolymerization using RAFT. Copolymer combinations consist of one carrier monomer: 4-acryloylmorpholine (MORPH), N -(3-methoxypropyl)acrylamide (MPAM), N,N -dimethylacrylamide (DMA), N -hydroxyethyl acrylamide (HEAM), or acrylamide (AM). Each copolymer also contains one dopant monomer: N -[tris(hydroxymethyl)-methyl]acrylamide (TRI), 2-acrylamido-2-methylpropane sulfonic acid (AMP), (3-acrylamidopropyl)trimethylammonium chloride (TMA), N -isopropylacrylamide (NIP), N - tert -butylacrylamide (TBA), or N -phenylacrylamide (PHE). Each carrier-dopant combination was repeated at low, medium, and high dopant loadings: NIP at 6.7, 13.3, and 20 wt.%; TRI at 5, 10, and 15 wt.%; and AMP, TMA, TBA, and PHE at 3.3, 6.7, and 10 wt.%.

Techniques Used: Synthesized

19) Product Images from "Programmable ROS‐Mediated Cancer Therapy via Magneto‐Inductions, Programmable ROS‐Mediated Cancer Therapy via Magneto‐Inductions"

Article Title: Programmable ROS‐Mediated Cancer Therapy via Magneto‐Inductions, Programmable ROS‐Mediated Cancer Therapy via Magneto‐Inductions

Journal: Advanced Science

doi: 10.1002/advs.201902933

Characterization of the IONs’ physical properties. A) Elemental mapping analysis showing the composition and element distribution of IONs. B) Magnetic properties represent by M–H curves of IONs and RGD‐IONs (temperature: 298 K). C) Infrared thermal images with letter‐shaped acrylamide gel coating RGD‐IONs under AMF with frequency of 375 kHz for 20 min. D) Temperature raised curves of RGD‐IONs with different iron concentrations dispersed in water under AMF with frequency of 375 kHz for 20 min recorded by IR thermometer. E) Optical images showing the assembly of RGD‐IONs and rotation under RMF with strength of 40 mT and frequency of 0.1 Hz (the scare bar: 40 µm).
Figure Legend Snippet: Characterization of the IONs’ physical properties. A) Elemental mapping analysis showing the composition and element distribution of IONs. B) Magnetic properties represent by M–H curves of IONs and RGD‐IONs (temperature: 298 K). C) Infrared thermal images with letter‐shaped acrylamide gel coating RGD‐IONs under AMF with frequency of 375 kHz for 20 min. D) Temperature raised curves of RGD‐IONs with different iron concentrations dispersed in water under AMF with frequency of 375 kHz for 20 min recorded by IR thermometer. E) Optical images showing the assembly of RGD‐IONs and rotation under RMF with strength of 40 mT and frequency of 0.1 Hz (the scare bar: 40 µm).

Techniques Used: Acrylamide Gel Assay

20) Product Images from "In situ formation of DNA-templated copper nanoparticles as fluorescent indicator for hydroxylamine detection †"

Article Title: In situ formation of DNA-templated copper nanoparticles as fluorescent indicator for hydroxylamine detection †

Journal: RSC Advances

doi: 10.1039/c9ra04476k

(A) Fluorescence spectra of the proposed method in the increasing concentrations of HA (from bottom: 0, 0.1, 0.2, 0.4, 0.5, 0.8, 1.2, 1.5, 1.8, and 2.0 mM, respectively). The inset shows calibration curve of the assay system for HA sensing. (B) Selectivity of the fluorescent method plotted in a histogram form (from left: blank, HA, ethylenediamine, aniline, sulfanilamide, acrylamide, and glutamic acid). HA is at a concentration of 2 mM. The others are at a concentration of 10 mM, respectively. The error bars represent the standard deviation of three independent measurements.
Figure Legend Snippet: (A) Fluorescence spectra of the proposed method in the increasing concentrations of HA (from bottom: 0, 0.1, 0.2, 0.4, 0.5, 0.8, 1.2, 1.5, 1.8, and 2.0 mM, respectively). The inset shows calibration curve of the assay system for HA sensing. (B) Selectivity of the fluorescent method plotted in a histogram form (from left: blank, HA, ethylenediamine, aniline, sulfanilamide, acrylamide, and glutamic acid). HA is at a concentration of 2 mM. The others are at a concentration of 10 mM, respectively. The error bars represent the standard deviation of three independent measurements.

Techniques Used: Fluorescence, Concentration Assay, Standard Deviation

21) Product Images from "Comparison of neurons derived from mouse P19, rat PC12 and human SH-SY5Y cells in the assessment of chemical- and toxin-induced neurotoxicity"

Article Title: Comparison of neurons derived from mouse P19, rat PC12 and human SH-SY5Y cells in the assessment of chemical- and toxin-induced neurotoxicity

Journal: BMC Pharmacology & Toxicology

doi: 10.1186/s40360-017-0151-8

Concentration-dependent effects of MeHg, okadaic acid and acrylamide on cell viability and expression of the neuron-specific protein βIII-tubulin in neuronally differentiated P19, PC12 and SH-SY5Y cells. The cells were plated at a density of 500 cells/mm 2 and cultured for 6 days in the differentiation media, followed by exposure to the test compounds for 48 h. Effects of MeHg ( a , b ), okadaic acid ( c , d ) and acrylamide ( e , f ) on the cell viability were assessed by using the calcein-AM assay ( a , c , e ), and the immunofluorescence of βIII-tubulin ( b , d , f ). The data are means ± SEM of n = 6 independent experiments ( n = 3 for okadaic acid in the βIII-tubulin assay; panel d ). The results are expressed as percentage of non-treated cells or cells treated with 0.1% DMSO (used as vehicle). Wells treated with 2% Triton X-100 for 30 min served as controls for maximal cell death. Statistical analysis was performed using repeated measures one-way ANOVA with post hoc Dunnett’s multiple comparisons test (* p
Figure Legend Snippet: Concentration-dependent effects of MeHg, okadaic acid and acrylamide on cell viability and expression of the neuron-specific protein βIII-tubulin in neuronally differentiated P19, PC12 and SH-SY5Y cells. The cells were plated at a density of 500 cells/mm 2 and cultured for 6 days in the differentiation media, followed by exposure to the test compounds for 48 h. Effects of MeHg ( a , b ), okadaic acid ( c , d ) and acrylamide ( e , f ) on the cell viability were assessed by using the calcein-AM assay ( a , c , e ), and the immunofluorescence of βIII-tubulin ( b , d , f ). The data are means ± SEM of n = 6 independent experiments ( n = 3 for okadaic acid in the βIII-tubulin assay; panel d ). The results are expressed as percentage of non-treated cells or cells treated with 0.1% DMSO (used as vehicle). Wells treated with 2% Triton X-100 for 30 min served as controls for maximal cell death. Statistical analysis was performed using repeated measures one-way ANOVA with post hoc Dunnett’s multiple comparisons test (* p

Techniques Used: Concentration Assay, Expressing, Cell Culture, Calcein AM Assay, Immunofluorescence

Representative fluorescence microscopy images of neuronally differentiated P19, PC12 and SH-SY5Y cells exposed to 1 μM methylmercury, 10 nM okadaic acid and 1 mM acrylamide. The cells were plated at a density of 500 cells/mm 2 and cultured for 6 days in the differentiation media, followed by exposure to the test compounds for 48 h. The cells were immunolabeled against the neuron-specific protein βIII-tubulin and the fluorescence microscopy images were obtained at 20 × magnification
Figure Legend Snippet: Representative fluorescence microscopy images of neuronally differentiated P19, PC12 and SH-SY5Y cells exposed to 1 μM methylmercury, 10 nM okadaic acid and 1 mM acrylamide. The cells were plated at a density of 500 cells/mm 2 and cultured for 6 days in the differentiation media, followed by exposure to the test compounds for 48 h. The cells were immunolabeled against the neuron-specific protein βIII-tubulin and the fluorescence microscopy images were obtained at 20 × magnification

