edta (Millipore)
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edta
Edta, supplied by Millipore, used in various techniques. Bioz Stars score: 99/100, based on 81 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/result/edta/product/Millipore
Average 99 stars, based on 81 article reviews
Price from $9.99 to $1999.99
Edta, supplied by Millipore, used in various techniques. Bioz Stars score: 99/100, based on 81 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/result/edta/product/Millipore
Average 99 stars, based on 81 article reviews
Price from $9.99 to $1999.99
edta - by Bioz Stars,
2020-01
99/100 stars
Related Products / Commonly Used Together
Images
1) Product Images from "Metal chelator combined with permeability enhancer ameliorates oxidative stress-associated neurodegeneration in rat eyes with elevated intraocular pressure"
Article Title: Metal chelator combined with permeability enhancer ameliorates oxidative stress-associated neurodegeneration in rat eyes with elevated intraocular pressure
Journal: Free radical biology & medicine
doi: 10.1016/j.freeradbiomed.2014.01.039
Figure Legend Snippet: Treatment with EDTA-MSM reduced protein-HHE adducts in the optic nerves and retinas of HA-injected eyes. Anti-protein-HHE immunohistochemistry counterstained with hematoxylin. Upper panel: optic nerve head and longitudinal section of initial segment of
Techniques Used: Injection, Immunohistochemistry
Figure Legend Snippet: EDTA-MSM treatment decreased the activity of COX-2 in HA-injected eyes. Optic nerve cross-section. Upper panel: COX-2 fluorescent immunohistochemistry (green). Lower panel: COX-2 fluorescence (green) co-stained with DAPI (blue). (A, D) Control optic nerve
Techniques Used: Activity Assay, Injection, Immunohistochemistry, Fluorescence, Staining
Figure Legend Snippet: Treatment with EDTA-MSM reduced protein-MDA adducts in the optic nerves and retinas of HA-injected eyes. Upper and center panels, Anti protein-MDA immunohistochemistry counterstained with hematoxylin. Upper panel: longitudinal section of optic nerve,
Techniques Used: Multiple Displacement Amplification, Injection, Immunohistochemistry
Figure Legend Snippet: EDTA-MSM ameliorated cytoarchitectural disruption of the optic nerve induced by HA injection. Longitudinal sections of paraffin-embedded rat eyeballs including the optic nerve head and initial segment were stained with hematoxylin and eosin. Upper panel:
Techniques Used: Injection, Staining
Figure Legend Snippet: EDTA-MSM ameliorated the edema of optic nerve under HA-induced ocular hypertension. Transverse frozen section of optic nerve, stained with hematoxylin and eosin. Upper panel: 40X magnification; Lower panel: 200X magnification. (A) Optic nerve of control
Techniques Used: Staining
Figure Legend Snippet: EDTA-MSM treatment mitigates demyelination in the optic nerve associated with increased IOP. Longitudinal sections of the optic nerve are stained with Luxol fast blue and counterstained with cresyl violet. 200X magnification. (A) Control optic nerve from
Techniques Used: Staining
Figure Legend Snippet: Treatment with EDTA-MSM reduced protein-HNE adducts in the optic nerves and retinas of HA-injected eyes. Anti-protein-HNE immunohistochemistry counterstained with hematoxylin. Upper panel: longitudinal section of optic nerve, 100X magnification; lower
Techniques Used: Injection, Immunohistochemistry
Figure Legend Snippet: EDTA-MSM treatment had no effect on IOP. Graph of IOP measured weekly over the 12 weeks of this experiment. There was no difference between the groups before injection (week 0). There were no statistical differences between the PBS-injected eyes treated
Techniques Used: Injection
2) Product Images from "Optimization of Liver Decellularization Maintains Extracellular Matrix Micro-Architecture and Composition Predisposing to Effective Cell Seeding"
Article Title: Optimization of Liver Decellularization Maintains Extracellular Matrix Micro-Architecture and Composition Predisposing to Effective Cell Seeding
Journal: PLoS ONE
doi: 10.1371/journal.pone.0155324
Figure Legend Snippet: Decellularization of the rat liver is achieved following one cycle of DET and EDTA-DET treatments. (A) Timeframe and infusion of solutions for the DET and EDTA-DET protocols. (B) Macroscopic appearance of the liver scaffolds showed no difference between the DET and EDTA-DET scaffolds. Following dH 2 O addition, the livers became blanched, with SDC and DNase addition resulting in the livers becoming transparent. (C) H E staining demonstrated absence of cells in sections from DET and EDTA-DET scaffolds. (D) DNA quantification reduced DNA in DET and EDTA-DET scaffolds compared with fresh tissue (p
Techniques Used: Staining
Figure Legend Snippet: Decellularization preserves ECM components, with a higher amount of collagen and elastin present in the EDTA-DET scaffold. (A) MT staining demonstrated acellularity in both scaffolds, showing composition only by connective tissue. (B) PR staining demonstrated composition mostly by collagen fibers. (C) EVG staining revealed maintenance of elastin fibers in the inner surface of blood vessels. (D) AB staining confirmed the presence of GAG in both scaffolds. (E) Collagen was significantly increased in EDTA-DET scaffolds (p
Techniques Used: Staining
Figure Legend Snippet: Addition of EDTA to the protocol makes the matrix more compact in the parenchyma and vasculature. (A-C) SEM confirmed acellularity in the scaffolds, demonstrating composition by a three-dimensional network of connective tissue fibers arranged in a honeycomb-like manner. The structure of the portal triads was identified clearly at low magnification (asterisk). (C) Scaffolds prepared with EDTA-DET were more tightly packed compared to the DET scaffolds, as the porous structure appeared to be compressed. (D) Quantification of the hepatocyte pockets in the EDTA-DET scaffold showed a reduction to approximately 50% of the size in the DET scaffolds. (E, F) Synchrotron-based x-ray phase contrast imaging corroborated these results, demonstrating a denser scaffold in scaffolds pre-treated with EDTA. (G) Infusion of trypan blue dye via the portal vein showed maintenance of the vascular network architecture. There was no dye leakage through the walls to the surrounding tissue; the dye followed the regular pathway of flow to the IVC. Macroscopically, the DET scaffolds were seen to possess a denser vascular network with the dye diffusing through the vessels more readily. (H) Dye intensity within the DET scaffolds followed an S-shaped curve, reaching a maximum point at approximately 35 seconds. Dye intensity within the EDTA-DET scaffold increased in a less steep S-shaped manner with the exponential part lasting 45 seconds instead of 15. Maximum intensity was reached at 75 seconds. (I) These results were paralleled by the quantification of surface area of dye distribution with the point of maximal surface area coverage having a difference of 40 seconds between the two scaffolds; #: p
Techniques Used: Imaging, Flow Cytometry
Figure Legend Snippet: Immunostaining demonstrates the preservation of ECM proteins in the decellularized scaffolds. (A) Collagen I staining in fresh tissue was positive as fine strands in the parenchymal space as well as around the blood vessels (asterisk). This was preserved following decellularization with a strong signal from vascular structures both in DET and EDTA-DET scaffolds. (B, C) Collagen III and collagen IV staining demonstrated a similar distribution and preservation in fresh tissue and decellularized scaffolds. Weak parenchymal staining was observed, and a strong signal surrounding vascular and biliary structures. EDTA-DET scaffolds demonstrated slightly increased staining in the parenchymal space when compared to DET scaffolds. (D) Fibronectin showed strong staining around the main blood vessels in fresh tissue with a more distributed signal pattern in decellularized scaffolds. (E) Laminin showed strong staining around the main blood vessels in fresh tissue with a more distributed signal pattern in decellularized scaffolds; scale bar: 100 μm.
Techniques Used: Immunostaining, Preserving, Staining
3) Product Images from "Surface Charge Density Determines the Efficiency of Cationic Gemini Surfactant Based Lipofection"
Article Title: Surface Charge Density Determines the Efficiency of Cationic Gemini Surfactant Based Lipofection
Journal: Biophysical Journal
doi:
Figure Legend Snippet: The static light scattering of liposome-DNA complexes as a function of X SR-1 . DNA concentration was 0.5 (▪), 1.5 (•), 2.5 (▴), 5.0 (▾), 10.0 (♦), and 15.0 μ M (+). Temperature was maintained at 37°C. Buffer was 5 mM Hepes, 0.1 mM EDTA, pH 7.4 and total concentration of lipid was 50 μ M.
Techniques Used: Concentration Assay
Figure Legend Snippet: Changes in steady-state fluorescence anisotropy of DPH ( X DPH = 0.002) in SR-1/DMPC binary liposomes as a function of X SR-1 . Concentration of DNA was 0 (▪), 1 (•), and 10 mM (▴). Temperature was maintained at 37°C. Buffer was 5 mM Hepes, 0.1 mM EDTA, pH 7.4 and the total lipid concentration was 50 μ M.
Techniques Used: Fluorescence, Concentration Assay
Figure Legend Snippet: Normalized fluorescence emission intensity of DNA associated ethidium bromide at 590 nm as a function of lipid concentration. The mole fraction of SR-1 in DMPC liposomes was X SR-1 = 0.00 (▪), 0.25 (•), 0.50 (▴), 0.75 (▾), and 1.00 (♦). Temperature was maintained at 37°C. Buffer was 5 mM Hepes, 0.1 mM EDTA, pH 7.4. Total concentrations of DNA and ethidium bromide were 34 μ M (in basepairs) and 16 μ M, respectively.
Techniques Used: Fluorescence, Concentration Assay
Figure Legend Snippet: ( A ) DSC traces for SR-1/DMPC MLVs with the indicated mole fractions of the cationic gemini surfactant. Total lipid concentration was one mM in 5 mM Hepes, 0.1 mM EDTA, pH 7.4. ( B ) Thermograms of SR-1/DMPC MLVs with 0.05 mM (in basepairs) DNA. The calibration bars correspond to 5 mJ × °C −1 .
