Journal: Journal of veterinary diagnostic investigation : official publication of the American Association of Veterinary Laboratory Diagnosticians, Inc

Article Title: Diagnostic gap in Bovine viral diarrhea virus serology during the periparturient period in cattle.

doi: 10.1177/1040638713501172

Figure Lengend Snippet: Figure 2. Bovine immunoglobulin G (IgG) concentrations in serum of 5 cows antepartum (a.p.), at birth (p.), and postpartum (p.p.). For the detailed sampling time points, see Figure 1 (serum neutralization test [SNT]). The total immunoglobulin (IgG) (A), IgG1 (B), and IgG2 (C) concentrations were determined by enzyme-linked immunosorbent assay (ELISA).i Dashed lines highlight animals that showed a diagnostic gap in Bovine viral diarrhea virus (BVDV) antibody ELISAa around parturition. The IgG1-to-IgG2 ratio (D) was calculated for the antepartum serum samples.

Article Snippet: Bovine IgG Quantitation ELISA Set, Bethyl Laboratories Inc., Montgomery, TX. j. Sheep anti-bovine IgG1 antibody, HRP conjugated, Bethyl Laboratories Inc., Montgomery, TX. k. Sheep anti-bovine IgG2 antibody, HRP conjugated, Bethyl Laboratories Inc., Montgomery, TX. l. Purified bovine IgG1, Bethyl Laboratories Inc., Montgomery, TX. m. Purified bovine IgG2, Bethyl Laboratories Inc., Montgomery, TX.

Techniques: Sampling, Neutralization, Enzyme-linked Immunosorbent Assay, Diagnostic Assay, Virus

Journal: Journal of veterinary diagnostic investigation : official publication of the American Association of Veterinary Laboratory Diagnosticians, Inc

Article Title: Diagnostic gap in Bovine viral diarrhea virus serology during the periparturient period in cattle.

doi: 10.1177/1040638713501172

Figure Lengend Snippet: Figure 3. Immunoglobulin G (IgG) class-specific Bovine viral diarrhea virus (BVDV) antibody enzyme-linked immunosorbent assay (ELISA) results (relative optical density [OD] values) in serum of 5 cows antepartum (a.p.), at birth (p.), and postpartum (p.p.). For the detailed sampling time points, see Figure 1 (serum neutralization test [SNT]). The total anti-BVDV IgG (A), anti-BVDV IgG1 (B), and anti-BVDV IgG2 (C) OD values were determined by an adapted in-house ELISA. Dashed lines highlight animals that showed a diagnostic gap in BVDV antibody ELISAa around parturition. The anti-BVDV IgG1-to-IgG2 ratio (D) was calculated for the antepartum serum samples.

Article Snippet: Bovine IgG Quantitation ELISA Set, Bethyl Laboratories Inc., Montgomery, TX. j. Sheep anti-bovine IgG1 antibody, HRP conjugated, Bethyl Laboratories Inc., Montgomery, TX. k. Sheep anti-bovine IgG2 antibody, HRP conjugated, Bethyl Laboratories Inc., Montgomery, TX. l. Purified bovine IgG1, Bethyl Laboratories Inc., Montgomery, TX. m. Purified bovine IgG2, Bethyl Laboratories Inc., Montgomery, TX.

Techniques: Virus, Enzyme-linked Immunosorbent Assay, Sampling, Neutralization, Diagnostic Assay

Journal: Advanced Functional Materials

Article Title: Silica Nanostructures Produced Using Diatom Peptides with Designed Post‐Translational Modifications