Techniques Used: Fluorescence, Microscopy, Cell Culture, Immunolabeling

22) Product Images from "Synthesis, Characterization, and CO2/N2 Separation Performance of POEM-g-PAcAm Comb Copolymer Membranes"

Article Title: Synthesis, Characterization, and CO2/N2 Separation Performance of POEM-g-PAcAm Comb Copolymer Membranes

Journal: Polymers

doi: 10.3390/polym13020177

( a ) FTIR spectra of acrylamide, POEM, PPOEM, PAcAM, and POEM- g -PAcAm comb copolymers with different compositions; ( b ) 1 H NMR spectra of POEM- g -PAcAm comb copolymers with different compositions.
Figure Legend Snippet: ( a ) FTIR spectra of acrylamide, POEM, PPOEM, PAcAM, and POEM- g -PAcAm comb copolymers with different compositions; ( b ) 1 H NMR spectra of POEM- g -PAcAm comb copolymers with different compositions.

Techniques Used: Nuclear Magnetic Resonance

23) Product Images from "Acrylamide induces HepG2 cell proliferation through upregulation of miR-21 expression"

Article Title: Acrylamide induces HepG2 cell proliferation through upregulation of miR-21 expression

Journal: Journal of Biomedical Research

doi: 10.7555/JBR.31.20170016

Acrylamide downregulated the expression of PTEN and upregulated the expression of p-AKT in HepG2 cells. A and B: The expression of PTEN, p-AKT, cyclin1, EGFR and CYP2E1 after treatment with acrylamide (0 ¦̭ol/L, 50 ¦̭ol/L, 100 ¦̭ol/L, 500 ¦̭ol/L) for 24 hours. C: The expression of cyclin D1, p-AKTafter treatment with acrylamide (100 ¦̭ol/L), LY294002 (20 ¦̭ol/L), and the combination. A, B and C, as tested by Western blotting. D and E: The surviving fraction and apoptosis rate of HepG2 cells after treatment with acrylamide (100 ¦̭ol/L), LY294002 (20 ¦̭ol/L), and the combination, as measured by MTT assay and flow cytometry, respectively. *P
Figure Legend Snippet: Acrylamide downregulated the expression of PTEN and upregulated the expression of p-AKT in HepG2 cells. A and B: The expression of PTEN, p-AKT, cyclin1, EGFR and CYP2E1 after treatment with acrylamide (0 ¦̭ol/L, 50 ¦̭ol/L, 100 ¦̭ol/L, 500 ¦̭ol/L) for 24 hours. C: The expression of cyclin D1, p-AKTafter treatment with acrylamide (100 ¦̭ol/L), LY294002 (20 ¦̭ol/L), and the combination. A, B and C, as tested by Western blotting. D and E: The surviving fraction and apoptosis rate of HepG2 cells after treatment with acrylamide (100 ¦̭ol/L), LY294002 (20 ¦̭ol/L), and the combination, as measured by MTT assay and flow cytometry, respectively. *P

Techniques Used: Expressing, Western Blot, MTT Assay, Flow Cytometry, Cytometry

Curcumin suppressed the upregulation of miR-21 in HepG2 cells induced by acrylamide and induced cell apoptosis. A: Apoptosis rate of HepG2 cells after treatment with curcumin (10 ¦̭ol/L) for 24 hours, as measured by flow cytometry analysis. B: HepG2 cell apoptosis after treatment with curcumin (0 ¦̭ol/L, 1 ¦̭ol/L, 5 ¦̭ol/L, 10 ¦̭ol/L) for 24 hours, as assessed by Hoechest 33258 staining. C and D: The level of PTEN, p-AKT, Bcl2 and Bax in HepG2 cells after pre-treatment with curcumin (10 ¦̭ol/L) for 2 hours and combination with acrylamide for 24 hours, as analyzed by western blotting. E: The expression of miR-21 in HepG2 cells after treatment with curcumin (0 ¦̭ol/L, 1 ¦̭ol/L, 5 ¦̭ol/L, 10 ¦̭ol/L) for 24 hours, as detected by qRT-PCR. F: The expression of miR-21 in HepG2 cells, after pre-treatment by curcumin (10 ¦̭ol/L) for 2 hours and combination with acrylamide for 24 hours, as detected by qRT-PCR. * P
Figure Legend Snippet: Curcumin suppressed the upregulation of miR-21 in HepG2 cells induced by acrylamide and induced cell apoptosis. A: Apoptosis rate of HepG2 cells after treatment with curcumin (10 ¦̭ol/L) for 24 hours, as measured by flow cytometry analysis. B: HepG2 cell apoptosis after treatment with curcumin (0 ¦̭ol/L, 1 ¦̭ol/L, 5 ¦̭ol/L, 10 ¦̭ol/L) for 24 hours, as assessed by Hoechest 33258 staining. C and D: The level of PTEN, p-AKT, Bcl2 and Bax in HepG2 cells after pre-treatment with curcumin (10 ¦̭ol/L) for 2 hours and combination with acrylamide for 24 hours, as analyzed by western blotting. E: The expression of miR-21 in HepG2 cells after treatment with curcumin (0 ¦̭ol/L, 1 ¦̭ol/L, 5 ¦̭ol/L, 10 ¦̭ol/L) for 24 hours, as detected by qRT-PCR. F: The expression of miR-21 in HepG2 cells, after pre-treatment by curcumin (10 ¦̭ol/L) for 2 hours and combination with acrylamide for 24 hours, as detected by qRT-PCR. * P

Techniques Used: Flow Cytometry, Cytometry, Staining, Western Blot, Expressing, Quantitative RT-PCR

Mutual regulation of CYP2E1 and miR-21. A and B: The cell viability of HepG2 cells after the treatment with acrylamide (100 ¦̭ol/L) alone, combination with miR-21 inhibitor (100 nmol/L), siCYP2E1 alone and combination with siCYP2E1 for 24 hours, as measured by MTT assay and EdU staining. C: The expression of miR-21 after the cells were treated with acrylamide (100 ¦̭ol/L), siCYP2E1, and the combination of acrylamide and siCYP2E1 for 24 hours, as detected by qRT-PCR. D: The expression of CYP2E1 in HepG2 cells after transfection with miR-21 inhibitor (100 nmol/L) or miR-21 mimic (20 nmol/L) for 24 hours, as measured by Western blotting. * P
Figure Legend Snippet: Mutual regulation of CYP2E1 and miR-21. A and B: The cell viability of HepG2 cells after the treatment with acrylamide (100 ¦̭ol/L) alone, combination with miR-21 inhibitor (100 nmol/L), siCYP2E1 alone and combination with siCYP2E1 for 24 hours, as measured by MTT assay and EdU staining. C: The expression of miR-21 after the cells were treated with acrylamide (100 ¦̭ol/L), siCYP2E1, and the combination of acrylamide and siCYP2E1 for 24 hours, as detected by qRT-PCR. D: The expression of CYP2E1 in HepG2 cells after transfection with miR-21 inhibitor (100 nmol/L) or miR-21 mimic (20 nmol/L) for 24 hours, as measured by Western blotting. * P