Techniques Used: Concentration Assay
4) Product Images from "Identification of Peptides Derived from the C-terminal Domain of Fibulin-7 Active for Endothelial Cell Adhesion and Tube Formation Disruption"
Article Title: Identification of Peptides Derived from the C-terminal Domain of Fibulin-7 Active for Endothelial Cell Adhesion and Tube Formation Disruption
Journal: Biopolymers
doi: 10.1002/bip.22754
Figure Legend Snippet: Effects of EDTA, heparin, and integrin β1 blocking antibody on the attachment of HUVECs on peptide-coated plates (A) Effect of EDTA and heparin on HUVECs attachment to the peptide-coated plates. 96-well plates were coated with peptides and Fbln7-C as indicated. Either 5 mM EDTA or 10 μg/ml heparin was added to the cell suspension. After a 10 min incubation at 37°C, cells were added to the wells. After 1 hour, the cells were fixed and stained with Crystal Violet and absorbance at 570 nm was measured. Each value represents the mean of six replicates ± SD. p=0.01–0.05; **p=0.001–0.01; ***p=0.0001–0.001. (B) Effects of anti-integrin β1 blocking antibody on HUVECs attachment to the peptides. Cells were preincubated for 10 min at 37°C with 10 μg/ml of the integrin β1-blocking antibody and then added to the wells. Quantification was assessed as described in (A). Each value represents the mean of six replicates ± SD. *p=0.01–0.05; **p=0.001–0.01. Fbln7-C recombinant protein and AG73 and EF-1 peptides were used as controls.
Techniques Used: Blocking Assay, Incubation, Staining, Recombinant
Figure Legend Snippet: Effects of EDTA, heparin, and integrin β1 blocking antibody on the attachment of HUVECs on peptide-coated plates (A) Effect of EDTA and heparin on HUVECs attachment to the peptide-coated plates. 96-well plates were coated with peptides and Fbln7-C as indicated. Either 5 mM EDTA or 10 μg/ml heparin was added to the cell suspension. After a 10 min incubation at 37°C, cells were added to the wells. After 1 hour, the cells were fixed and stained with Crystal Violet and absorbance at 570 nm was measured. Each value represents the mean of six replicates ± SD. p=0.01–0.05; **p=0.001–0.01; ***p=0.0001–0.001. (B) Effects of anti-integrin β1 blocking antibody on HUVECs attachment to the peptides. Cells were preincubated for 10 min at 37°C with 10 μg/ml of the integrin β1-blocking antibody and then added to the wells. Quantification was assessed as described in (A). Each value represents the mean of six replicates ± SD. *p=0.01–0.05; **p=0.001–0.01. Fbln7-C recombinant protein and AG73 and EF-1 peptides were used as controls.
Techniques Used: Blocking Assay, Incubation, Staining, Recombinant
5) Product Images from "Electrostatic Stabilization Plays a Central Role in Autoinhibitory Regulation of the Na+,K+-ATPase"
Article Title: Electrostatic Stabilization Plays a Central Role in Autoinhibitory Regulation of the Na+,K+-ATPase
Journal: Biophysical Journal
doi: 10.1016/j.bpj.2016.12.008
Figure Legend Snippet: Effect of ionic strength, I , of the preincubation buffer solution on the observed rate constant, k obs , for phosphorylation of rabbit kidney ( A ) and pig kidney ( B ) Na + ,K + -ATPase by ATP (pH 7.4, 24°C). The ionic strength of the solution was controlled by varying the Tris concentration (from 1 to 75 mM). In addition to Tris, the preincubation buffer contained 0.1 mM EDTA. Phosphorylation was induced by mixing with an equal volume of phosphorylation-initiating solution (30 mM Imidazole, 5 mM MgCl 2 ). The protein concentration before mixing was 20 μ g/mL. ( Solid lines ) Nonlinear least squares fits of Eqs. 2, 3, 6, and 11 to the experimental data.
Techniques Used: Concentration Assay, Protein Concentration
Figure Legend Snippet: Normalized fluorescence excitation spectra of eosin (29 nM) in the presence of 230 μ g/mL of pig kidney Na + ,K + -ATPase. The blue spectrum is in a solution containing 1 mM Tris ( I = 0.86 mM) and the red spectrum is in a solution containing 75 mM Tris ( I = 63 mM). Each solution contained 0.1 mM EDTA (pH = 7.4, 24°C). The emission wavelength was 550 nm (+OG530 cutoff filter). The bandwidths for both the excitation and emission were 5 nm. To see this figure in color, go online.
Techniques Used: Fluorescence
6) Product Images from "Formation of Three-Dimensional Structures in Supported Lipid Bilayers"
Article Title: Formation of Three-Dimensional Structures in Supported Lipid Bilayers
Journal:
doi: 10.1529/biophysj.106.101139
Figure Legend Snippet: FRAP experiment showing that the lipids freely exchange between the flat and curved regions. The bilayer was composed of 69 mol % DOPC/30 mol % DOPA/1 mol % NBD-PC. The fusion buffer was 250 mM KCl, 50 mM MES, 0.1 mM EDTA, pH 5 solution. To form the caps,
Techniques Used:
Figure Legend Snippet: Epifluorescence images of a 69 mol % DOPC/30 mol % DOPA/1 mol % NBD-PC bilayer. The bilayer was formed in a 250 mM KCl, 50 mM MES, 0.1 mM EDTA, pH 5 solution. After formation, the excess vesicles were rinsed away and the bilayer imaged ( a ); the ionic
Techniques Used:
Figure Legend Snippet: Epifluorescence ( a – e ) and confocal ( f and g ) images of two 69 mol % DOPC/30 mol % DOPA/1 mol % NBD-PC bilayers. The bilayers were formed in a 250 mM KCl, 50 mM MES, 0.1 mM EDTA, pH 5 solution. After the excess vesicles were removed, the outside
Techniques Used:
Figure Legend Snippet: Effect of composition on cap formation was examined using epifluorescence microscopy. Bilayers containing 0–40 mol % DOPA in DOPC with 1 mol % NBD-PC were formed by vesicle fusion in a 250 mM KCl, 50 mM MES, 0.1 mM EDTA, pH 5 solution ( top row
Techniques Used: Epifluorescence Microscopy
7) Product Images from "Expression and oncogenic properties of membranous Notch1 in oral leukoplakia and oral squamous cell carcinoma"
Article Title: Expression and oncogenic properties of membranous Notch1 in oral leukoplakia and oral squamous cell carcinoma
Journal: Oncology Reports
doi: 10.3892/or.2018.6335
Figure Legend Snippet: Validation of Notch1 antibody for detection of membranous and nuclear Notch1 in HN4 cells. (A) Immunofluorescent staining was observed after HN4 cells were treated with PBS (a-c) or 2.5 mM EDTA (d-f) for 10 min and immunostained with the anti-Notch1 antibody. The cells treated with PBS demonstrated strong membranous staining of Notch1 (a-c). An obvious nuclear enrichment of Notch1 staining was observed in the cells treated with EDTA (d-f). Scale bars, 10 µm. (B) Western blot analysis (left) and the quantification (right) of protein extracted from HN4 cells with different treatments revealed transmembranous (TM) Notch1 (S2 cleaved and S3 uncleaved, solid dot) and activated NICD (S3 cleaved, hollow circle). In PBS-treated HN4 cells, the Notch1 protein was mostly in the transmembranous form. The EDTA treatment induced NICD S3-cleaved, as a smaller size band was detected by the Notch1 antibody, and the cleaved state was further confirmed by the Notch1 Val1744-specific antibody. The treatment with CaCl 2 neutralized the function of EDTA and reversed the S3-cleaved status induced by EDTA. The PBS-treated cells were set as the control group. The quantification analysis was calculated from three independent experiments.
Techniques Used: Staining, Western Blot
8) Product Images from "Condensation of oligonucleotides assembled into nicked and gapped duplexes: potential structures for oligonucleotide delivery"
Article Title: Condensation of oligonucleotides assembled into nicked and gapped duplexes: potential structures for oligonucleotide delivery
Journal: Nucleic Acids Research
doi: 10.1093/nar/gki156
Figure Legend Snippet: TEM images of particles formed by various DNA samples upon condensation with the Tat-NLS peptide. ( A ) Condensates formed by the nicked-DNA duplexes of oligonucleotides N1 and N2. ( B ) Condensates formed by the gapped-DNA duplexes of oligonucleotides G1 and G2. ( C ) Condensates formed by the nicked-gapped-DNA duplex of oligonucleotides N1 and G2. ( D ) Condensates formed by 3kbDNA . ( E ) Condensates formed by 21mer duplex. For all samples, DNA was 15 μM in base pair, and was condensed by mixing with the Tat-NLS peptide at a charge ratio of 1:2 (DNA phosphate:cationic charged group of the peptide) in 5 mM Bis-Tris, 50 μM EDTA (pH 7.0). Scale bar is 100 nm.
Techniques Used: Transmission Electron Microscopy
Figure Legend Snippet: Condensation of 3kbDNA , nicked-DNA and a 21mer duplex by hexammine cobalt chloride, as monitored by light scattering. For each data point shown, DNA concentration was 7.5 μM in base pair (5 mM Bis-Tris, 50 μM EDTA, pH 7.0). Light-scattering intensities shown are averages from measurements taken over a 5 min period. Inset : 3kbDNA and nicked-DNA scattering intensities, as a function of hexammine cobalt chloride concentration, normalized to maximum observed intensity. Note : nicked-DNA condensation occurs at a lower hexammine cobalt chloride concentration than 3kbDNA .
