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(A-D): ionized calcium-binding adaptor molecule 1 (Iba1)-stained microglia cells from control (A), pilocarpine(PILO)-treated (B, C) and SZR104 + PILO-treated (D) animals. Scale bars: 10 µm. (E): The average microglia cell areas (cell body and processes) in µm2 values on the y-axis. Biotinylated secondary antibodies (1:400) and the signal was detected with peroxidase-labeled streptavidin (1:6000) (p/n orb348765). (n = 10, mean SEM) in control, PILO-treated and SZR104 + PILO-treated animals (* p 0.05). |
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Development of PDMS MB well surface coating to enhance capture cells with affinity for alpha-IgG antibody. FITC-conjugated IgG was added to MB wells coated with a streptavidin + biotinylated alpha-IgG, b biotinylated alpha-IgG only, c uncoated MBs and d streptavidin + biotinylated alpha-Transferrin. Quantification of the fluorescent intensity averaged over 12 wells is illustrated in (e). Results indicate that FITC-IgG predominantly binds to the (SA) + b-alpha(IgG) coating. Bars indicate standard error, n = 12, *P < 0.0001. Streptavidin (p/n orb348765). |
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Dot Blot Results of Llama IgG2 Isotype control Biotin Conjugated. Llama IgG2 Isotype control Biotin Conjugate (1) 100 ng, (2) 33.33 ng, (3) 11.11 ng, (4) 3.70 ng, (5) 1.23. Antibody: Streptavidin (p/n orb348765) at 1:40000 for 30 mins at RT. Block: BlockOut (p/n orb348644) for 30 mins at RT. Exposure: 1 sec. |
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Multiplex lateral flow detection strips with three detection zones and a positive control zone. Strips tested positive(shown from top to bottom) for Giardia, Entamoeba histolytica, Cryptosporidium, Giardia + Cryptosporidium, Entamoeba histolytica + Cryptosporidium, Giardia + Entamoeba histolytica, and Giardia + Cryptosporidium + Entamoeba histolytica, and no pathogens. Streptavidin-coated gold colloid for lateral flow strips (Streptavidin p/n orb348765). |
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Optimization of streptavidin and aptamers, each concentration and incubation time repeated three times, respectively: (a) Streptavidin concentration, (b) Streptavidin incubation time, (c) Aptamer concentration, (d) Aptamer incubation time. Streptavidin (p/n orb348765). |
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SDS-Page of Streptavidin. Lane 1: Molecular weight markers. Lane 2: Streptavidin. Load: 1.0 ug per lane. Predicted/Observed size: The molecular weight of streptavidin is 55000 daltons. The protein is composed of 4 essentially identical polypeptide chains (homotetramer). This product is chromatographically pure Streptavidin and shows predominantly a single 13.800 dalton band by SDS-PAGE. |
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alphaE-catenin ABD binds cooperatively to actin filaments. (A) alphaE-catenin is composed of an array of five four-helix bundles (blue-shaded boxes) and a C-terminal five-helix bundle (red box). The beta-catenin/homodimerization region and actin-binding domain are marked. All alphaE-catenin constructs used in this study are defined. (B) Localization of 1 µm GFP alphaE-catenin ABD bound to phalloidin-stabilized filamentous actin (20% Cy3 labeled). Scale bar, 5 µm. (C) Average fluorescence signal of GFP alphaE-catenin ABD bound to single-actin filaments plotted against total concentration of GFP alphaE-catenin ABD. Each data point represents average GFP fluorescence per pixel measured over 100 µm of single actin filaments ( 2 TIRF flow chambers). Data were fitted to either a Hill equation (black, straight line) or a hyperbolic function (red, dashed line). (D) Kymographs showing 2 nM GFP alphaE-catenin ABD binding and dissociating from the sides of single actin filaments in the absence or presence of 0.5 or 1 µm dark alphaE-catenin ABD. (E-G) Histograms of 2 nM GFP alphaE-catenin ABD dwell times on filamentous actin in the absence (E) or presence (F) of 0.5 µm dark alphaE-catenin ABD or (G) 1 µm dark alphaE-catenin ABD. Inset, curve fit of the 1-cumulative distribution frequency: (E) single-exponential fit (tau1 = 70 2 ms, n = 1244 molecules), (F) double-exponential fit (tau1 = 88 3 ms [58%)], tau2 = 659 15 ms [42%], n = 1289 molecules), and (G) double-exponential fit (tau1 = 144 4 ms [64%], tau2 = 986 26 ms [36%], n = 1210 molecules). Strept |