Techniques Used: MTT Assay, Staining, Expressing, Quantitative RT-PCR, Transfection, Western Blot

MiR-21 inhibitor reversed HepG2 cell proliferation induced by acrylamide. A and B: Level of miR-21 and the rate of colony formation after the cells were transfected with miR-21 inhibitor (100 nmol/L), as analyzed by qRT-PCR and colony formation assay. C: HepG2 cell proliferation after treatment with acrylamide (100 ¦̭ol/L), miR-21 inhibitor (100 nmol/L) and the combination, as analyzed by EdU staining assay. D: The level of miR- 21 after treatment with miR-21 inhibitor (100 nmol/L) and acrylamide (100 ¦̭ol/L) in HepG2 cells. * P
Figure Legend Snippet: MiR-21 inhibitor reversed HepG2 cell proliferation induced by acrylamide. A and B: Level of miR-21 and the rate of colony formation after the cells were transfected with miR-21 inhibitor (100 nmol/L), as analyzed by qRT-PCR and colony formation assay. C: HepG2 cell proliferation after treatment with acrylamide (100 ¦̭ol/L), miR-21 inhibitor (100 nmol/L) and the combination, as analyzed by EdU staining assay. D: The level of miR- 21 after treatment with miR-21 inhibitor (100 nmol/L) and acrylamide (100 ¦̭ol/L) in HepG2 cells. * P

Techniques Used: Transfection, Quantitative RT-PCR, Colony Assay, Staining

MiR-21 regulated the signaling pathway of miR-21/ PTEN/ AKT in HepG2 cells. A and B: The expression of PTEN, p-AKT, EGFR and cyclin D1 after cells were transfected with miR-21 inhibitor (100 nmol/L) and treated with acrylamide (100 ¦̭ol/L), as determined by Western blotting. * P
Figure Legend Snippet: MiR-21 regulated the signaling pathway of miR-21/ PTEN/ AKT in HepG2 cells. A and B: The expression of PTEN, p-AKT, EGFR and cyclin D1 after cells were transfected with miR-21 inhibitor (100 nmol/L) and treated with acrylamide (100 ¦̭ol/L), as determined by Western blotting. * P

Techniques Used: Expressing, Transfection, Western Blot

Acrylamide induced miR-21 expression in HepG2 cells. A: Level of miR-21 after treatment with acrylamide (0 ¦̭ol/L, 50 ¦̭ol/L, 100 ¦̭ol/L, 500 ¦̭ol/L) for 24 hours, as analyzed by qRT-PCR. B: Level of miR-21 after treatment with acrylamide at 100 ¦̭ol/L for the indicated time points (0, 3, 6, 12, 24, and 36 hours), as tested by qRT-PCR. *P
Figure Legend Snippet: Acrylamide induced miR-21 expression in HepG2 cells. A: Level of miR-21 after treatment with acrylamide (0 ¦̭ol/L, 50 ¦̭ol/L, 100 ¦̭ol/L, 500 ¦̭ol/L) for 24 hours, as analyzed by qRT-PCR. B: Level of miR-21 after treatment with acrylamide at 100 ¦̭ol/L for the indicated time points (0, 3, 6, 12, 24, and 36 hours), as tested by qRT-PCR. *P

Techniques Used: Expressing, Quantitative RT-PCR

24) Product Images from "Transient Effects in Fluorescence Quenching Measured by 2-GHz Frequency-Domain Fluorometry"

Article Title: Transient Effects in Fluorescence Quenching Measured by 2-GHz Frequency-Domain Fluorometry

Journal: The Journal of physical chemistry

doi: 10.1021/j100296a035

Transient decay analysis of indole in the presence of 0.5 M acrylamide. The data were analyzed by using the Smoluchowski model with R fixed at 7 Å (---, O) and the radiation model with κ = 253 cm/s. The lower panels show the deviations (○, ●).
Figure Legend Snippet: Transient decay analysis of indole in the presence of 0.5 M acrylamide. The data were analyzed by using the Smoluchowski model with R fixed at 7 Å (---, O) and the radiation model with κ = 253 cm/s. The lower panels show the deviations (○, ●).

Techniques Used:

25) Product Images from "The Simultaneous Formation of Acrylamide, β-carbolines, and Advanced Glycation End Products in a Chemical Model System: Effect of Multiple Precursor Amino Acids"

Article Title: The Simultaneous Formation of Acrylamide, β-carbolines, and Advanced Glycation End Products in a Chemical Model System: Effect of Multiple Precursor Amino Acids

Journal: Frontiers in Nutrition

doi: 10.3389/fnut.2022.852717

Proposed reaction scheme for the simultaneous formation of acrylamide, CML, CEL, harman and norharman in multiple precursors amino acids/ glucose chemical model system (A) . Proposed acrolein pathway for the production of acrylamide (B) and Proposed THβC pathway for the generation of β-carbolines (C) .
Figure Legend Snippet: Proposed reaction scheme for the simultaneous formation of acrylamide, CML, CEL, harman and norharman in multiple precursors amino acids/ glucose chemical model system (A) . Proposed acrolein pathway for the production of acrylamide (B) and Proposed THβC pathway for the generation of β-carbolines (C) .

Techniques Used:

Kinetic profiles of Maillard reaction products includes Acrylamide (A,B) , harman (C,D) , and norharman (E,F) in the different amino acid/glucose model system heated at 170°C (A,C,E) and 200°C (B,D,F) . Data were expressed as mean ± SD in triplicates ( n = 3), *, ( P
Figure Legend Snippet: Kinetic profiles of Maillard reaction products includes Acrylamide (A,B) , harman (C,D) , and norharman (E,F) in the different amino acid/glucose model system heated at 170°C (A,C,E) and 200°C (B,D,F) . Data were expressed as mean ± SD in triplicates ( n = 3), *, ( P

Techniques Used:

26) Product Images from "Fast free-of-acrylamide clearing tissue (FACT)—an optimized new protocol for rapid, high-resolution imaging of three-dimensional brain tissue"

Article Title: Fast free-of-acrylamide clearing tissue (FACT)—an optimized new protocol for rapid, high-resolution imaging of three-dimensional brain tissue

Journal: Scientific Reports

doi: 10.1038/s41598-017-10204-5

Pipeline overview of the Fast Free-of-Acrylamide Clearing Tissue (FACT) protocol in comparison with seven other protocols for clearing of mouse brain slices. After perfusion and fixation of brains with paraformaldehyde (PFA) or hydrogel solution, brain slices were allocated into four different clearing solutions with varying sodium dodecyl sulfate (SDS) concentrations and pH. The four subgroups were cleared at two different temperatures.
Figure Legend Snippet: Pipeline overview of the Fast Free-of-Acrylamide Clearing Tissue (FACT) protocol in comparison with seven other protocols for clearing of mouse brain slices. After perfusion and fixation of brains with paraformaldehyde (PFA) or hydrogel solution, brain slices were allocated into four different clearing solutions with varying sodium dodecyl sulfate (SDS) concentrations and pH. The four subgroups were cleared at two different temperatures.

Techniques Used:

27) Product Images from "pH-Sensitive Starch-Based Hydrogels: Synthesis and Effect of Molecular Components on Drug Release Behavior"

Article Title: pH-Sensitive Starch-Based Hydrogels: Synthesis and Effect of Molecular Components on Drug Release Behavior

Journal: Polymers

doi: 10.3390/polym12091974

Chemical structure of the monomers and crosslinker: ( a ) Acrylic acid; ( b ) Acrylamide; ( c ) Methylene bisacrylamide; ( d ) 2-Hydroxy ethyl methacrylate; ( e ) Butyl methacrylate.
Figure Legend Snippet: Chemical structure of the monomers and crosslinker: ( a ) Acrylic acid; ( b ) Acrylamide; ( c ) Methylene bisacrylamide; ( d ) 2-Hydroxy ethyl methacrylate; ( e ) Butyl methacrylate.