Techniques Used: Concentration Assay
Figure Legend Snippet: TEM images of particles formed by various DNA samples upon condensation with hexammine cobalt chloride. ( A ) Condensates formed by the nicked-DNA duplexes of oligonucleotides N1 and N2. ( B ) Condensates formed by the gapped-DNA duplexes of oligonucleotides G1 and G2. ( C ) Condensates formed by the nicked-gapped-DNA duplex of oligonucleotides N1 and G2. ( D ) Condensates formed by 3kbDNA . For all samples, DNA was 15 μM in base pair, and condensed by mixing with an equal volume of 200 μM hexammine cobalt chloride in 5 mM Bis-Tris, 50 μM EDTA (pH 7.0). Scale bar is 100 nm.
Techniques Used: Transmission Electron Microscopy
9) Product Images from "Stimulation of Na+-K+-2Cl− cotransport by arsenite in ferret erythrocytes"
Article Title: Stimulation of Na+-K+-2Cl− cotransport by arsenite in ferret erythrocytes
Journal: The Journal of Physiology
doi: 10.1111/j.1469-7793.1999.0143o.x
Figure Legend Snippet: Effects of kinase inhibitors and Mg 2+ removal on 86 Rb uptake stimulated by the combined effects of arsenite and calyculin A Cells (stored for 2 days) were incubated in FBM containing 11 mM glucose with no further additions (Con) or with 1 mM sodium arsenite and 20 nM calyculin A (C/As) for 1 h. 86 Rb was added to an aliquot of these suspensions to determine uptake rate, and to other aliquots the following additions were made: 2 μM staurosporine (C/As + Sta), 0.3 mM genistein (C/As + Gen), 50 μM PP1 (C/As + PP1), or 10 μM A23187 together with 2 mM EDTA (C/As + I + E). These were incubated for a further 15 min before 86 Rb was added to determine uptake. Bars represent influx rate constants with standard errors.
Techniques Used: Incubation
Figure Legend Snippet: Effects of kinase inhibitors and Mg 2+ removal on 86 Rb influx determined after the subsequent addition of arsenite and calyculin A Cells (stored for 3 days) were incubated in FBM containing 11 mM glucose with no further additions (Con), or with 2 μM staurosporine (Sta), 0.3 mM genistein (Gen), 50 μM PP1 (PP1), or 10 μM A23187 together with 2 mM EDTA (I + E) for 15 min. 86 Rb was added to an aliquot of each suspension to determine influx, and 1 mM sodium arsenite together with 20 nM calyculin A (C/A) were added to another. After incubation for a further hour, 86 Rb was added to those suspensions containing calyculin and arsenite, and influx rates were determined. Bars represent influx rate constants with standard errors.
Techniques Used: Incubation
Figure Legend Snippet: Reversal of the arsenite effect by kinase inhibitors and Mg 2+ removal Cells (stored for 1 day) were incubated in FBM containing 11 mM glucose for 15 min (Con) and in the same medium with the addition of 1 mM sodium arsenite for 60 min (As). 86 Rb uptake rates were determined in aliquots of these suspensions. Staurosporine (2 μM; As + Sta), 0.3 mM genistein (As + Gen), 50 μM PP1 (As + PP1) or 10 μM of the ionophore A23187 together with 2 mM EDTA (As + I + E) were then added to aliquots of the arsenite-containing suspension and incubation continued for a further 15 min. 86 Rb was added and the uptake rate determined. Bars represent the 86 Rb influx rate constants with standard errors.
Techniques Used: Incubation
10) Product Images from "Binding of cGMP to the transducin-activated cGMP phosphodiesterase, PDE6, initiates a large conformational change involved in its deactivation"
Article Title: Binding of cGMP to the transducin-activated cGMP phosphodiesterase, PDE6, initiates a large conformational change involved in its deactivation
Journal: The FEBS journal
doi: 10.1111/j.1742-4658.2011.08104.x
![Change of Pαβγ's characteristics by cGMP binding. A . Dissociation of [ 3 H]cGMP bound to Pαβγ. Purified Pαβγ (16.0 μg) suspended in 640 μl of 55.5 mM Tris·HCl (pH 7.5) containing 4.44 mM EDTA and 1.11 mM IBMX, and [ 3 H]cGMP binding was initiated by adding 80 μl of 9 μM [ 3 H]cGMP. After incubation for 30 min on ice, an aliquot (72 μl) was withdrawn and applied to a Millipore filter, and its radioactivity was designated as the level at time 0. Simultaneously, 72 μl of 10 mM unlabeled cGMP (●) or water (○) was added to the assay mixture. After incubation for 0.25, 0.5, 0.75, 1, 2, 5, 10, and 20 min, an aliquot (80 μl) was withdrawn and applied to a Millipore filter, and its [ 3 H]-radioactivity was measured. The arrow indicates the addition of cGMP or water. The 100% activity indicates that 1.32 pmol of [ 3 H]cGMP was detected in 1.6 μg of Pαβγ (7.72 pmol). B . Elution profile of Pαβγ from a gel filtration column. Purified Pαβγ (70 μg) was incubated with (black) or without (red) unlabeled cGMP (0.5 mM) in 0.5 ml of 25 mM Tris·HCl, pH 7.5, 0.1 mM EDTA, and 1 mM IBMX for 30 min on ice and applied to a Superdex 200 HR column that had been equilibrated with Buffer E. Detailed conditions for this elution are in Experimental Procedure. PDE activity was assayed using 5 μl of the fraction (●). The 100% PDE activity indicates that 12.5 nmol cGMP hydrolyzed/min/tube. [ 3 H]cGMP binding activity was measured using 50 μl of the fraction (□). The 100% activity indicates that 1.50 pmol of [ 3 H]cGMP was detected in the assay mixture.](https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3097306/bin/nihms283948f5.jpg "... 55.5 mM Tris·HCl (pH 7.5) containing 4.44 mM EDTA and 1.11 mM IBMX, and [ 3 H]cGMP ...")
Figure Legend Snippet: Change of Pαβγ's characteristics by cGMP binding. A . Dissociation of [ 3 H]cGMP bound to Pαβγ. Purified Pαβγ (16.0 μg) suspended in 640 μl of 55.5 mM Tris·HCl (pH 7.5) containing 4.44 mM EDTA and 1.11 mM IBMX, and [ 3 H]cGMP binding was initiated by adding 80 μl of 9 μM [ 3 H]cGMP. After incubation for 30 min on ice, an aliquot (72 μl) was withdrawn and applied to a Millipore filter, and its radioactivity was designated as the level at time 0. Simultaneously, 72 μl of 10 mM unlabeled cGMP (●) or water (○) was added to the assay mixture. After incubation for 0.25, 0.5, 0.75, 1, 2, 5, 10, and 20 min, an aliquot (80 μl) was withdrawn and applied to a Millipore filter, and its [ 3 H]-radioactivity was measured. The arrow indicates the addition of cGMP or water. The 100% activity indicates that 1.32 pmol of [ 3 H]cGMP was detected in 1.6 μg of Pαβγ (7.72 pmol). B . Elution profile of Pαβγ from a gel filtration column. Purified Pαβγ (70 μg) was incubated with (black) or without (red) unlabeled cGMP (0.5 mM) in 0.5 ml of 25 mM Tris·HCl, pH 7.5, 0.1 mM EDTA, and 1 mM IBMX for 30 min on ice and applied to a Superdex 200 HR column that had been equilibrated with Buffer E. Detailed conditions for this elution are in Experimental Procedure. PDE activity was assayed using 5 μl of the fraction (●). The 100% PDE activity indicates that 12.5 nmol cGMP hydrolyzed/min/tube. [ 3 H]cGMP binding activity was measured using 50 μl of the fraction (□). The 100% activity indicates that 1.50 pmol of [ 3 H]cGMP was detected in the assay mixture.
Techniques Used: Binding Assay, Purification, Incubation, Radioactivity, Activity Assay, Filtration
![Binding of [ 3 H]cGMP to Pαβγ. A . Concentration of [ 3 H]cGMP. [ 3 H]cGMP binding to Pαβγ (1.92 μg) was measured with indicated concentrations of [ 3 H]cGMP. The [ 3 H]cGMP-binding activity was analyzed by Scatchard plotting (Insert). B . Time-course. Pαβγ (17.3 μg) was incubated in 55 mM Tris·HCl, (pH 7.5) containing 4.4 mM EDTA and 1.1 mM IBMX (final volume, 720 μl) on ice for 10 min. The [ 3 H]cGMP binding was initiated by adding 80 μl of 10 μM [ 3 H]cGMP. After incubation for indicated periods, an aliquot (80 μl) was taken and applied to a Millipore filter. C . The cyclic nucleotide-specificity. After incubation of Pαβγ (1.92 μg) with indicated concentration of unlabeled cGMP (●) or cAMP (○) on ice for 10 min, [ 3 H]cGMP binding was measured with 1 μM [ 3 H]cGMP. The 100% activity indicates that 1.46 pmol [ 3 H]cGMP bound to Pαβγ in tubes. D . Levels of [ 3 H]cGMP-bound Pαβγ trapped by the filter. OS homogenates (18.9 mg protein) were suspended in 9.7 ml of Buffer A. After isolation by the TSK-DEAE 5PW column chromatography and concentration to 0.3 ml, the Pαβγ preparation (∼80 μg) was incubated with 1 μM [ 3 H]cGMP for 30 min on ice and applied to a TSK 250 column that had been equilibrated with Buffer D. The level of [ 3 H]cGMP bound to Pαβγ was calculated based on the [ 3 H]-radioactivity in 70 μl of the fraction (●). The fraction (70 μl) was also applied to a Millipore filter and the [ 3 H]-radioactivity on the filter was measured (□). Only fractions containing Pαβγ were shown. Insert: The rate of [ 3 H]-radioactivity on the filter per the level of [ 3 H]-radioactivity in the fraction. The 100% radioactivity indicates the [ 3 H]-radioactivity detected in fraction 15. Fraction 15 (70 μl) contained 3.2 μg Pαβγ (15.5 pmol) and 13.1 pmol of [ 3 H]cGMP.](https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3097306/bin/nihms283948f4.jpg "... 55 mM Tris·HCl, (pH 7.5) containing 4.4 mM EDTA and 1.1 mM IBMX (final volume, 720 μl) ...")
