Journal: Sensors and Actuators Reports

Article Title: Integrated Microphotonic Platform for Highly Sensitive Virus Detection

doi: 10.1016/j.snr.2025.100320

Figure Lengend Snippet: Fig. 6. Sensorgrams for the TE mode at 1310 nm acquired from BSA-antiBSA studies in the case of RR with strip waveguides (on the top) and RR with slot waveguides (on the bottom). The region boundaries that involve a change in the circulating solution are indicated by the vertical lines. In particular, the new solution takes approximately 8 min to get to the sensor.

Article Snippet: BSA used in the experiments is supplied by Fisher Chemical and produced by a proprietary heat shock process (catalog number: BPE9702-100), whereas antiBSA is provided by Bethyl Laboratories, Inc (catalog number: A10-113).

Techniques: Stripping Membranes

Journal: Sensors and Actuators Reports

Article Title: Integrated Microphotonic Platform for Highly Sensitive Virus Detection

doi: 10.1016/j.snr.2025.100320

Figure Lengend Snippet: Fig. 7. Evaluation of the resonance wavelength shift against the antiBSA con centration in the case of ring resonator with strip waveguides (on the top) and slot waveguides (on the bottom). The error bars are evaluated by considering 3.3 times the standard deviation of the measurements done while flowing PBS 1X in the first step of the assay.

Article Snippet: BSA used in the experiments is supplied by Fisher Chemical and produced by a proprietary heat shock process (catalog number: BPE9702-100), whereas antiBSA is provided by Bethyl Laboratories, Inc (catalog number: A10-113).

Techniques: Stripping Membranes, Standard Deviation

Journal: Molecular Medicine

Article Title: d -Amino Acid Substitution of Peptide-Mediated NF-κB Suppression in mdx Mice Preserves Therapeutic Benefit in Skeletal Muscle, but Causes Kidney Toxicity

doi: 10.2119/molmed.2013.00141

Figure Lengend Snippet: Urinalysis from untreated and 8K-NBD peptide-treated mdx mice at multiple time points. Urine samples (7.5 μL) were electrophoresed on a 10% resolving SDS-PAGE gel followed by visualization of separated proteins by Coomassie Blue R-250 staining. Representative urine samples collected after 1 wk of treatment (early urinalysis) and after 4 wks of treatment (final urinalysis) are shown in (A). Immunoblotting for albumin in mouse urine using an anti-mouse albumin antibody is shown in the far right lane of (A), confirming presence of the 68-kDa albumin protein in urine. Densitometric measurements of the 68-kDa albumin band present in all urine samples (see arrow in [A]) is shown in (B) as average band density ± standard error. In (B), an asterisk (*) indicates a significant difference between early urinalysis groups compared with untreated mdx (white bars); two asterisks (**) indicate a significant difference between late urinalysis groups compared with untreated mdx mice (black bars) and § indicates a significant difference between early and late treatment samples in specified treatment groups (p < 0.05). To represent relative amounts and timing of proteinuria in 8K-NBD peptide-treated mdx mice, the total number of protein bands after SDS-PAGE electrophoresis of urine samples from each mouse in the study was quantified and the data is presented as the average number of protein bands present in the gel ± standard error (C). In (C), an asterisk (*) indicates the 8K-NBD peptide treatment group is significantly different than untreated mdx (p < 0.05). In (D), 10 μL urine samples, collected from mdx mice prior to, and 30 min and 24 h after 1, 2 or 3 high-dose, d-8K-wild-type-NBD peptide injections were electrophoresed and stained as in (A) to show early onset of severe proteinuria in this treatment group. Age-matched mdx mice served as the untreated mdx group. n = number of animals per group.

Article Snippet: The albumin band was confirmed by immunoblotting with a 1:1000 diluted goat anti-mouse albumin antibody (Bethyl Laboratories Inc.), followed by a 1:30,000 diluted IRDye 800CW goat anti-mouse IgG (H + L) conjugated secondary antibody (LI-COR Biosciences).

Techniques: SDS Page, Staining, Western Blot, Electrophoresis

Journal: Nature Communications

Article Title: Tailored collagen binding of albumin-fused hyperactive coagulation factor IX dictates in vivo distribution and functional properties

doi: 10.1038/s41467-025-62955-9

Figure Lengend Snippet: a Illustration of the ELISA-based binding assay used to study binding between hFcRn or mFcRn and FIX-HSA variants at pH 5.5. Soluble truncated FcRn (light gray) was captured on IgG1 MST/HN (blue) coated in the well, before FIX-HSA (red/black) was added to the wells, and the HSA region of the fusion protein was detected by an ALP-conjugated anti-HSA antibody (dark gray). b , c Results from the ELISA-based hFcRn and mFcRn binding assays performed at pH 5.5. Data represent the mean ± SD of technical duplicates from one representative experiment. d Illustration of the SPR experiment used to study the interaction between FcRn (gray) and FIX-HSA (orange/black) performed by immobilizing FIX-HSA fusion proteins on a CM5 sensor chip before injecting a truncated form of soluble FcRn in a concentration gradient. Representative sensorgrams from SPR performed by injecting soluble truncated hFcRn ( e – h ) or mFcRn ( i – l ) over immobilized FIX-HSA variants at pH 5.5, showing one out of three independent experiments performed. The dotted lines show curves fitted by the 1:1 Langmuir binding model. m An illustration of the HERA setup designed to study hFcRn-mediated cellular ( n ), uptake and ( o ), recycling of FIX-HSA fusion proteins. Data are presented as relative to FIX-HSA WT (=1, dotted line) and represent the group mean ± SD of three independent experiments performed in technical triplicates (uptake: n = 9, except n = 8 for FIX KA -HSA WT and FIX KR -HSA WT , n = 6 for Padua KR -HSA QMP ; recycling: n = 9, except n = 7 for FIX KA -HSA WT ). Statistical significance was tested by unpaired two-tailed Student’s t tests with 95% confidence level (precise p -values are given in Supplementary Table ). FIX-HSA WT , black; Padua-HSA QMP , gray; FIX KA -HSA WT , blue; FIX KR -HSA WT , orange ; Padua KA -HSA QMP , pink; Padua KR -HSA QMP , purple. Source data are provided as a Source Data file. a , d , m Created in BioRender. Hovden Aaen, K. (2025) https://BioRender.com/auh41ln .

Article Snippet: After incubation for 90 min at 37 °C, the wells were washed as before, and bound proteins were detected by adding a polyclonal goat anti-HSA HRP-conjugated antibody (Bethyl Laboratories, #A80-129P, lot 32) diluted 1:2000 in sample buffer and incubating the wells as before.

Techniques: Enzyme-linked Immunosorbent Assay, Binding Assay, Concentration Assay, Two Tailed Test