Techniques Used:

28) Product Images from "Steric repulsion forces contributed by PEGylation of interleukin-1 receptor antagonist (rhIL-1ra) reduce gelation and aggregation at the silicone oil-water interface"

Article Title: Steric repulsion forces contributed by PEGylation of interleukin-1 receptor antagonist (rhIL-1ra) reduce gelation and aggregation at the silicone oil-water interface

Journal: Journal of pharmaceutical sciences

doi: 10.1016/j.xphs.2018.10.045

Stern-Volmer plots for A) rhIL-1ra and B) PEG rhIL-1ra in 10 mM phosphate buffer, pH 6.5 (white diamonds), urea-unfolded (black diamonds), and adsorbed protein to silicone oil emulsion (gray diamonds). K sv values are determined from the slope of the inverse relative fluorescence versus acrylamide concentration. Each data point represents the average of three samples with error bars representing the standard deviation from the average.
Figure Legend Snippet: Stern-Volmer plots for A) rhIL-1ra and B) PEG rhIL-1ra in 10 mM phosphate buffer, pH 6.5 (white diamonds), urea-unfolded (black diamonds), and adsorbed protein to silicone oil emulsion (gray diamonds). K sv values are determined from the slope of the inverse relative fluorescence versus acrylamide concentration. Each data point represents the average of three samples with error bars representing the standard deviation from the average.

Techniques Used: Fluorescence, Concentration Assay, Standard Deviation

29) Product Images from "Expression and Purification of a Bispecific Antibody against CD16 and Hemagglutinin Neuraminidase (HN) in E. Coli for Cancer Immunotherapy"

Article Title: Expression and Purification of a Bispecific Antibody against CD16 and Hemagglutinin Neuraminidase (HN) in E. Coli for Cancer Immunotherapy

Journal: Reports of Biochemistry & Molecular Biology

doi: 10.29252/rbmb.9.1.50

A. Expression of bsAb minus Fc (bsHN-CD16) in E. coli , Rosetta (DE3). Induction for protein expression was done by 1 mM IPTG at OD 0.6. A. SDS-PAGE of the crude extracts on 12% acrylamide gel. The 55 kDa band showed expression of the desired protein. Lanes 2 and 4 were the bacterial lysate before induction and the lanes 3 and 5 were after induction (circled regions). B. Western blot on the crude lysate using rabbit anti-human whole IgG HRP conjugate. Lanes 4 and 5 were before induction, while lanes 6 and 7 were after induction (Lanes 2 and 3 were colonies with low expression levels).
Figure Legend Snippet: A. Expression of bsAb minus Fc (bsHN-CD16) in E. coli , Rosetta (DE3). Induction for protein expression was done by 1 mM IPTG at OD 0.6. A. SDS-PAGE of the crude extracts on 12% acrylamide gel. The 55 kDa band showed expression of the desired protein. Lanes 2 and 4 were the bacterial lysate before induction and the lanes 3 and 5 were after induction (circled regions). B. Western blot on the crude lysate using rabbit anti-human whole IgG HRP conjugate. Lanes 4 and 5 were before induction, while lanes 6 and 7 were after induction (Lanes 2 and 3 were colonies with low expression levels).

Techniques Used: Expressing, SDS Page, Acrylamide Gel Assay, Western Blot

30) Product Images from "Microfluidic immunoassays as rapid saliva-based clinical diagnostics"

Article Title: Microfluidic immunoassays as rapid saliva-based clinical diagnostics

Journal:

doi: 10.1073/pnas.0607254104

Multistep photopolymerization process enables fabrication of μCEI device. ( A ) μCEI chip layout with size-exclusion membrane. ( B ) Separation gel precursor solution loaded into channels. UV photomasking is used to define an 8% total acrylamide
Figure Legend Snippet: Multistep photopolymerization process enables fabrication of μCEI device. ( A ) μCEI chip layout with size-exclusion membrane. ( B ) Separation gel precursor solution loaded into channels. UV photomasking is used to define an 8% total acrylamide

Techniques Used: Chromatin Immunoprecipitation

31) Product Images from "How Insertion of a Single Tryptophan in the N-Terminus of a Cecropin A-Melittin Hybrid Peptide Changes Its Antimicrobial and Biophysical Profile"

Article Title: How Insertion of a Single Tryptophan in the N-Terminus of a Cecropin A-Melittin Hybrid Peptide Changes Its Antimicrobial and Biophysical Profile

Journal: Membranes

doi: 10.3390/membranes11010048

W-BP100-induced membrane saturation in POPC:POPG (1:1) LUV. ( A ) Titration of POPC:POPG (1:1) LUV in HEPES buffer, containing 100 mmol dm −3 acrylamide, with increasing concentrations of W-BP100, at 25 ± 0.1 °C, as described by Melo et al. [ 32 ]. The breaking points in each curve, where a change of slope is observed, represent membrane saturation points. The fluorescence spectra of each titration are reported in the supplementary material (Figure S7) . ( B ) Plotting of W-BP100 and POPC:POPG (1:1) concentrations at saturation points, and fitting to the membrane saturation model Equation (2). Data points and error bars represent the mean ± SD of three independent experiments.
Figure Legend Snippet: W-BP100-induced membrane saturation in POPC:POPG (1:1) LUV. ( A ) Titration of POPC:POPG (1:1) LUV in HEPES buffer, containing 100 mmol dm −3 acrylamide, with increasing concentrations of W-BP100, at 25 ± 0.1 °C, as described by Melo et al. [ 32 ]. The breaking points in each curve, where a change of slope is observed, represent membrane saturation points. The fluorescence spectra of each titration are reported in the supplementary material (Figure S7) . ( B ) Plotting of W-BP100 and POPC:POPG (1:1) concentrations at saturation points, and fitting to the membrane saturation model Equation (2). Data points and error bars represent the mean ± SD of three independent experiments.

Techniques Used: Titration, Fluorescence

Acrylamide quenching of peptide fluorescence in aqueous solution and in the presence of LUV. Quenching of fluorescence of ( A ) BP100 and ( B ) W-BP100 in HEPES buffer and in the presence of POPC:POPG (1:1) and POPC LUV. Experimental data was fitted to the Stern–Volmer equation for collisional quenching, Equation (3). Data points and error bars are the Mean ± SD of three independent experiments. The fluorescence spectra for each condition are reported in the supplementary material (Figure S8) .
Figure Legend Snippet: Acrylamide quenching of peptide fluorescence in aqueous solution and in the presence of LUV. Quenching of fluorescence of ( A ) BP100 and ( B ) W-BP100 in HEPES buffer and in the presence of POPC:POPG (1:1) and POPC LUV. Experimental data was fitted to the Stern–Volmer equation for collisional quenching, Equation (3). Data points and error bars are the Mean ± SD of three independent experiments. The fluorescence spectra for each condition are reported in the supplementary material (Figure S8) .