Figure Legend Snippet: Binding of [ 3 H]cGMP to Pαβγ. A . Concentration of [ 3 H]cGMP. [ 3 H]cGMP binding to Pαβγ (1.92 μg) was measured with indicated concentrations of [ 3 H]cGMP. The [ 3 H]cGMP-binding activity was analyzed by Scatchard plotting (Insert). B . Time-course. Pαβγ (17.3 μg) was incubated in 55 mM Tris·HCl, (pH 7.5) containing 4.4 mM EDTA and 1.1 mM IBMX (final volume, 720 μl) on ice for 10 min. The [ 3 H]cGMP binding was initiated by adding 80 μl of 10 μM [ 3 H]cGMP. After incubation for indicated periods, an aliquot (80 μl) was taken and applied to a Millipore filter. C . The cyclic nucleotide-specificity. After incubation of Pαβγ (1.92 μg) with indicated concentration of unlabeled cGMP (●) or cAMP (○) on ice for 10 min, [ 3 H]cGMP binding was measured with 1 μM [ 3 H]cGMP. The 100% activity indicates that 1.46 pmol [ 3 H]cGMP bound to Pαβγ in tubes. D . Levels of [ 3 H]cGMP-bound Pαβγ trapped by the filter. OS homogenates (18.9 mg protein) were suspended in 9.7 ml of Buffer A. After isolation by the TSK-DEAE 5PW column chromatography and concentration to 0.3 ml, the Pαβγ preparation (∼80 μg) was incubated with 1 μM [ 3 H]cGMP for 30 min on ice and applied to a TSK 250 column that had been equilibrated with Buffer D. The level of [ 3 H]cGMP bound to Pαβγ was calculated based on the [ 3 H]-radioactivity in 70 μl of the fraction (●). The fraction (70 μl) was also applied to a Millipore filter and the [ 3 H]-radioactivity on the filter was measured (□). Only fractions containing Pαβγ were shown. Insert: The rate of [ 3 H]-radioactivity on the filter per the level of [ 3 H]-radioactivity in the fraction. The 100% radioactivity indicates the [ 3 H]-radioactivity detected in fraction 15. Fraction 15 (70 μl) contained 3.2 μg Pαβγ (15.5 pmol) and 13.1 pmol of [ 3 H]cGMP.
Techniques Used: Binding Assay, Concentration Assay, Activity Assay, Incubation, Isolation, Column Chromatography, Radioactivity
![Effects of Pγ and its mutants on [ 3 H]cGMP binding to Pαβγ. A . The effect on the level of [ 3 H]cGMP binding. After incubation or Pαβγ (1.92 μg) with various concentrations of Pγ or its mutants, the [ 3 H]cGMP-binding activity was measured. The 100% activity indicates that 1.46 pmol [ 3 H]cGMP bound to Pαβγ in tubes. Following Pγ and its mutants were used: ●, wild type Pγ; □, N18del; △, N22del; ▲, C18Sub, and ▼, C10del. B . The effect on the time-course of [ 3 H]cGMP-binding. Pαβγ (17.3 μg) was incubated with 1.11 μM Pγ or its mutants in 55 mM Tris·HCl, (pH 7.5) containing 4.4 mM EDTA and 1.1 mM IBMX (final volume, 720 μl) on ice for 30 min. The [ 3 H]cGMP binding was initiated by adding 80 μl of 10 μM [ 3 H]cGMP. After incubation for indicated periods on ice, an aliquot (80 μl) was taken and applied to a Millipore filter. Following Pγ and its mutants were used: ○, control; ●, wild type Pγ; △, N22del; and ▲, C18Sub. C . The effect on the Scatchard plot. Pαβγ (1.92 μg) was incubated with 1 mM of wild type Pγ (●) or N22del (△). As a control, Pαβγ alone was incubated (○). Then, [ 3 H]cGMP binding was initiated by adding indicated concentrations of [ 3 H]cGMP ( C-1 ). The [ 3 H]cGMP binding in C-1 is analyzed by Scatchard plotting ( C-2 ).](https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3097306/bin/nihms283948f6.jpg "... 55 mM Tris·HCl, (pH 7.5) containing 4.4 mM EDTA and 1.1 mM IBMX (final volume, 720 μl) ...")
Figure Legend Snippet: Effects of Pγ and its mutants on [ 3 H]cGMP binding to Pαβγ. A . The effect on the level of [ 3 H]cGMP binding. After incubation or Pαβγ (1.92 μg) with various concentrations of Pγ or its mutants, the [ 3 H]cGMP-binding activity was measured. The 100% activity indicates that 1.46 pmol [ 3 H]cGMP bound to Pαβγ in tubes. Following Pγ and its mutants were used: ●, wild type Pγ; □, N18del; △, N22del; ▲, C18Sub, and ▼, C10del. B . The effect on the time-course of [ 3 H]cGMP-binding. Pαβγ (17.3 μg) was incubated with 1.11 μM Pγ or its mutants in 55 mM Tris·HCl, (pH 7.5) containing 4.4 mM EDTA and 1.1 mM IBMX (final volume, 720 μl) on ice for 30 min. The [ 3 H]cGMP binding was initiated by adding 80 μl of 10 μM [ 3 H]cGMP. After incubation for indicated periods on ice, an aliquot (80 μl) was taken and applied to a Millipore filter. Following Pγ and its mutants were used: ○, control; ●, wild type Pγ; △, N22del; and ▲, C18Sub. C . The effect on the Scatchard plot. Pαβγ (1.92 μg) was incubated with 1 mM of wild type Pγ (●) or N22del (△). As a control, Pαβγ alone was incubated (○). Then, [ 3 H]cGMP binding was initiated by adding indicated concentrations of [ 3 H]cGMP ( C-1 ). The [ 3 H]cGMP binding in C-1 is analyzed by Scatchard plotting ( C-2 ).
Techniques Used: Binding Assay, Incubation, Activity Assay
11) Product Images from "Functional interaction of human Ssu72 with RNA polymerase II complexes"
Article Title: Functional interaction of human Ssu72 with RNA polymerase II complexes
Journal: PLoS ONE
doi: 10.1371/journal.pone.0213598
Figure Legend Snippet: RNA length restriction for phosphatase activity and potential factor involvement. A , EC-EMSA of EECs generated from a 30-second limiting UC pulse with and without a 30-second chase. Complexes were incubated for 0 or 30 minutes prior to HSW isolation. B , RNAs associated with phosphorylated (P) and unphosphorylated (UnP) complexes were extracted from EC-EMSA gel in A and analyzed by urea PAGE. C , EC-EMSA of EECs generated from PICs in the presence of HNE or from PICs that were isolated before the pulse. Each were given a 30-second limiting UC pulse and a 30-second chase, stopped with EDTA, and either incubated for 0 or 30 minutes. D , RNAs associated with each EC-EMSA complex from C were analyzed as in B . E , The normalized profile of transcripts associated with the unphosphorylated complexes after 30 minutes of phosphatase function (HNE UnP) was compared to RNA from the phosphorylated complex generated during the pulse (HNE P) or to RNA associated with unphosphorylated complexes generated from isolated PICs that were incubated for 30 minutes (Isolated UnP). Specific transcript sizes are indicated and a dotted line demarcates the position of the loss of phosphatase activity in HNE.
Techniques Used: Activity Assay, Generated, Incubation, Isolation, Polyacrylamide Gel Electrophoresis
Figure Legend Snippet: Influence of P-TEFb on the phosphatase assay. A , RNA generated during a 3-minute limiting UC pulse with or without a subsequent chase on a template with a 503 nt runoff. Excess P-TEFb (P) or flavopiridol (F) were added during PIC formation. Indicated complexes were chased (C) for 3 minutes in the absence or presence of flavopiridol (FC). B , EC-EMSA of EECs generated in the presence of flavopiridol or P-TEFb and pulsed with limiting UC for 3 minutes. Complexes were stopped with EDTA and incubated for the indicated times prior to HSW (1.6 M KCL) and LSW (60 mM KCl). C , quantification of phosphatase activity in B . Total amount of counts within the unphosphorylated band (UnP) was divided be total counts within the lane to determine percent phosphatased.
Techniques Used: Phosphatase Assay, Generated, Incubation, Activity Assay
12) Product Images from "Secreted cysteine proteases of the carcinogenic liver fluke, Opisthorchis viverrini: regulation of cathepsin F activation by autocatalysis and trans-processing by cathepsin B"
Article Title: Secreted cysteine proteases of the carcinogenic liver fluke, Opisthorchis viverrini: regulation of cathepsin F activation by autocatalysis and trans-processing by cathepsin B
Journal: Cellular microbiology
doi: 10.1111/j.1462-5822.2010.01433.x
Figure Legend Snippet: Exogenous activation of Ov -CF-1 by Ov -CB-1. Purified recombinant Ov -CF-1 was pre-incubated with Ov -CB-1 in 0.1 M sodium acetate containing 1 mM EDTA and 1 mM DTT (pH 5.5) for 1 h at 37°C. Each recombinant was also incubated alone as control reactions. (A) Reactions were analysed on 4-12 % Bis-Tris gels. A band with a molecular mass of ∼ 30 kDa ( arrowhead ) consistent with the mass of mature cathepsin F, that appeared when Ov -CF-1 and Ov -CB-1 were co-incubated was confirmed as a processed variant of Ov -CF-1 by nanoLC-ESI-MS/MS. (B) Following the 1 h pre-incubation step, the dipeptide substrate Z-Leu-Arg-NHMec was added and the reaction was assayed for proteolytic activity by monitoring the release of the fluorogenic leaving group (-NHMec) over 90 min at 37°C. The specific activity of Ov -CF-1 against Z-Leu-Arg-NHMec increased over the course of the assay when the enzyme was pre-incubated with Ov -CB-1. (C) Prolonged incubation (up to 24 h) of Ov -CF-1 with Ov -CB-1 resulted in a SDS-PAGE profile consistent with the molecular sizes of the Ov -CF-1 mature enzyme and liberated prosegment that was identical to that observed when Ov -CF-1 was trans ). (D) The ∼ 30 kDa processed variant of Ov -CF-1 (A, arrowhead ) was digested with trypsin and analysed by nano-LC-ESI-MS/MS. A high-scoring putative N-terminal peptide MDNSNFDWR ( m/z 592.773) was detected (shaded in grey) and indicates that Ov -CB-1 removes the prosegment of Ov -CF-1 via cleavage at Val -1 -Asp -1 ↓ Met 1 ( arrow ) which is also the site used during Ov -CF-1 autocatalysis and exogenous cleavage of the Ov .
