Journal: Nanoscale Research Letters

Article Title: Strong plasmon-exciton coupling in a hybrid system of gold nanostars and J-aggregates

doi: 10.1186/1556-276X-8-134

Figure Lengend Snippet: Surface-enhanced Raman spectra, scanning electron microscopy image, and Raman micromapping. Surface-enhanced Raman spectrum (red curve) of the hybrid nanostructure of gold nanostars and the J-aggregates of JC1 dye as compared to the Raman spectrum of J-aggregates of JC1 only (black curve). Scanning electron microscopy image and Raman micromapping of tightly bound agglomerates of gold nanostars and J-aggregates of JC1 dye are given in the left and the right insets, respectively.

Article Snippet: The formation of the hybrid structures of two constituent compounds has been further confirmed by surface-enhanced Raman scattering (SERS) measurements using a confocal Raman microscopy setup (Alpha300, 600 mm −1 grating, 3 cm −1 spectral resolution, continuous wave laser excitation at 532 nm, WITec, Ulm, Germany), as the hot spots provided by sharp tips of agglomerated Au nanostars are expected to enhance Raman scattering response of the attached organic compounds [ ].

Techniques: Electron Microscopy

Journal: PLoS ONE

Article Title: Enrichment of GABARAP Relative to LC3 in the Axonal Initial Segments of Neurons

doi: 10.1371/journal.pone.0063568

Figure Lengend Snippet: (A) Expression of GFP-GABARAP in tissues of GFP-GABARAP transgenic mice. Cell lysates were immunoblotted with anti-GFP antibody to detect GFP-GABARAP. Endogenous GABARAP and LC3 were detected with anti-GABARAP and anti-LC3 antibodies, respectively. Arrow-heads indicate GFP-GABARAP; asterisks indicate non-specific bands in the skeletal muscle. CON, lysate from control mouse tissue; tg, lysate from GFP-GABARAP transgenic mouse tissue; SK muscle, skeletal muscle. ( B – I ) Confocal fluorescence images of GFP-GABARAP in the heart ( B and C ), liver ( E and F ), and SK muscle ( H and I ). Fluorescence of GFP-GABARAP was observed under confocal laser-scanning microscopy (FV1000: Olympus), and GFP-GABARAP dots were counted using an ImageJ program ( http://rsbweb.nih.gov/ij/ ) with a TopHat plugin ( http://rsb.info.nih.gov/ij/plugins/lipschitz/ ). ( D , G , and J ) Relative ratios of GFP-GABARAP dots per unit area in the heart ( D ), liver ( E ), and skeletal muscle ( J ), using at least 10 images from each tissue in four mice. Fed , tissues under fed conditions; Starvation , tissues under starvation conditions for 48 h. Bars indicate 10 mm.

Article Snippet: Polyclonal anti-GFP antibody was purchased from Rockland (600-101-215).

Techniques: Expressing, Transgenic Assay, Control, Fluorescence, Confocal Laser Scanning Microscopy

Journal: Molecules

Article Title: Flame-Retarded Rigid Polyurethane Foam Composites with the Incorporation of Steel Slag/Dimelamine Pyrophosphate System: A New Strategy for Utilizing Metallurgical Solid Waste

doi: 10.3390/molecules27248892

Figure Lengend Snippet: Raman spectra of RPUF and RPUF-R composites: ( a ) RPUF; ( b ) RPUF-1; ( c ) RPUF-3; ( d ) RPUF-5.

Article Snippet: Laser confocal Raman spectroscopy (Roman): The carbon slag was obtained by calcining the composites in a muffle furnace at 600 °C for 10 min, and then tested by laser confocal Raman spectroscopy (LabRAM HR Evolution, HORIBA Scientific) to investigate the graphitization degree of the carbon slag for the composites.

Techniques:

Journal: PLoS Pathogens

Article Title: Human Papillomaviruses Activate the ATM DNA Damage Pathway for Viral Genome Amplification upon Differentiation

doi: 10.1371/journal.ppat.1000605

Figure Lengend Snippet: HFK-31 cells, as well as normal HFKs were harvested, fixed and permeabilized at either time 0 (undifferentiated cells), or after 48 hours of differentiation in high calcium medium containing DMSO, or 10 uM of the ATM inhibitor KU-55933. Samples were stained with (A) anti-pATM Ser1981 (red), anti-H2AX Ser139 (γ-H2AX) (green) antibodies; (B) anti-pCHK2 Thr68 (green), anti-γ-H2AX (red) antibodies; or (C) an anti-K10 antibody as a marker of differentiation. Samples were subsequently analyzed by confocal laser scanning microscopy using either a 60× objective lens (panels A and B), or a 40× objective lens (panel C). Cellular DNA was counterstained with DAPI. (D) Sections from organotypic raft cultures generated from HFK-31 cells, or normal HFKs were stained with an antibody to detect pCHK2-Thr68 (green). Cellular DNA was counterstained with DAPI. Images were visualized using confocal laser scanning microscopy. Ca = calcium.

Article Snippet: Primary antibody dilutions for mouse anti-phospho-ATM Ser1981 (Rockland), anti phospho-H2AX Ser139 (γ-H2AX) (Upstate) were 1∶400 and 1∶500, respectively.