Techniques Used: Fluorescence

32) Product Images from "Effects of Maillard-type caseinate glycation on the preventive action of caseinate digests in acrylamide-induced intestinal barrier dysfunction in IEC-6 cells"

Article Title: Effects of Maillard-type caseinate glycation on the preventive action of caseinate digests in acrylamide-induced intestinal barrier dysfunction in IEC-6 cells

Journal: RSC Advances

doi: 10.1039/c8ra08103d

Diffusion of FD-4 in IEC-6 cells treated with two digests for 24 (a) or 48 h (b), and then treated with 2.5 mmol L −1 acrylamide for 24 h. The statistical treatment was done comparing concentrations of different digests. Different letters above the columns indicate that the mean values differ significantly ( p
Figure Legend Snippet: Diffusion of FD-4 in IEC-6 cells treated with two digests for 24 (a) or 48 h (b), and then treated with 2.5 mmol L −1 acrylamide for 24 h. The statistical treatment was done comparing concentrations of different digests. Different letters above the columns indicate that the mean values differ significantly ( p

Techniques Used: Diffusion-based Assay

TJ protein expression and their change levels in IEC-6 cells treated with two digests for 24 (a and c) or 48 h (b and d) and then treated with 2.5 mmol L −1 acrylamide for 24 h. * p
Figure Legend Snippet: TJ protein expression and their change levels in IEC-6 cells treated with two digests for 24 (a and c) or 48 h (b and d) and then treated with 2.5 mmol L −1 acrylamide for 24 h. * p

Techniques Used: Expressing

Relative mRNA expression of TJ proteins in IEC-6 cells treated with two digests for 24 (a) or 48 h (b), and then treated with 2.5 mmol L −1 acrylamide for 24 h. The statistical treatment was done comparing concentrations of different digests. Different letters above the columns indicate that the mean values differ significantly ( p
Figure Legend Snippet: Relative mRNA expression of TJ proteins in IEC-6 cells treated with two digests for 24 (a) or 48 h (b), and then treated with 2.5 mmol L −1 acrylamide for 24 h. The statistical treatment was done comparing concentrations of different digests. Different letters above the columns indicate that the mean values differ significantly ( p

Techniques Used: Expressing

Immunofluorescence staining for TJ proteins in IEC-6 cells treated with two digests for 24 (a) or 48 h (b) and then treated with 2.5 mmol L −1 acrylamide for 24 h. The nuclei were counterstained blue with DAPI. Each merge image shows overlap of one TJ protein. Scale bars = 50 μm.
Figure Legend Snippet: Immunofluorescence staining for TJ proteins in IEC-6 cells treated with two digests for 24 (a) or 48 h (b) and then treated with 2.5 mmol L −1 acrylamide for 24 h. The nuclei were counterstained blue with DAPI. Each merge image shows overlap of one TJ protein. Scale bars = 50 μm.

Techniques Used: Immunofluorescence, Staining

Cytotoxicity (%) of acrylamide (1.25–10 mmol L −1 ) to IEC-6 cells with treatment time of 24 h. Different letters above the columns indicate that the mean values differ significantly ( p
Figure Legend Snippet: Cytotoxicity (%) of acrylamide (1.25–10 mmol L −1 ) to IEC-6 cells with treatment time of 24 h. Different letters above the columns indicate that the mean values differ significantly ( p

Techniques Used:

Viability values (%) of IEC-6 cells treated with two digests for 24 (a) or 48 h (b) and then treated with 2.5 mmol L −1 acrylamide for 24 h. The statistical treatment was done comparing concentrations of different digests. Different letters above the columns indicate that the mean values differ significantly ( p
Figure Legend Snippet: Viability values (%) of IEC-6 cells treated with two digests for 24 (a) or 48 h (b) and then treated with 2.5 mmol L −1 acrylamide for 24 h. The statistical treatment was done comparing concentrations of different digests. Different letters above the columns indicate that the mean values differ significantly ( p

Techniques Used:

Time-responses of TEER in IEC-6 cells treated with two digests for 12–48 h and then treated with 2.5 mmol L −1 acrylamide for 24 h. Data are expressed as percentage of TEER relative to the control. The statistical treatment was done comparing concentrations of different digests. Different letters above the columns indicate that the mean values differ significantly ( p
Figure Legend Snippet: Time-responses of TEER in IEC-6 cells treated with two digests for 12–48 h and then treated with 2.5 mmol L −1 acrylamide for 24 h. Data are expressed as percentage of TEER relative to the control. The statistical treatment was done comparing concentrations of different digests. Different letters above the columns indicate that the mean values differ significantly ( p

Techniques Used:

LDH release in IEC-6 cells treated with two digests for 24 (a) and 48 h (b) and then treated with 2.5 mmol L −1 acrylamide for 24 h. The statistical treatment was done comparing concentrations of different digests. Different letters above the columns indicate that the mean values differ significantly ( p
Figure Legend Snippet: LDH release in IEC-6 cells treated with two digests for 24 (a) and 48 h (b) and then treated with 2.5 mmol L −1 acrylamide for 24 h. The statistical treatment was done comparing concentrations of different digests. Different letters above the columns indicate that the mean values differ significantly ( p

Techniques Used:

33) Product Images from "DHTKD1 Deficiency Causes Charcot-Marie-Tooth Disease in Mice"

Article Title: DHTKD1 Deficiency Causes Charcot-Marie-Tooth Disease in Mice

Journal: Molecular and Cellular Biology

doi: 10.1128/MCB.00085-18

Dhtkd1 −/− mice develop CMT2-like phenotypes. (A to C) Tests of general motor and sensory performance using an accelerating rotarod (A), a treadmill (B), and a hot plate test (C) ( n = 15 mice per genotype). (D) When mice were exposed to 400 ppm of acrylamide for 6 days, retention time was assayed using an accelerating rotarod test ( n = 7 mice per genotype). (E) H E staining (left) denotes atrophies (arrows) in Dhtkd1 −/− gastrocnemius muscle. Magnification, ×200. Electron microscopy (right) of the gastrocnemius sections in wt and Dhtkd1 −/− mice shows sarcomere disorder in Dhtkd1 −/− gastrocnemius muscle. Scale bar, 2 μm. (F) mRNA levels of atrophy-associated ubiquitin ligases, Fbxo32 and MuRF1 , detected by real-time PCR. (G) Circulating LDH and CK levels in serum ( n = 6 mice per genotype). (H) Colocalization of alpha-bungarotoxin and SV2/SH3 markers indicates muscle innervations, partial colocalization representing semi-innervated junctions (arrow), and denervation as shown by alpha-bungarotoxin staining. On the basis of this classification, the percentages of innervated, semi-innervated, and denervated NMJ were analyzed by a chi-square test ( P
Figure Legend Snippet: Dhtkd1 −/− mice develop CMT2-like phenotypes. (A to C) Tests of general motor and sensory performance using an accelerating rotarod (A), a treadmill (B), and a hot plate test (C) ( n = 15 mice per genotype). (D) When mice were exposed to 400 ppm of acrylamide for 6 days, retention time was assayed using an accelerating rotarod test ( n = 7 mice per genotype). (E) H E staining (left) denotes atrophies (arrows) in Dhtkd1 −/− gastrocnemius muscle. Magnification, ×200. Electron microscopy (right) of the gastrocnemius sections in wt and Dhtkd1 −/− mice shows sarcomere disorder in Dhtkd1 −/− gastrocnemius muscle. Scale bar, 2 μm. (F) mRNA levels of atrophy-associated ubiquitin ligases, Fbxo32 and MuRF1 , detected by real-time PCR. (G) Circulating LDH and CK levels in serum ( n = 6 mice per genotype). (H) Colocalization of alpha-bungarotoxin and SV2/SH3 markers indicates muscle innervations, partial colocalization representing semi-innervated junctions (arrow), and denervation as shown by alpha-bungarotoxin staining. On the basis of this classification, the percentages of innervated, semi-innervated, and denervated NMJ were analyzed by a chi-square test ( P

Techniques Used: Mouse Assay, Hot Plate Test, Staining, Electron Microscopy, Real-time Polymerase Chain Reaction

34) Product Images from "Lignin‐g‐poly(acrylamide)‐g‐poly(diallyldimethyl‐ ammonium chloride): Synthesis, Characterization and Applications"

Article Title: Lignin‐g‐poly(acrylamide)‐g‐poly(diallyldimethyl‐ ammonium chloride): Synthesis, Characterization and Applications

Journal: ChemistryOpen

doi: 10.1002/open.201800105

Copolymerization mechanism of lignin with acrylamide and diallydimethyl ammonium chloride.
Figure Legend Snippet: Copolymerization mechanism of lignin with acrylamide and diallydimethyl ammonium chloride.