Techniques Used: Activation Assay, Purification, Recombinant, Incubation, Variant Assay, Mass Spectrometry, Activity Assay, SDS Page
Figure Legend Snippet: Hydrolysis of human haemoglobin by Ov -CB-1 and Ov -CF-1 and analysis of digests by nanoLC-ESI-MS/MS. (A) Purified human haemoglobin (Hb) was digested by Ov -CB-1 and Ov -CF-1 in 0.1 M sodium acetate buffer (pH 4.0), containing 1 mM DTT and 1mM EDTA at 37°C. Reactions were stopped at time 0 and at various time-points (10, 15, 30, 60, 90, 120, 240 and 360 min) by the addition of the cysteine protease inhibitor E-64 and aliquots analysed on 4-12 % Bis-Tris NuPage gels. (B) Map of Hb α- and β-chains indicating sites of Ov -CB-1 and Ov -CF-1 cleavage. Cleavage sites within Hb present in 15 min reactions as determined by nanoLC-ESI-MS/MS are shown. Arrows , cleavage sites shared by Ov -CB-1 and Ov -CF-1; open arrowheads, Ov -CB-1-specific cleavage sites; filled arrowheads, Ov -CF-1-specific cleavage sites. (C) Frequency of peptides of varying length released following hydrolysis of Hb alpha and beta chains by Ov -CB-1 and Ov -CF-1.
Techniques Used: Mass Spectrometry, Purification, Protease Inhibitor
13) Product Images from "A Simple Alkaline Method for Decellularizing Human Amniotic Membrane for Cell Culture"
Article Title: A Simple Alkaline Method for Decellularizing Human Amniotic Membrane for Cell Culture
Journal: PLoS ONE
doi: 10.1371/journal.pone.0079632
Figure Legend Snippet: Laminin γ3 chain and type IV collagen α1/α2 chain expression in intact HAM and after various treatments. Laminin γ3 (A) and type IV collagen α1/α2 (B) are found in the limbal epithelial BM but not in the central corneal BM. Here and below, single long arrows show denuded parts with no cells (DAPI-counterstained nuclei). Double arrows show places where HAM is disrupted after scraping the membrane with electric toothbrush on low speed. EDTA together with rubbing or n-heptanol leaves a number of epithelial cells still attached to HAM. In contrast, thermolysin and NaOH leave little (single short arrows) to no epithelium on the treated HAM. Except for EDTA+toothbrush scraping, all treatments preserve normal continuous staining patterns of both BM components. Immunohistochemical staining of O.C.T.-embedded and sectioned HAM. Bar = 20 µm.
Techniques Used: Expressing, Staining, Immunohistochemistry
Figure Legend Snippet: Laminin γ2 chain and nidogen-2 expression in intact HAM and after various treatments. Laminin γ2 (A) and nidogen-2 (B) are also expressed in central and limbal epithelial BM. The effects of various treatments are similar to the ones shown on Fig. 3 . EDTA treatment results in incomplete cell removal or even HAM damage (double arrows) after extensive scraping. Thermolysin treatment removes cells well but shows some local irregular staining for proteolysis-sensitive laminin γ2 chain (A). NaOH produces HAM virtually devoid of epithelial cells with continuous staining for both BM components. Immunohistochemical staining of O.C.T.-embedded and sectioned HAM. Bar = 20 µm.
Techniques Used: Expressing, Staining, Immunohistochemistry
14) Product Images from "Liquid Cladding Mediated Optical Fiber Sensors for Copper Ion Detection"
Article Title: Liquid Cladding Mediated Optical Fiber Sensors for Copper Ion Detection
Journal: Micromachines
doi: 10.3390/mi9090471
Figure Legend Snippet: Scanning electron microscopy (SEM) images of ( a ) optical fiber core; ( b ) fiber core treated with APTES; ( c ) fiber core/APTES functionalized with chitosan conjugated EDTA (the inset image is a part of fiber cross-section that contains parts of immobilized layers and the fiber core).
Techniques Used: Electron Microscopy
Figure Legend Snippet: The fiber sensor device output power vs. Cu 2+ concentrations (0 to 2 mM) with APTES/chitosan-EDTA functionalization on the surface.
Techniques Used:
Figure Legend Snippet: Atomic force microscope (AFM) image of ( a ) silica surface; ( b ) APTES-treated silica surface; ( c ) surface functionalized with chitosan conjugated EDTA.
Techniques Used: Microscopy
15) Product Images from "Efficient amplification of self-gelling polypod-like structured DNA by rolling circle amplification and enzymatic digestion"
Article Title: Efficient amplification of self-gelling polypod-like structured DNA by rolling circle amplification and enzymatic digestion
Journal: Scientific Reports
doi: 10.1038/srep14979
Figure Legend Snippet: ( a ) Denaturing PAGE analysis of RCA products before and after digestion by restriction enzyme. Lane 1, 100 p marker; lane 2, 20 bp marker; lane 3, digested DNA fragments without EDTA treatment; lane 4, digested DNA fragments after EDTA treatment. ( b ) Fluorescent microscope image of the RCA product. The highly viscous RCA product was stained using SYBR Gold. Scale bar = 100 μm. ( c ) SEM image of the RCA product. RCA product was dehydrated using ethanol, and freeze-dried. Particle size of microflower like structure was estimated around 2–3 μm, and similar to the structure of RNAi-microsponges previously reported 19 . ( d ) Fluorescent microscope image of RCA product before/after treatment of EDTA. (upper) Before EDTA treatment, microparticles were observed. (lower) After EDTA treatment, microparticles disappeared. Scale bar = 50 μm.
Techniques Used: Polyacrylamide Gel Electrophoresis, Marker, Microscopy, Staining
Figure Legend Snippet: Schematic diagram of the mass amplification of tripodna with adhesive 5′-ends. The template oligodeoxynucleotides (template 1) were designed to satisfy the following requirements: ( a ) the polypodna automatically forms by self-assembly; ( b ) each pod of the polypodna contains a 9 base long TspRI restriction digest site; ( c ) Each 5′-terminal end is phosphorylated in order to ligate with 3′-terminal within the polypodna body, and ( d ) connecting chain is added to the 3′-terminal of the polypodna to allow polypodna to be connected to one another. The designed templates were amplified via the following steps. ( 1 ) The template ssODNs were circularized using T4 DNA ligase. ( 2 ) After annealing the primer (primer 1), the DNA template was amplified through rolling circle amplification technique using Phi29 polymerase. ( 3 ) Before enzyme digestion, the RCA product was treated with EDTA and folded. ( 4 ) Long single-stranded DNAs were digested using restriction enzyme. ( 5 ) The target sequences were purified by size chromatography. ( 6 ) The resultant DNAs self-assembled after annealing, and they formed a hydrogel.
Techniques Used: Amplification, Purification, Chromatography
16) Product Images from "Secondary Structure of a Conserved Domain in an Intron of Influenza A M1 mRNA"
Article Title: Secondary Structure of a Conserved Domain in an Intron of Influenza A M1 mRNA
Journal: Biochemistry
doi: 10.1021/bi500611j
Figure Legend Snippet: Optical melting curves for the wild-type RNA. The absorbance was measured at 280 nm in 20 mM sodium cacodylate (pH 7.0), 0.5 mM EDTA, and 100 mM KCl (blue line); 20 mM sodium cacodylate (pH 7.0), 0.5 mM EDTA, 100 mM KCl, and 10 mM MgCl 2 (black line); 20 mM sodium cacodylate (pH 7.0), 0.5 mM EDTA, 300 mM KCl, and 10 mM MgCl 2 (green line); and 20 mM sodium cacodylate (pH 7.0), 0.5 mM EDTA, and 1 M NaCl (red line).
Techniques Used:
Figure Legend Snippet: 2D-NOESY spectrum of the multibranch structure. (A) The 61 nucleotide construct of the multibranch structure. (B) The imino region of a 2D-NOESY spectrum recorded at 12 °C, with 100 ms mixing time. RNA was folded in 20 mM KH 2 PO 4 (pH 6.5), 80 mM KCl, and 0.05 mM EDTA. Base pairs involved in observed helical walks are shown by colored dots (red = GC, blue = AU, green = GU). Four helical walks are shown by different color, which corresponds to the color of base pairs in panel A. The inset shows the region between 11.8–12.8 ppm with increased contour level to show the imino cross peaks of G129 to G130 and G135 to G146. The imino cross peak between G130 and U152 is not apparent from this plot but can be seen with contour level lowered. The evidence of connection between G130–C153 and A131–U152 is shown in Figure S2 .