doi: 10.1002/adfm.202000849

Figure Lengend Snippet: Figure 2. Production and characterization of recombinant R5 for silica precipitation. a) Scheme for producing and using recombinant R5 for mate- rial synthesis. b) Sodium dodecyl sulfate polyacrylamide gel electrophoresis (SDS-PAGE) and western blot of expression and purification products of recombinant R5 (left to right): molecular weight marker; cell lysate; unbound (untagged protein that did not bind to amylose resin); elution (affinity purified MBP-His-TEV-tagged-R5); 30K retentate (retentate from the 30 kDa spin column containing the cleaved MBP-His-TEV tags); 3K elution (flow through from the 3 kDa spin column showing minimal loss of cleaved R5 peptide); 3K retentate (retentate from the 3 kDa spin column containing the concentrated R5 peptide); recombinant R5 (final purified recombinant R5 peptide); Synthetic R5 (chemically synthesized peptide). The synthesis pro- cess was repeated over 10 times on different days and produced similarly pure peptide. c) Silica synthesized using synthetic and recombinant R5. The images reflect representative data from experiments repeated 8 times on different days. d) Size distributions for synthetic and recombinant R5 silica nanoparticles. Particle size data are representative of experiments repeated 8 times on different days. e) The correlation between silicic acid (TMOS) concentration and the amount of silica precipitated when R5 concentration was held constant at 2.8 × 10−3 m is shown. Additional images are provided in Figure S3 (Supporting Information). The experiment was repeated three times on different days and the mean mass of precipitated silica is shown. The error bars represent the standard deviation across the three replicates. f) SEM micrographs of silica precipitated using 0.5 × 10−3 and 1.0 × 10−3 m R5 peptide, 0 × 10−3 and 30 × 10−3 m phosphate, and 100 × 10−3 m of tetraethyl orthosilicate or Ludox HS as the silica source. Average particle sizes are provided in Table S2 (Supporting Information) and additional SEM micrographs of intermediate concentrations tested are provided in Figure S4 (Supporting Information). All subpanels reflect representative data from experiments repeated on three times on different days.

Article Snippet: The reaction mixture was loaded onto polyacrylamide beads (Bio-Gel P-10, Bio Rad #1504144) for gravity flow size exclusion chromatography (Bio-Rad #7375031) and eluted in 20 × 10−3 m NaCl.

Techniques: Recombinant, Polyacrylamide Gel Electrophoresis, SDS Page, Western Blot, Expressing, Purification, Molecular Weight, Marker, Affinity Purification, Synthesized, Produced, Concentration Assay, Standard Deviation

Journal: Cellular physiology and biochemistry : international journal of experimental cellular physiology, biochemistry, and pharmacology

Article Title: The Regulation of Trophoblastic p53 Homeostasis by the p38-Wip1 Feedback Loop is Disturbed in Placentas from Pregnancies Complicated by Preeclampsia.

doi: 10.33594/000000023

Figure Lengend Snippet: Fig. 2. Wip1 activates p38 and dephosphorylates p53 in trophoblasts under conditions of hypoxia. A: Lentiviral transfection efficiency was examined by FCM and IF. Scale bar 400 µm; B: Wip1 protein expression was confirmed by western blotting, n=4, *P<0.05 vs. scrambled shRNA, one-way ANOVA, Dunnett-t multiple comparison test; C-D. Representative Western blots of p-p38Thr180/Tyr182, p38, cl-cas9, Mdm2, p-p53Ser15, and p53 in HTR8/SVneo cells after 24 h of HII (A) or SIB (B) in the presence of 20 µM GSK2830371 (GSK), DMSO (0.1%), shWip1, or scrambled shRNA (MOI=50). n=4, (*P<0.05, **P<0.01, ***P<0.001, ****P<0.0001, one- way ANOVA, Sidak’s multiple comparisons test. Experiments were performed in triplicate.

Article Snippet: KG Tan et al.: p38-Wip1 Loop Regulates p53 in Trophoblast p38 (1:1000), and cleaved caspase-9 (cl-cas9, 1:1000) were purchased from Cell Signaling Technology (Danvers, USA); p53 (1:2000) and β-actin (1:1000) were purchased from Proteintech (Rosemont, USA); Wip1 (1:1000) and Mdm2 (1:1000) were purchased from Abcam (Cambridge, UK) and Invitrogen (Waltham, USA), respectively.

Techniques: Transfection, Expressing, Western Blot, shRNA, Comparison