Techniques Used:

35) Product Images from "Interleukin-1β and tumor necrosis factor-α increase stiffness and impair contractile function of articular chondrocytes"

Article Title: Interleukin-1β and tumor necrosis factor-α increase stiffness and impair contractile function of articular chondrocytes

Journal: Acta Biochimica et Biophysica Sinica

doi: 10.1093/abbs/gmu116

The stiffness of goat articular chondrocytes was largely dependent on actin cytoskeleton (A) Schematic of optical magnetic twisting cytometry (OMTC) for probing cellular stiffness. (B) A micrograph showing real-time tracking of magnetic microbeads that were adhered to the chondrocytes during OMTC measurement. (C) Normalized stiffness ( G′ / G′ 0 ) of chondrocytes in control group ( n = 692), acrylamide (Acryl)-treated group ( n = 756), and cytochalasin D (Cyto D)-treated group ( n = 175). Data were presented as the mean ± SEM. NS, non-significant. ** P
Figure Legend Snippet: The stiffness of goat articular chondrocytes was largely dependent on actin cytoskeleton (A) Schematic of optical magnetic twisting cytometry (OMTC) for probing cellular stiffness. (B) A micrograph showing real-time tracking of magnetic microbeads that were adhered to the chondrocytes during OMTC measurement. (C) Normalized stiffness ( G′ / G′ 0 ) of chondrocytes in control group ( n = 692), acrylamide (Acryl)-treated group ( n = 756), and cytochalasin D (Cyto D)-treated group ( n = 175). Data were presented as the mean ± SEM. NS, non-significant. ** P

Techniques Used: Cytometry

36) Product Images from "Novel pH-Sensitive Cyclic Peptides"

Article Title: Novel pH-Sensitive Cyclic Peptides

Journal: Scientific Reports

doi: 10.1038/srep31322

Quenching of fluorescence of peptides in the presence of POPC liposomes at pH 8 (blue lines) or at pH 3 (red lines) by acrylamide (green lines), and 10-DN (magenta lines) are shown. The percentage of quenching is given in Table S3 .
Figure Legend Snippet: Quenching of fluorescence of peptides in the presence of POPC liposomes at pH 8 (blue lines) or at pH 3 (red lines) by acrylamide (green lines), and 10-DN (magenta lines) are shown. The percentage of quenching is given in Table S3 .

Techniques Used: Fluorescence

37) Product Images from "The New Approach to the Preparation of Polyacrylamide-Based Hydrogels: Initiation of Polymerization of Acrylamide with 1,3-Dimethylimidazolium (Phosphonooxy-)Oligosulphanide under Drying Aqueous Solutions"

Article Title: The New Approach to the Preparation of Polyacrylamide-Based Hydrogels: Initiation of Polymerization of Acrylamide with 1,3-Dimethylimidazolium (Phosphonooxy-)Oligosulphanide under Drying Aqueous Solutions

Journal: Polymers

doi: 10.3390/polym13111806

The 1 H NMR spectra of the reaction system obtained in the process of drying an aqueous solution of acrylamide at a temperature of 298 K (25 °C) after: ( A ) 1 day; ( B ) 4 days; ( C ) 5 days; ( D ) 6 days after the start of the reaction.
Figure Legend Snippet: The 1 H NMR spectra of the reaction system obtained in the process of drying an aqueous solution of acrylamide at a temperature of 298 K (25 °C) after: ( A ) 1 day; ( B ) 4 days; ( C ) 5 days; ( D ) 6 days after the start of the reaction.

Techniques Used: Nuclear Magnetic Resonance

38) Product Images from "Microconstriction Arrays for High-Throughput Quantitative Measurements of Cell Mechanical Properties"

Article Title: Microconstriction Arrays for High-Throughput Quantitative Measurements of Cell Mechanical Properties

Journal: Biophysical Journal

doi: 10.1016/j.bpj.2015.05.029

Change in stiffness and fluidity of K562 leukemia cells after drug treatment. ( a ) Scatter plots of entry times versus applied pressure for control cells and for cells treated with Mg 2+ Ca 2+ -ions ( mgca ), 5-AZA-2′-deoxycytidine ( AZA ), cytochalasin D ( cytoD ), glutaraldehyde ( ga ), nocodazole ( noc ), paclitaxel ( pax ), and acrylamide ( acry ); n > 2000 cells for each measurement. ( Solid markers ) Geometric mean of ∼200–400 cells binned according to pressure. ( Solid lines ) Fit of Eq. 3 to the binned data. Fit to control data is shown in all other plots for comparison ( dashed line ). ( b ) Population average of cell stiffness ( top ) and cell fluidity ( bottom ) for different drug treatments. Error bars represent SDs calculated by bootstrapping. ( Asterisks ) Significant differences with p
Figure Legend Snippet: Change in stiffness and fluidity of K562 leukemia cells after drug treatment. ( a ) Scatter plots of entry times versus applied pressure for control cells and for cells treated with Mg 2+ Ca 2+ -ions ( mgca ), 5-AZA-2′-deoxycytidine ( AZA ), cytochalasin D ( cytoD ), glutaraldehyde ( ga ), nocodazole ( noc ), paclitaxel ( pax ), and acrylamide ( acry ); n > 2000 cells for each measurement. ( Solid markers ) Geometric mean of ∼200–400 cells binned according to pressure. ( Solid lines ) Fit of Eq. 3 to the binned data. Fit to control data is shown in all other plots for comparison ( dashed line ). ( b ) Population average of cell stiffness ( top ) and cell fluidity ( bottom ) for different drug treatments. Error bars represent SDs calculated by bootstrapping. ( Asterisks ) Significant differences with p

Techniques Used:

39) Product Images from "HS-SPME Gas Chromatography Approach for Underivatized Acrylamide Determination in Biscuits"

Article Title: HS-SPME Gas Chromatography Approach for Underivatized Acrylamide Determination in Biscuits

Journal: Foods

doi: 10.3390/foods10092183

Acrylamide (AA) content determined in wheat meal biscuits. Different letters represent values that are significantly different ( p
Figure Legend Snippet: Acrylamide (AA) content determined in wheat meal biscuits. Different letters represent values that are significantly different ( p

Techniques Used:

Acrylamide external calibration curve (RSD
Figure Legend Snippet: Acrylamide external calibration curve (RSD

Techniques Used:

40) Product Images from "Human Cystathionine γ-Lyase Is Inhibited by s-Nitrosation: A New Crosstalk Mechanism between NO and H2S"

Article Title: Human Cystathionine γ-Lyase Is Inhibited by s-Nitrosation: A New Crosstalk Mechanism between NO and H2S

Journal: Antioxidants

doi: 10.3390/antiox10091391

Identification of CSE buried s -nitrosated cysteine(s) by mass spectrometry. Comparison of peak areas from ions corresponding to the tryptic peptides containing Cys84 ( a ), Cys109 ( b ), Cys137 ( c ), Cys172 ( d ), Cys229 ( e ), and Cys307/Cys310 ( f ) with acrylamide (AA) incorporation, in GSNO-treated and Ctrl samples. The isotopic pattern ([M], [M + 1] and [M + 2] peaks) obtained is fully consistent with the one expected for the modified peptide.
Figure Legend Snippet: Identification of CSE buried s -nitrosated cysteine(s) by mass spectrometry. Comparison of peak areas from ions corresponding to the tryptic peptides containing Cys84 ( a ), Cys109 ( b ), Cys137 ( c ), Cys172 ( d ), Cys229 ( e ), and Cys307/Cys310 ( f ) with acrylamide (AA) incorporation, in GSNO-treated and Ctrl samples. The isotopic pattern ([M], [M + 1] and [M + 2] peaks) obtained is fully consistent with the one expected for the modified peptide.