Techniques Used: Construct, Mass Spectrometry
17) Product Images from "Comparison of diamine and Mg2+ interactions with RNA tertiary structures: similar vs. differential effects on the stabilities of diverse RNA folds"
Article Title: Comparison of diamine and Mg2+ interactions with RNA tertiary structures: similar vs. differential effects on the stabilities of diverse RNA folds
Journal: Biochemistry
doi: 10.1021/bi400529q
Figure Legend Snippet: Melting profile of the M-box riboswitch. Data are plotted as the derivative of absorbance with respect to temperature at 260 nm (blue) and 280 nm (red). Closed circles correspond to data collected in buffer with 50 mM K + , 1 mM putrescine 2+ and 1 mM Mg 2+ , in K•MOPS – EDTA buffer. Solid lines correspond to data collected in the same buffer with 50 mM K + and no divalent ions. Arrow indicates new transition that appears in the presence of Mg 2+ .
Techniques Used:
Figure Legend Snippet: Effect of putrescine 2+ on the stability of RNAs without Mg 2+ chelation sites. ΔΔG° obs for both RNAs was measured in K•MOPS - EDTA buffer with 50 mM K + and 0.1 mM (red), 0.2 mM (blue) or 0.5 mM (green) MgCl 2 . 20 μM DAP was included with the A-riboswitch. A , A-riboswitch; B , TLR RNA.
Techniques Used:
18) Product Images from "Application of Paper-Supported Printed Gold Electrodes for Impedimetric Immunosensor Development"
Article Title: Application of Paper-Supported Printed Gold Electrodes for Impedimetric Immunosensor Development
Journal: Biosensors
doi: 10.3390/bios3010001
Figure Legend Snippet: ( A ) SPR signal response after injecting 1–20 μg/mL bio-CRP antigen in HEPES-EDTA buffer over MuOH:Biotin-PEG-thiol (85:15 mol%)/streptavidin sensor surface. Down arrows represents the time of bio-CRP antigen injections: 1. = 1 µg/mL, 2. = 2 µg/mL, 3. = 5 µg/mL, 4. = 10 µg/mL and 5. = 20 µg/mL. Up arrows represents the injection of buffer without bio-CRP antigen. ( B ) Mass areal density of bio-CRP antigen showing the Langmuir fit over the data points.
Techniques Used: SPR Assay, Injection
Figure Legend Snippet: ( A ) Surface plasmon resonance (SPR) signal response after injecting 1.25–300 nM streptavidin in HEPES-EDTA buffer over MuOH:Biotin-PEG-thiol (85:15 mol%) SAM sensor surface. Down arrows represents the time of streptavidin injections: 1. = 2.5 nM, 2. = 5 nM, 3. = 10 nM, 4. = 20 nM, 5. = 40 nM, 6. = 80 nM, 7. = 160 nM and 8. = 300 nM. Up arrows represent the injection of buffer without streptavidin. ( B ) Mass areal density curve for streptavidin showing the Langmuir fit over the data points.
Techniques Used: SPR Assay, Injection
19) Product Images from "Thrombospondin-1 protects against pathogen-induced lung injury by limiting extracellular matrix proteolysis"
Article Title: Thrombospondin-1 protects against pathogen-induced lung injury by limiting extracellular matrix proteolysis
Journal: JCI Insight
doi: 10.1172/jci.insight.96914
Figure Legend Snippet: The majority of protease activity secreted by Pseudomonas aeruginosa (PA) exhibits the profile of a metalloprotease and TSP-1 shows dose-dependent inhibition of PA exoprotease activity. ( A ) PA cell-free supernatant (SN) was tested for total protease activity by measuring the hydrolysis of fluorogenic casein substrate over time in the presence or absence of inhibitor. Increasing width of arrowheads indicates increasing molar concentrations of inhibitors. Although SN from Klebsiella pneumoniae (Kp) grown under the same conditions shows no detectable protease activity, that from PA exhibits robust protease activity that is inhibited by EDTA (20, 50, and 100 μM). The effects of serine protease inhibitor aprotinin (20, 50, and 100 μM), and cysteine protease inhibitor E-64 (20, 50, and 100 μM) on PA protease activity are shown for comparison. ( B ) Recombinant human TSP-1 (rhTSP-1) dose-dependently inhibits PA protease activity (rhTSP-1 at 78, 156, and 312 nM). This is compared with the inhibitory activity of EDTA (50 μM, 500 μM, and 5 mM), and specific LasB inhibitor (LasBI) N -mercaptoacetyl-Phe-Tyr-amide (1, 10, and 100 μM). PA SN in the absence of inhibitor is the reference control set as 100% protease activity. ( C ) Human purified TSP-1 (200 pM, 1 nM, and 78 nM) dose-dependently inhibits PA LasB activity as measured by hydrolysis of specific LasB substrate aminobenzoyl-Ala-Gly-Leu-Ala- p -nitro-benzyl-amide. This is compared with the inhibitory activity of LasBI (78 nM, 312 nM, and 20 μM). ( D ) Purified LasB protein (pLasB) was incubated with human TSP-1 from thrombin-activated platelet releasates (PRs) at 1 μg or 10 μg total protein concentrations and elastase activity measured by hydrolysis of elastin substrate over time. LasBI (500 nM, 50 μM, and 100 μM) was incubated with pLasB protein and the degree of percentage pLasB elastase activity inhibition is shown as a comparison. ( A – D ) Assays were performed in triplicate and a representative study of 3 independent experiments is shown. Lines indicate the median.
Techniques Used: Activity Assay, Inhibition, Protease Inhibitor, Recombinant, Purification, Incubation
20) Product Images from "Soluble matrix protein is a potent modulator of mesenchymal stem cell performance"
Article Title: Soluble matrix protein is a potent modulator of mesenchymal stem cell performance
Journal: Proceedings of the National Academy of Sciences of the United States of America
doi: 10.1073/pnas.1812951116
Figure Legend Snippet: Integrin-mediated effects of tropoelastin on MSC adhesion, spreading, and proliferation. ( A ) Cell adhesion to substrate-bound tropoelastin in the presence of EDTA. ( B ) Cell binding to tropoelastin in cation-free buffer with increasing doses of exogenous Mg 2+ , Ca 2+ , and Mn 2+ divalent cations. ( C – E ) Cell spreading on tropoelastin with increasing concentrations of an ( C ) anti-αvβ5, ( D ) anti-αvβ3, or ( E ) pan anti-αv integrin antibody. Cell spreading on fibronectin with and without the anti-αv integrin antibody is shown as a control. ( F ) Cell spreading on tropoelastin in the presence of optimal inhibitory concentrations of anti-αvβ3, anti-αvβ5, combined anti-αvβ3 and anti-αvβ5, and anti-αv integrin antibodies. Cell spreading on TCP and that on tropoelastin in the absence of antibodies or with a nonspecific mouse IgG antibody are also included as controls. Asterisks above the data columns refer to statistical differences from the no-antibody control. ( G ) Representative images of MSC spreading on tropoelastin, with and without integrin-blocking antibodies. (Scale bar: 100 μm.) ( H ) Confocal microscope images of MSCs adhered on tropoelastin- or BSA-coated TCP, stained for focal adhesion vinculin (green) and cell nuclei (blue). The relative density of focal adhesion staining per cell is indicated. (Scale bar: 20 μm.) ( I and J ) MSC proliferation in the presence of ( I ) FGFR and ( J ) integrin inhibitors. Cells were grown on TCP in normal media, in media with 20 μg/mL tropoelastin, or in bFGF-supplemented media for 7 d. ( I ) Increasing doses of the FGFR inhibitor, SU-5402, were added to the media during the proliferation period. Cell numbers were normalized against samples without SU-5402. Cell numbers in media containing tropoelastin or bFGF were compared with those in normal media at each inhibitor concentration to account for the nonspecific toxicity of SU-5402. ( J ) Optimal inhibitory concentrations of anti-αvβ3, anti-αvβ5, anti-αvβ5 and anti-αvβ3, or anti-αv were added to the media over 7 d. Controls without antibodies or with an antibody against a nonexpressed integrin (anti-β8) were included. Green arrows indicate cells grown in the presence of tropoelastin and αv integrin subunit antibodies. Asterisks above individual columns denote significant differences from cells in normal media at each antibody condition. ( K ) MSC proliferation after 7 d in the presence of an FAK inhibitor (FAK inhibitor 14) or a PKB/AKT inhibitor (perifosine). Cell numbers were normalized against uninhibited samples. Asterisks above individual columns represent comparison with the no-inhibitor control. * P
Techniques Used: Binding Assay, Blocking Assay, Microscopy, Staining, Concentration Assay
21) Product Images from "Synergistic Activities of an Efflux Pump Inhibitor and Iron Chelators against Pseudomonas aeruginosa Growth and Biofilm Formation ▿"
Article Title: Synergistic Activities of an Efflux Pump Inhibitor and Iron Chelators against Pseudomonas aeruginosa Growth and Biofilm Formation ▿
Journal: Antimicrobial Agents and Chemotherapy
doi: 10.1128/AAC.00463-10
Figure Legend Snippet: Growth of P. aeruginosa wild-type PAO1 and pvdA mutant in the presence of different PAβN-acetohydroxamic acid combinations (A) and PAβN-EDTA combinations (B). The optical densities of the cultures were recorded after 0, 2, 4, 6, 8, 10,