Techniques: Staining, Marker, Confocal Laser Scanning Microscopy, Generated

Journal: Journal of Lipid Research

Article Title: Importance of the carboxyl terminus of FAT/CD36 for plasma membrane localization and function in long-chain fatty acid uptake

doi: 10.1194/jlr.m600255-jlr200

Figure Lengend Snippet: Fig. 1. Truncation mutants were used to explore the involvement of the cytoplasmic C-terminus in the intracellular trafficking of fatty acid translocase (FAT/CD36). A: Schematic diagrams of wild-type FAT/ CD36 and C-terminal truncation mutants. Hydrophobic transmembrane domains (TM) are depicted as hatched boxes, which define the boundaries of the extracellular domain (ECD) spanning the region. B: Western blot analysis of surface-labeled proteins from transfectants expressing FAT/CD36 or truncation mutants FAT/CD36del5 and FAT/CD36del10. Cells were surface-biotinylated and lysed with 1% Triton X- 100 in TNE buffer, and the biotinylated proteins were captured with streptavidin-conjugated agarose beads. Samples of lysates (20 mg) and streptavidin precipitates were subjected to SDS-PAGE and immunoblotting with monoclonal antibodies against FAT/CD36 (monoclonal antibody MO25) or b-actin. Results are representative of replicate experiments. C: Localization of FAT/CD36 and FAT/CD36 truncation mutants by confocal laser scanning microscopy (340 objective plus 33 zoom). Cells were grown on coverslips, fixed, and stained by indirect immunofluorescence (red) to detect FAT CD36 (monoclonal antibody UA009 plus Cy3-conjugated anti-mouse Ig) either with (intracellular) or without (cell surface) permeabilization. Nuclei were stained with 4¶,6-diamino-phenylindole (blue).

Article Snippet: The following antibodies were purchased: mouse monoclonal anti-caveolin-1 (clone C060; BD Transduction Laboratories, Lexington, KY), biotinylated goat polyclonal anti-green fluorescent protein (Rockland Immunochemicals, Gilbertsville, PA), mouse monoclonal anti-b-actin (Sigma, St. Louis, MO), horseradish peroxidase-conjugated anti-mouse IgG F(ab¶)2 (Amersham Biosciences, Piscataway, NJ), FITC-conjugated anti-mouse immunoglobulin (BD Pharmingen, San Diego, CA), and Cy3-conjugated anti-mouse IgG ( Jackson ImmunoResearch Laboratories,WestGrove,PA).Horseradishperoxidase-conjugated streptavidin was purchased from Amersham, and Alexa Fluor 594 cholera toxin B subunit (CT-B) conjugate was purchased from Molecular Probes (Eugene, OR).

Techniques: Western Blot, Labeling, Expressing, SDS Page, Bioprocessing, Confocal Laser Scanning Microscopy, Staining, Immunofluorescence

Journal: Journal of Lipid Research

Article Title: Importance of the carboxyl terminus of FAT/CD36 for plasma membrane localization and function in long-chain fatty acid uptake

doi: 10.1194/jlr.m600255-jlr200

Figure Lengend Snippet: Fig. 5. Enrichment of FAT/CD36 in lipid raft and non- raft components of the plasma membrane. H4IIE cells stably expressing FAT/CD36 were surface-biotinylated, lysed in 1% Triton X-100 at 4jC, and subjected to discontinu- ous 5–40% sucrose gradient centrifugation as detailed in Methods. A: Aliquots from each fraction were subjected to SDS-PAGE and immunoblotting with anti-FAT/CD36 using monoclonal antibody MO25 (upper panel). Im- munoblots were then stripped and reprobed with strep- tavidin-HRP (lower panel). B: Fractions 2–4 were pooled (DRM fractions), as were fractions 8–12 (nonraft frac- tions), and biotinylated plasma membrane (PM) proteins were precipitated from each using streptavidin-conjugated agarose beads. Streptavidin precipitates and 20 ml from the washings were subjected to SDS-PAGE and immuno- blotting with anti-FAT/CD36 (upper panel). Membranes were then stripped and reprobed with streptavidin-HRP (lower panel).

Article Snippet: The following antibodies were purchased: mouse monoclonal anti-caveolin-1 (clone C060; BD Transduction Laboratories, Lexington, KY), biotinylated goat polyclonal anti-green fluorescent protein (Rockland Immunochemicals, Gilbertsville, PA), mouse monoclonal anti-b-actin (Sigma, St. Louis, MO), horseradish peroxidase-conjugated anti-mouse IgG F(ab¶)2 (Amersham Biosciences, Piscataway, NJ), FITC-conjugated anti-mouse immunoglobulin (BD Pharmingen, San Diego, CA), and Cy3-conjugated anti-mouse IgG ( Jackson ImmunoResearch Laboratories,WestGrove,PA).Horseradishperoxidase-conjugated streptavidin was purchased from Amersham, and Alexa Fluor 594 cholera toxin B subunit (CT-B) conjugate was purchased from Molecular Probes (Eugene, OR).

Techniques: Clinical Proteomics, Membrane, Stable Transfection, Expressing, Gradient Centrifugation, SDS Page, Western Blot