Techniques Used: Mass Spectrometry, Modification

Identification of CSE exposed s -nitrosated cysteine(s) by mass spectrometry. Comparison of the peak areas corresponding to the tetra charged ion at m/z 658.81, which corresponds to the tryptic peptide 213 YMNGHSDVVMGLVSVNCESLHNR 235 with acrylamide (AA) i ncorporation at Cys229 in: GSNO-treated CSE (+GSNO); GSNO-treated CSE following incubation with ascorbate (+GSNO +Asc); GSNO pre-incubation with ascorbate before CSE treatment (+Asc-treated GSNO); untreated CSE (untreated). Two representative replicates of each sample are represented. The isotopic pattern ([M], [M + 1] and [M + 2] peaks) obtained is fully consistent with the one expected for the modified peptide. Idotp: dot product of the expected isotope distributions.
Figure Legend Snippet: Identification of CSE exposed s -nitrosated cysteine(s) by mass spectrometry. Comparison of the peak areas corresponding to the tetra charged ion at m/z 658.81, which corresponds to the tryptic peptide 213 YMNGHSDVVMGLVSVNCESLHNR 235 with acrylamide (AA) i ncorporation at Cys229 in: GSNO-treated CSE (+GSNO); GSNO-treated CSE following incubation with ascorbate (+GSNO +Asc); GSNO pre-incubation with ascorbate before CSE treatment (+Asc-treated GSNO); untreated CSE (untreated). Two representative replicates of each sample are represented. The isotopic pattern ([M], [M + 1] and [M + 2] peaks) obtained is fully consistent with the one expected for the modified peptide. Idotp: dot product of the expected isotope distributions.

Techniques Used: Mass Spectrometry, Incubation, Modification

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  • 99
    Millipore acrylamide
    <t>Acrylamide-induced</t> quenching of intrinsic fluorescence of GGBP/H152C. Modified according Equation (12), Stern-Volmer dependences of the GGBP/H152C fluorescence intensity on acrylamide concentration in the solutions without denaturant (black curve) and in the presence of 0.1 M GdnHCl (red curve). The excitation wavelength was 297 nm.
    Acrylamide, supplied by Millipore, used in various techniques. Bioz Stars score: 99/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Millipore protein a beads slurry
    NS1 interacts with the structural proteins. ( A )  Capsid ,  prM and Envelope proteins co-immunoprecipitate with NS1 . Naïve VeroE6 (CTRL), VeroE6_NS1 WT  (WT) or VeroE6_NS1 HA  (HA) cells were infected with 1 MOI of DVR2A ΔNS1  TCPs. Forty-height hours post-infection, cell lysates clarified by centrifugation were used for immunoprecipitation with HA-affinity agarose beads and eluates (IP) or whole cell lysates (Input) analyzed by western-blotting using antibodies specified on the right of each panel. Numbers on the left refer to molecular weight standards expressed in kDa; black arrowhead on the right indicates the ΔNS1 protein expressed by the DVR2A ΔNS1  genome. A representative experiment of four independent repetitions is shown. ( B )  Interaction between NS1 and prM/E in DENV-2 wild-type virus-infected cells . VeroE6 cells were mock infected or infected with DENV-2 at an MOI of 1. Forty-eight hours later clarified cell lysates were used for immunoprecipitation using a NS1-specific rabbit polyclonal antiserum or the corresponding pre-immune (PIS) antiserum and protein A-Sepharose beads. After extensive washing, eluted protein complexes were analyzed by western-blotting using polyclonal anti-NS1 and anti-prM or mouse monoclonal anti-E or anti-C specific antibodies as specified on the right of each panel. DENV proteins are indicated with arrowheads, asterisks refer to the immunoglobulin heavy chain.
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    Millipore paa
    Surface morphologies of the microspheres of (A) neat PLLA, (B) PLLA- g <t>-PAA,</t> (C) PAM g , (D) PAH2.5 g , (E) PAH5 g , (F) PAM g GO, (G) <t>PAH</t> g GO, (H) PAM g FeO, and (I) PAH g FeO.
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    Acrylamide-induced quenching of intrinsic fluorescence of GGBP/H152C. Modified according Equation (12), Stern-Volmer dependences of the GGBP/H152C fluorescence intensity on acrylamide concentration in the solutions without denaturant (black curve) and in the presence of 0.1 M GdnHCl (red curve). The excitation wavelength was 297 nm.

    Journal: International Journal of Molecular Sciences

    Article Title: Osmolyte-Like Stabilizing Effects of Low GdnHCl Concentrations on d-Glucose/d-Galactose-Binding Protein

    doi: 10.3390/ijms18092008

    Figure Lengend Snippet: Acrylamide-induced quenching of intrinsic fluorescence of GGBP/H152C. Modified according Equation (12), Stern-Volmer dependences of the GGBP/H152C fluorescence intensity on acrylamide concentration in the solutions without denaturant (black curve) and in the presence of 0.1 M GdnHCl (red curve). The excitation wavelength was 297 nm.

    Article Snippet: Materials d -Glucose, guanidine hydrochloride, urea, tris(2-carboxyethylphosphine (TCEP), acrylamide (Sigma, St. Louis, MO, USA), and fluorescent label BADAN (AnaSpec, Fremont, CA, USA) were used without further purification.

    Techniques: Fluorescence, Modification, Concentration Assay

    Schematic representation of passive tissue clearing methods. ( A ) The individual reagents or processes used for polymerization in the passive clearing methods are shown, including the additional incubation steps in polymerization solution (4% acrylamide and 4% paraformaldehyde (PFA) in phosphate-buffered saline (PBS) (IM1), 0.25% 2,2′-azobis[2-(2-imidazolin-2-yl)propane]dihydrochloride (VA-044) and 4% PFA in PBS (IM2), 4% acrylamide-based solution containing N,N,N′,N′-tetramethyl ethylenediamine (TEMED) (AD1), and 4% acrylamide-based solution containing ammonium persulfate (APS) (AD2)) in the initial embedding passive tissue clearing technique (IMPACT)-Basic and IMPACT-Advance protocols. ( B ) Schematic representation of IMPACT optimized for mouse embryos. The steps for IMPACT-Basic and IMPACT-Advance, are drawn in greater detail.

