Journal: Brain, behavior, and immunity

Article Title: Alcohol Exposure after Mild Focal Traumatic Brain Injury Impairs Neurological Recovery and Exacerbates Localized Neuroinflammation

doi: 10.1016/j.bbi.2014.11.006

Figure Lengend Snippet: Diagram of coronal rat brain section showing the site of injury and photographed region (4 A). Representative immunofluorescence images (10 ×) of ipsilateral cortex GFAP, ED-1, and HMGB1 immunoreactivity (green) combined with DAPI (blue) at 14 days post-TBI (10 days post-alcohol exposure) (4 B).

Article Snippet: Anti-HMGB1 Rabbit polyclonal (Abcam, Cambridge, UK) , 1:100 , Donkey anti-Rabbit Alexa Fluor 488 (Invitrogen, Carlsbad, CA) , 1:200.

Techniques: Immunofluorescence

Journal: Brain, behavior, and immunity

Article Title: Alcohol Exposure after Mild Focal Traumatic Brain Injury Impairs Neurological Recovery and Exacerbates Localized Neuroinflammation

doi: 10.1016/j.bbi.2014.11.006

Figure Lengend Snippet: Quantification of ipsilateral cortex GFAP, ED-1, and HMGB1 immunoreactivity at 14 days post-TBI (10 days post-alcohol exposure). Images are quantified as % area of positive staining in 1.035 mm2 (10×). Values are shown as means ± SEM. For GFAP and ED-1, Sham/Air n = 4, Sham/Alcohol n = 4, TBI/Air n = 4, TBI/Alcohol n = 6. For HMGB1, Sham/Air n = 4, Sham/Alcohol n = 5, TBI/Air n = 5, TBI/Alcohol n = 7 (each n represents the average of 3 images taken from each animal) * p < 0.05 of the TBI groups vs. time-matched sham controls; $ p < 0.05 of the TBI/Alcohol group vs. TBI/Air group, by two-way ANOVA (5 A, 5 C, and 5 E).

Article Snippet: Anti-HMGB1 Rabbit polyclonal (Abcam, Cambridge, UK) , 1:100 , Donkey anti-Rabbit Alexa Fluor 488 (Invitrogen, Carlsbad, CA) , 1:200.

Techniques: Staining

Journal: Brain, behavior, and immunity

Article Title: Alcohol Exposure after Mild Focal Traumatic Brain Injury Impairs Neurological Recovery and Exacerbates Localized Neuroinflammation

doi: 10.1016/j.bbi.2014.11.006

Figure Lengend Snippet: Primary and Secondary Antibodies.

Article Snippet: Anti-HMGB1 Rabbit polyclonal (Abcam, Cambridge, UK) , 1:100 , Donkey anti-Rabbit Alexa Fluor 488 (Invitrogen, Carlsbad, CA) , 1:200.

Techniques: Concentration Assay

Journal: The Journal of biological chemistry

Article Title: Chimeric erythropoietin-interferon gamma receptors reveal differences in functional architecture of intracellular domains for signal transduction.

doi: 10.1074/jbc.272.8.4993

Figure Lengend Snippet: FIG. 7. Phosphorylation of Jak1 and Jak2 kinases. Untreated cells or cells treated with Hu-IFN-g or Epo were lysed and immunoprecipi- tated (I.P.) with monoclonal anti-phosphotyrosine antibodies (anti-P-Tyr panels), polyclonal anti-Jak1 antibodies (anti-Jak1 panels) or anti-Jak2 antibodies (anti-Jak2 panels) as described under “Materials and Methods.” The cell lines are indicated on the figure and are defined in the legend to Fig. 1. Immunoprecipitates were resolved on SDS-PAGE, transferred to PVDF membranes and the blots probed with anti-Jak1 or anti-Jak2 antibodies as noted under the respective horizontal panels.

Article Snippet: Rabbit anti-Jak2 antibody (catalogue no. SC-294) and rabbit anti-Stat5 antibody (catalogue no. SC-835) were from Santa Cruz Biotechnology.

Techniques: Phospho-proteomics, SDS Page

Journal: The Journal of biological chemistry

Article Title: Chimeric erythropoietin-interferon gamma receptors reveal differences in functional architecture of intracellular domains for signal transduction.

doi: 10.1074/jbc.272.8.4993

Figure Lengend Snippet: FIG. 8. Schematic representation of receptor complexes. A represents the IFN-gR1 homodimer bound to IFN-g. The cytoplasmic domains of the two chains are too far apart to permit transactivation of the two Jak1 kinases. B represents the active heteromeric IFN-g receptor com- plex with two IFN-gR1 and two IFN-gR2 subunits per complex. The IFN-g ho- modimer binds to two IFN-gR1 chains, followed by its interaction with two IFN- gR2 chains. The associated Jak2 and Jak1 kinases activate one another by transphosphorylation, with subsequent phosphorylation and dimerization of Stat1a. C depicts the EpoR/gR1 ho- modimer, which, unlike the IFN-gR1 ho- modimer, permits transactivation of the two Jak1 molecules. D illustrates the structure of the heterodimer of EpoR/gR1 and EpoR/gR2, which is the putative ac- tive receptor complex.

Article Snippet: Rabbit anti-Jak2 antibody (catalogue no. SC-294) and rabbit anti-Stat5 antibody (catalogue no. SC-835) were from Santa Cruz Biotechnology.

Techniques: Phospho-proteomics

Journal: Life

Article Title: Anticancer Effects of Weizmannia coagulans MZY531 Postbiotics in CT26 Colorectal Tumor-Bearing Mice by Regulating Apoptosis and Autophagy

doi: 10.3390/life14101334

Figure Lengend Snippet: Western blotting diagram of the effect of W. coagulans MZY531 postbiotics on the expression of apoptosis signaling pathway proteins. ( A ) Bax, Bcl2, and caspase-3 protein expressions in tumor tissue. ( B – D ) Bax, Bcl2, and caspase-3 protein expression gray value. ( E ) Phosphorylation of JAK2 and STAT3 and the expression levels of unphosphorylated JAK2 and STAT3 proteins in tumor tissue. ( F , G ) P-JAK2/JAK2 and P-STAT3/STAT3 protein expression gray value. Statistical analysis was conducted using ANOVA, with subsequent post hoc testing performed via Duncan’s multiple comparison test. Means with different superscript letters (a, b, c, and d) are statistically significantly different from each other ( p < 0.05), with ‘a’ representing the highest value and ‘d’ representing the lowest.

Article Snippet: Following blocking with 5% bovine serum albumin, the membranes were incubated with the appropriate antibodies: β-actin, p-JAK2, STAT3, Bcl-2 and Bax (GeneTex, San Antonio, TX, USA), JAK2, p-STAT3, PI3K, AKT, mTOR and p-mTOR (Bioss, Beijing, China), caspase-3 (Abcam, Cambridge, MA, USA), TGF-β, and SMAD4 (Proteintech, Wuhan, China).

Techniques: Western Blot, Expressing, Phospho-proteomics, Comparison