Techniques Used: Mutagenesis
Figure Legend Snippet: Biofilm formation at the air-liquid interface of glass slides immersed in culture medium containing medium alone (A), 20 μg/ml Dipy (B), 80 μg/ml acetohydroxamic acid (C), 5 μg/ml EDTA (D), 50 μg/ml PAβN (E), 50
Techniques Used:
22) Product Images from "Laminin heparin-binding peptides bind to several growth factors and enhance diabetic wound healing"
Article Title: Laminin heparin-binding peptides bind to several growth factors and enhance diabetic wound healing
Journal: Nature Communications
doi: 10.1038/s41467-018-04525-w
Figure Legend Snippet: Laminin HBD peptides promote cell adhesion in vitro. a , b A total of 3000 cells/well human lung fibroblasts were cultured a without or b with 5 mM EDTA in FGM-2 culture media containing 1% FBS. c , d A total of 3000 cells/well HUVEC were cultured c without or d with 5 mM EDTA in EBM-2 culture media containing 100 ng/mL VEGF-A165 and 1% FBS. Cells were plated on 1 μg/mL laminin peptide pre-coated non-tissue culture-treated plates and incubated for 30 min at 37 °C. After plate washes, cell numbers were quantified using a CyQUANT assay ( n = 10, mean ± SEM). The signals obtained from BSA-coated wells are normalized to 1, and relative fold increases of cell numbers were calculated. Statistical analyses were performed using ANOVA with Tukey’s test. Kruskal–Wallis test followed by Dunn’s multiple comparison was used in b , c . * p
Techniques Used: In Vitro, Cell Culture, Incubation, CyQUANT Assay
23) Product Images from "Laminin heparin-binding peptides bind to several growth factors and enhance diabetic wound healing"
Article Title: Laminin heparin-binding peptides bind to several growth factors and enhance diabetic wound healing
Journal: Nature Communications
doi: 10.1038/s41467-018-04525-w
Figure Legend Snippet: Laminin HBD peptides promote cell adhesion in vitro. a , b A total of 3000 cells/well human lung fibroblasts were cultured a without or b with 5 mM EDTA in FGM-2 culture media containing 1% FBS. c , d A total of 3000 cells/well HUVEC were cultured c without or d with 5 mM EDTA in EBM-2 culture media containing 100 ng/mL VEGF-A165 and 1% FBS. Cells were plated on 1 μg/mL laminin peptide pre-coated non-tissue culture-treated plates and incubated for 30 min at 37 °C. After plate washes, cell numbers were quantified using a CyQUANT assay ( n = 10, mean ± SEM). The signals obtained from BSA-coated wells are normalized to 1, and relative fold increases of cell numbers were calculated. Statistical analyses were performed using ANOVA with Tukey’s test. Kruskal–Wallis test followed by Dunn’s multiple comparison was used in b , c . * p
Techniques Used: In Vitro, Cell Culture, Incubation, CyQUANT Assay
24) Product Images from "The unique histidine in OSCP subunit of F‐ATP synthase mediates inhibition of the permeability transition pore by acidic pH"
Article Title: The unique histidine in OSCP subunit of F‐ATP synthase mediates inhibition of the permeability transition pore by acidic pH
Journal: EMBO Reports
doi: 10.15252/embr.201744705
Figure Legend Snippet: Effect of acidic pH and DPC on the interactions of CyPD with F‐ATP synthase at OSCP and carbethoxylation of OSCP H112 A Bovine heart mitochondria were incubated at the indicated pH in the absence or presence of 200 μM DPC, treated with 1% (w/v) digitonin, and F‐ATP synthase was immunoprecipitated with an anti‐F‐ATP synthase Ab followed by 15% SDS–PAGE. β subunit and CyPD content were detected by Western blotting. The ratio between CyPD and the corresponding β subunit is reported in the lower part of the panel, referring to pH 7.4 values as 100%. Data are an average ± s.e. of three independent experiments. The P ‐values calculated with the Student's t ‐test are shown, *** P ≤ 0.001. B, C EDTA‐SMP were solubilized at the indicated pH values, extracted with 1% (w/v) digitonin, and subjected to BN‐PAGE in order to separate dimers ( V d ) and monomers ( V m ), which were identified by Coomassie blue (B) or in‐gel activity staining (C) and analyzed by densitometry, which is reported in the bottom part of each panel. Values report the dimer/monomer ratio, where the ratio at pH 7.4 was taken as 100%. Data are an average ± s.e. of three independent experiments. The P ‐values calculated with the Student's t ‐test are shown, * P ≤ 0.05 *** P ≤ 0.001. D Sequence of peptides 95–113 of OSCP before (left panel) and after reaction with DPC (right panel) obtained from tryptic digests of the SDS–PAGE band corresponding to the expected molecular mass of OSCP in immunoprecipitated F‐ATP synthase. Fragments of the series b and y identified in the LC‐MS/MS analysis are indicated on the sequence of the peptides. H112 and H112 CeT are indicated in red boldface. Ions y 4 –y 17 show a mass shift of +72 Da in the modified peptide.
Techniques Used: Incubation, Immunoprecipitation, SDS Page, Western Blot, Polyacrylamide Gel Electrophoresis, Activity Assay, Staining, Sequencing, Liquid Chromatography with Mass Spectroscopy, Mass Spectrometry, Modification
25) Product Images from "Evidence for the Lack of a Specific Interaction between Cholesterol and Sphingomyelin"
Article Title: Evidence for the Lack of a Specific Interaction between Cholesterol and Sphingomyelin
Journal: Biophysical Journal
doi:
Figure Legend Snippet: ( A ) I e / I m versus T – T m for PyrPC (▪) and PyrSM (□) residing in LUVs of DMPC at X probe of 0.01. ( B ) I e / I m versus T – T m for PyrPC (▪) and PyrSM (□) residing in DNPC LUVs at X probe = 0.01. Total phospholipid concentration was 25 μ M in 20 mM HEPES and 0.1 mM EDTA at pH 7.0.
Techniques Used: Concentration Assay
Figure Legend Snippet: I e / I m versus increasing contents of cholesterol for PyrPC and PyrSM residing in LUVs of DMPC ( A ) and DNPC ( B ) below (15°C; ▪, PyrPC; •, PyrSM) and above (40°C; □, PyrPC; ○, PyrSM) the main phase transition temperature of the matrix lipid. Total phospholipid concentration was 25 μ M in 20 mM HEPES and 0.1 mM EDTA at pH 7.0.
Techniques Used: Sublimation, Concentration Assay
26) Product Images from "Metallo-β-Lactamase Detection: Comparative Evaluation of Double-Disk Synergy versus Combined Disk Tests for IMP-, GIM-, SIM-, SPM-, or VIM-Producing Isolates "
Article Title: Metallo-β-Lactamase Detection: Comparative Evaluation of Double-Disk Synergy versus Combined Disk Tests for IMP-, GIM-, SIM-, SPM-, or VIM-Producing Isolates
Journal: Journal of Clinical Microbiology
doi: 10.1128/JCM.00818-07
Figure Legend Snippet: Phenotypic tests to detect MBL production. (A and B) DDST results using EDTA and MPA as the IMBL for P. aeruginosa and Acinetobacter spp. at a distance of 2.0 cm (center to center) between disks. (A) Imipenem presented the best results for screening for
Techniques Used:
Figure Legend Snippet: ROC curve from different volumes of EDTA (A) and MPA (B) in combination with ceftazidime for P. aeruginosa .
Techniques Used:
27) Product Images from "Light Emission from the Fe2+-EGTA-H2O2 System: Possible Application for the Determination of Antioxidant Activity of Plant Phenolics"
Article Title: Light Emission from the Fe2+-EGTA-H2O2 System: Possible Application for the Determination of Antioxidant Activity of Plant Phenolics
Journal: Molecules : A Journal of Synthetic Chemistry and Natural Product Chemistry
doi: 10.3390/molecules23040866
Figure Legend Snippet: Chemical structures of citric acid, EGTA and EDTA. The dashed line frame shows the two ether bonds of EGTA most probably involved in the light emission from the Fe 2+ -EGTA-H 2 O 2 system.
Techniques Used:
Figure Legend Snippet: Effect of iron and EGTA replacement with other divalent cations (Cu 2+ , Mn 2+ , Co 2+ , Cr 2+ ) and metal chelators (EDTA, citric acid) on the light emission from Fe 2+ -EGTA-H 2 O 2 system. Results obtained from four series of experiments expressed as mean and standard deviation and (median; interquartile range). (A) Fe 2+ -EGTA-H 2 O 2 ; (B) Cu 2+ -EGTA-H 2 O 2 ; (C) Mn 2+ -EGTA-H 2 O 2 ; (D) Co 2+ -EGTA-H 2 O 2 ; (E) Cr 2+ -EGTA-H 2 O 2 ; (F) Fe 2+ -EDTA-H 2 O 2 ; (G) Fe 2+ -citric acid-H 2 O 2 . * vs. value of B, C, D, E, F and G, p
Techniques Used: Standard Deviation
28) Product Images from "Light Emission from the Fe2+-EGTA-H2O2 System: Possible Application for the Determination of Antioxidant Activity of Plant Phenolics"
Article Title: Light Emission from the Fe2+-EGTA-H2O2 System: Possible Application for the Determination of Antioxidant Activity of Plant Phenolics
Journal: Molecules : A Journal of Synthetic Chemistry and Natural Product Chemistry
doi: 10.3390/molecules23040866
Figure Legend Snippet: Chemical structures of citric acid, EGTA and EDTA. The dashed line frame shows the two ether bonds of EGTA most probably involved in the light emission from the Fe 2+ -EGTA-H 2 O 2 system.
Techniques Used:
Figure Legend Snippet: Effect of iron and EGTA replacement with other divalent cations (Cu 2+ , Mn 2+ , Co 2+ , Cr 2+ ) and metal chelators (EDTA, citric acid) on the light emission from Fe 2+ -EGTA-H 2 O 2 system. Results obtained from four series of experiments expressed as mean and standard deviation and (median; interquartile range). (A) Fe 2+ -EGTA-H 2 O 2 ; (B) Cu 2+ -EGTA-H 2 O 2 ; (C) Mn 2+ -EGTA-H 2 O 2 ; (D) Co 2+ -EGTA-H 2 O 2 ; (E) Cr 2+ -EGTA-H 2 O 2 ; (F) Fe 2+ -EDTA-H 2 O 2 ; (G) Fe 2+ -citric acid-H 2 O 2 . * vs. value of B, C, D, E, F and G, p
Techniques Used: Standard Deviation
29) Product Images from "Mechano-redox control of integrin de-adhesion"
Article Title: Mechano-redox control of integrin de-adhesion
Journal: eLife
doi: 10.7554/eLife.34843
Figure Legend Snippet: ERp5 level in human platelets and platelet releasate. Washed human platelets were prepared from a healthy donor. One ml of platelet suspension (363,000 per µL) was untreated or activated with 20 µM ADP for 2 min. Platelet releasate was collected by centrifugation for 15 min at 1000 g. The platelet pellet was lysed with 50 µL 2% NP40, 30 mM Hepes, 150 mM NaCl, 2 mM EDTA, pH 7.4 buffer containing proteinase inhibitor cocktail and clarified by centrifugation at 10,000 g for 20 min at 4°C. One µL of platelet lysate and 10 µL of releasate were resolved on reducing SDS-PAGE and the ERp5 immunoblotted with 1 µg/mL rabbit anti-ERp5 polyclonal antibody. Platelet ERp5 levels were calculated by reference to a standard curve of recombinant ERp5 concentrations. Densitometry of the chemiluminescent bands was performed by ImageQuant TL software (Biorad). Molecular size markers are shown at left.
Techniques Used: Centrifugation, SDS Page, Recombinant, Software
30) Product Images from "Mesenchymal Stem Cell Alterations in Bone Marrow Lesions in Patients With Hip Osteoarthritis"
Article Title: Mesenchymal Stem Cell Alterations in Bone Marrow Lesions in Patients With Hip Osteoarthritis
Journal: Arthritis & Rheumatology (Hoboken, N.j.)
doi: 10.1002/art.39622
Figure Legend Snippet: Histologic appearance of bone and cartilage in bone marrow lesion (BML) and non‐BML specimens. A and B, Gross histologic appearance of an excised BML specimen with a subchondral cyst ( arrow ) ( A ) and corresponding non‐BML specimen from the same femoral head ( B ). C, Comparison of trabecular bone area (BML versus non‐BML) as a percentage of the total area (n = 14 pairs). ∗ = P = 0.001. D and E, Excised BML specimen showing some cartilage abnormalities above the articular end plate ( D ) and non‐BML fragment from the same femoral head showing intact cartilage above the articular end plate ( E ). F and G, Photomicrographs of Safranin O–stained paired BML ( F ) and non‐BML ( G ) specimens after decalcification in EDTA, showing a greater trabecular area in the BML region. Bars = 3.8 mm ( A and B ), 500 μ M ( D and E ), and 600 μ M ( F and G ).
Techniques Used: Staining
31) Product Images from "Down-Modulation of Monocyte Transendothelial Migration and Endothelial Adhesion Molecule Expression by Fibroblast Growth Factor "
Article Title: Down-Modulation of Monocyte Transendothelial Migration and Endothelial Adhesion Molecule Expression by Fibroblast Growth Factor
Journal: The American Journal of Pathology
doi:
Figure Legend Snippet: Flow cytometric analysis of the effect of SU6668 on ICAM-1 and VCAM-1 expression on resting or bFGF-stimulated endothelium. The HUVECs were cultured in 6-well plates to confluence with bFGF ± SU6668 (25 μmol/L) as indicated. Where indicated, TNF-α (25 U/ml) was added (4 hours) to stimulate the HUVECs. The cells were harvested with trypsin/EDTA and ICAM-1 and VCAM-1 expression was detected with mAb R6.5 or 4B9. The broken vertical line represents the 95th percentile fluorescence value with nonbinding isotype-matched mAb as negative control. Bound primary mAb was detected with fluorescein isothiocyanate-conjugated F(ab) 2 sheep anti-mouse IgG. The histograms are plotted on a log scale of fluorescence intensity. One representative experiment of three is shown.
Techniques Used: Flow Cytometry, Expressing, Cell Culture, Fluorescence, Negative Control
32) Product Images from "Breast Cancer-Derived Exosomes Alter Macrophage Polarization via gp130/STAT3 Signaling"
Article Title: Breast Cancer-Derived Exosomes Alter Macrophage Polarization via gp130/STAT3 Signaling
Journal: Frontiers in Immunology
doi: 10.3389/fimmu.2018.00871
Figure Legend Snippet: EO771 cells secrete exosomes which are taken up by bone marrow-derived macrophages (BMDMs). (A) Transmission electron microscopy of isolated particles indicates a sphere-shaped structure. The size bar represents 100 nm. (B) Size distribution and enumeration of particles assessed by Tunable Resistive Pulse Sensing ( n = 3). (C) Expression of exosomal and cell markers in EO771 cell lysate (Cell) and exosomes (Exo). (D) Immunofluorescence imaging of DiD-labeled, EO771-derived exosome uptake into macrophages after 24 h. Macrophages were pretreated with EDTA (1 µM) for an hour as indicated. The size bar represents 50 µm. (E,F) BMDMs were gated for CD11b + /F4/80 + double-positive populations and DiD + cells quantified. (E) Representative histogram of flow cytometry analyses. (F) Quantification of four independent repeats. * p
Techniques Used: Derivative Assay, Transmission Assay, Electron Microscopy, Isolation, Tunable Resistive Pulse Sensing, Expressing, Immunofluorescence, Imaging, Labeling, Flow Cytometry, Cytometry
33) Product Images from "Breast Cancer-Derived Exosomes Alter Macrophage Polarization via gp130/STAT3 Signaling"
Article Title: Breast Cancer-Derived Exosomes Alter Macrophage Polarization via gp130/STAT3 Signaling
Journal: Frontiers in Immunology
doi: 10.3389/fimmu.2018.00871
Figure Legend Snippet: EO771 cells secrete exosomes which are taken up by bone marrow-derived macrophages (BMDMs). (A) Transmission electron microscopy of isolated particles indicates a sphere-shaped structure. The size bar represents 100 nm. (B) Size distribution and enumeration of particles assessed by Tunable Resistive Pulse Sensing ( n = 3). (C) Expression of exosomal and cell markers in EO771 cell lysate (Cell) and exosomes (Exo). (D) Immunofluorescence imaging of DiD-labeled, EO771-derived exosome uptake into macrophages after 24 h. Macrophages were pretreated with EDTA (1 µM) for an hour as indicated. The size bar represents 50 µm. (E,F) BMDMs were gated for CD11b + /F4/80 + double-positive populations and DiD + cells quantified. (E) Representative histogram of flow cytometry analyses. (F) Quantification of four independent repeats. * p
Techniques Used: Derivative Assay, Transmission Assay, Electron Microscopy, Isolation, Tunable Resistive Pulse Sensing, Expressing, Immunofluorescence, Imaging, Labeling, Flow Cytometry, Cytometry
34) Product Images from "Neutrophil Interactions Stimulate Evasive Hyphal Branching by Aspergillus fumigatus"
Article Title: Neutrophil Interactions Stimulate Evasive Hyphal Branching by Aspergillus fumigatus
Journal: PLoS Pathogens
doi: 10.1371/journal.ppat.1006154
Figure Legend Snippet: Apical branching is induced following chelation of iron. (A) Treatment with iron chelators increased branching compared to controls. EDTA provides non-specific chelation of free metal ion, while HBED and lactoferrin provide specific chelation of Fe. Lactoferrin (Fe) provides an iron-saturated negative control for lactoferrin iron chelation. (B) Iron chelation significantly reduced hyphal tip growth speed. Lack of growth inhibition by iron-saturated lactoferrin demonstrates the specificity of lactoferrin activity in this assay. N = 25 hyphae scored per condition from 3 experiments. Errors bars: mean ± SEM. Statistics: One-way ANOVA with Tukey’s post test. Adjusted p values: *p≤0.05, **p≤0.01, ***p≤0.001, ****p≤0.0001.
Techniques Used: Negative Control, Inhibition, Activity Assay
35) Product Images from "Hard water softening effect of a baby cleanser"
Article Title: Hard water softening effect of a baby cleanser
Journal: Clinical, Cosmetic and Investigational Dermatology
doi: 10.2147/CCID.S111729
Figure Legend Snippet: The effect of HTT cleanser components on free Ca 2+ ion in solution. Notes: ( A ) In-use dilution 1% and ( B ) 10%. The line with slope =1 illustrates the starting conditions. BB= Burt’s Bees ® (Burt’s Bees Baby Bee Shampoo Wash, Durham, NC, USA). HTT= Johnson’s ® Head-To-Toe ® Baby Wash (Johnson Johnson Consumer Inc., Skillman, NJ, USA. CB= California Baby ® Super Sensitive™ Shampoo Bodywash (Los Angeles, CA, USA). Abbreviations: Ca 2+ , ionized calcium; EDTA, ethylenediaminetetraacetic acid; PEG80SL, PEG-80 sorbitan laurate; SLES, sodium laureth sulfate; SLES/CAPB/PEG80SL, sodium laureth sulfate, cocamidopropyl betaine, and PEG-80 sorbitan laurate in a 1:1:1 weight ratio.
Techniques Used:
36) Product Images from "Optimization of a Relative Telomere Length Assay by Monochromatic Multiplex Real-Time Quantitative PCR on the LightCycler 480"
Article Title: Optimization of a Relative Telomere Length Assay by Monochromatic Multiplex Real-Time Quantitative PCR on the LightCycler 480
Journal: The Journal of Molecular Diagnostics : JMD
doi: 10.1016/j.jmoldx.2016.01.004
Figure Legend Snippet: EDTA titration melting curves. Melting curves were derived using change in relative fluorescence units (ΔRFU) per 0.2°C on various amounts of pooled human whole-blood DNA. Melting curves for the following conditions are shown: 0 ( A ), 0.4 ( B ), 0.8 ( C ), 1.2 ( D ), and 1.6 ( E ) mmol/L added EDTA. The arrow indicates the dissociation peak of a nonspecific peak present in A through C .
Techniques Used: Titration, Derivative Assay, Fluorescence
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