    Journal: International Journal of Molecular Sciences

    Article Title: Investigation of PRDM10 and PRDM13 Expression in Developing Mouse Embryos by an Optimized PACT-Based Embryo Clearing Method

    doi: 10.3390/ijms22062892

    Figure Lengend Snippet: Schematic representation of passive tissue clearing methods. ( A ) The individual reagents or processes used for polymerization in the passive clearing methods are shown, including the additional incubation steps in polymerization solution (4% acrylamide and 4% paraformaldehyde (PFA) in phosphate-buffered saline (PBS) (IM1), 0.25% 2,2′-azobis[2-(2-imidazolin-2-yl)propane]dihydrochloride (VA-044) and 4% PFA in PBS (IM2), 4% acrylamide-based solution containing N,N,N′,N′-tetramethyl ethylenediamine (TEMED) (AD1), and 4% acrylamide-based solution containing ammonium persulfate (APS) (AD2)) in the initial embedding passive tissue clearing technique (IMPACT)-Basic and IMPACT-Advance protocols. ( B ) Schematic representation of IMPACT optimized for mouse embryos. The steps for IMPACT-Basic and IMPACT-Advance, are drawn in greater detail.

    Article Snippet: Slices were placed in a shaking incubator at room temperature with 10 mL of AD1 (4% acrylamide, 0.1% bis-acrylamide (Sigma-Aldrich Inc., MO, USA), 4% PFA, and 1.3% TEMED; Amresco Inc., Solon, PA, USA) in 0.1 M PBS) for 30 min and then submerged in AD2 (4% acrylamide, 0.1% bis-acrylamide, 4% PFA, and 2% APS; Amresco Inc., Solon, PA, USA) in 0.1 M PBS) solution at room temperature for 10 min.

    Techniques: Incubation

    NS1 interacts with the structural proteins. ( A )  Capsid ,  prM and Envelope proteins co-immunoprecipitate with NS1 . Naïve VeroE6 (CTRL), VeroE6_NS1 WT  (WT) or VeroE6_NS1 HA  (HA) cells were infected with 1 MOI of DVR2A ΔNS1  TCPs. Forty-height hours post-infection, cell lysates clarified by centrifugation were used for immunoprecipitation with HA-affinity agarose beads and eluates (IP) or whole cell lysates (Input) analyzed by western-blotting using antibodies specified on the right of each panel. Numbers on the left refer to molecular weight standards expressed in kDa; black arrowhead on the right indicates the ΔNS1 protein expressed by the DVR2A ΔNS1  genome. A representative experiment of four independent repetitions is shown. ( B )  Interaction between NS1 and prM/E in DENV-2 wild-type virus-infected cells . VeroE6 cells were mock infected or infected with DENV-2 at an MOI of 1. Forty-eight hours later clarified cell lysates were used for immunoprecipitation using a NS1-specific rabbit polyclonal antiserum or the corresponding pre-immune (PIS) antiserum and protein A-Sepharose beads. After extensive washing, eluted protein complexes were analyzed by western-blotting using polyclonal anti-NS1 and anti-prM or mouse monoclonal anti-E or anti-C specific antibodies as specified on the right of each panel. DENV proteins are indicated with arrowheads, asterisks refer to the immunoglobulin heavy chain.

    Journal: PLoS Pathogens

    Article Title: Dengue Virus Non-structural Protein 1 Modulates Infectious Particle Production via Interaction with the Structural Proteins

    doi: 10.1371/journal.ppat.1005277

    Figure Lengend Snippet: NS1 interacts with the structural proteins. ( A ) Capsid , prM and Envelope proteins co-immunoprecipitate with NS1 . Naïve VeroE6 (CTRL), VeroE6_NS1 WT (WT) or VeroE6_NS1 HA (HA) cells were infected with 1 MOI of DVR2A ΔNS1 TCPs. Forty-height hours post-infection, cell lysates clarified by centrifugation were used for immunoprecipitation with HA-affinity agarose beads and eluates (IP) or whole cell lysates (Input) analyzed by western-blotting using antibodies specified on the right of each panel. Numbers on the left refer to molecular weight standards expressed in kDa; black arrowhead on the right indicates the ΔNS1 protein expressed by the DVR2A ΔNS1 genome. A representative experiment of four independent repetitions is shown. ( B ) Interaction between NS1 and prM/E in DENV-2 wild-type virus-infected cells . VeroE6 cells were mock infected or infected with DENV-2 at an MOI of 1. Forty-eight hours later clarified cell lysates were used for immunoprecipitation using a NS1-specific rabbit polyclonal antiserum or the corresponding pre-immune (PIS) antiserum and protein A-Sepharose beads. After extensive washing, eluted protein complexes were analyzed by western-blotting using polyclonal anti-NS1 and anti-prM or mouse monoclonal anti-E or anti-C specific antibodies as specified on the right of each panel. DENV proteins are indicated with arrowheads, asterisks refer to the immunoglobulin heavy chain.

    Article Snippet: Samples were incubated with 40 μl of protein A beads slurry (Sigma Aldrich, St. Louis, USA) for 1 hour at 4°C, washed three times with 1 ml of lysis buffer and protein A-bound complexes were transferred into a fresh tube.

    Techniques: Infection, Centrifugation, Immunoprecipitation, Western Blot, Molecular Weight

    Surface morphologies of the microspheres of (A) neat PLLA, (B) PLLA- g -PAA, (C) PAM g , (D) PAH2.5 g , (E) PAH5 g , (F) PAM g GO, (G) PAH g GO, (H) PAM g FeO, and (I) PAH g FeO.

    Journal: Chemistry of Materials

    Article Title: Highlighting the Importance of Surface Grafting in Combination with a Layer-by-Layer Approach for Fabricating Advanced 3D Poly(l-lactide) Microsphere Scaffolds

    doi: 10.1021/acs.chemmater.6b00133

    Figure Lengend Snippet: Surface morphologies of the microspheres of (A) neat PLLA, (B) PLLA- g -PAA, (C) PAM g , (D) PAH2.5 g , (E) PAH5 g , (F) PAM g GO, (G) PAH g GO, (H) PAM g FeO, and (I) PAH g FeO.

    Article Snippet: The three different weak polyelectrolytes, PAA (99%, Sigma-Aldrich), PAH (99%, Alfa Aesar), and PAAm (99%, Polysciences), were used as received.

    Techniques:

    ATR-FTIR spectra of neat PLLA microspheres (black) and PEMs alternately assembled onto the surface of PLLA- g -PAA microspheres with PAM g (red), PAM g GO (magenta), PAM g FeO (orange), PAH2.5 g (green), PAH g GO (violet), PAH g FeO (gray), and PAH5 g (blue) in the region of (A) 1680–1500 cm –1 and (B) 3800–2300 cm –1 . (C) XRD patterns of the 3D microsphere scaffolds with and without GO functionalization.

    Journal: Chemistry of Materials

    Article Title: Highlighting the Importance of Surface Grafting in Combination with a Layer-by-Layer Approach for Fabricating Advanced 3D Poly(l-lactide) Microsphere Scaffolds

    doi: 10.1021/acs.chemmater.6b00133

    Figure Lengend Snippet: ATR-FTIR spectra of neat PLLA microspheres (black) and PEMs alternately assembled onto the surface of PLLA- g -PAA microspheres with PAM g (red), PAM g GO (magenta), PAM g FeO (orange), PAH2.5 g (green), PAH g GO (violet), PAH g FeO (gray), and PAH5 g (blue) in the region of (A) 1680–1500 cm –1 and (B) 3800–2300 cm –1 . (C) XRD patterns of the 3D microsphere scaffolds with and without GO functionalization.

    Article Snippet: The three different weak polyelectrolytes, PAA (99%, Sigma-Aldrich), PAH (99%, Alfa Aesar), and PAAm (99%, Polysciences), were used as received.

    Techniques: