mouse anti β actin  (Abcam)

 
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    Name:
    Anti beta Actin antibody AC 15
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    ab6276
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    Structured Review

    Abcam mouse anti β actin
    Human prostate cancer cells express lower levels of ADAM19 than normal prostate epithelial cells. a Western blotting for ADAM19 protein in androgen-sensitive human LNCaP cells and RWPE-1 cells. <t>β-actin</t> was used as a control. b ADAM19 protein expression in LNCaP and RWPE-1 cells as determined by immunocytochemistry. 100x magnification. Insert shows cytoplasmic staining

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    Images

    1) Product Images from "Genetic and cellular studies highlight that A Disintegrin and Metalloproteinase 19 is a protective biomarker in human prostate cancer"

    Article Title: Genetic and cellular studies highlight that A Disintegrin and Metalloproteinase 19 is a protective biomarker in human prostate cancer

    Journal: BMC Cancer

    doi: 10.1186/s12885-016-2178-4

    Human prostate cancer cells express lower levels of ADAM19 than normal prostate epithelial cells. a Western blotting for ADAM19 protein in androgen-sensitive human LNCaP cells and RWPE-1 cells. β-actin was used as a control. b ADAM19 protein expression in LNCaP and RWPE-1 cells as determined by immunocytochemistry. 100x magnification. Insert shows cytoplasmic staining
    Figure Legend Snippet: Human prostate cancer cells express lower levels of ADAM19 than normal prostate epithelial cells. a Western blotting for ADAM19 protein in androgen-sensitive human LNCaP cells and RWPE-1 cells. β-actin was used as a control. b ADAM19 protein expression in LNCaP and RWPE-1 cells as determined by immunocytochemistry. 100x magnification. Insert shows cytoplasmic staining

    Techniques Used: Western Blot, Expressing, Immunocytochemistry, Staining

    2) Product Images from "Loss of the chromatin regulator MRG15 limits neural stem/progenitor cell proliferation via increased expression of the p21 Cdk inhibitor"

    Article Title: Loss of the chromatin regulator MRG15 limits neural stem/progenitor cell proliferation via increased expression of the p21 Cdk inhibitor

    Journal: Stem cell research

    doi: 10.1016/j.scr.2011.04.002

    Defects of RAD51 focus formation in Mrg15 deficient NSCs after IR exposure Wild-type ( A ) and Mrg15 deficient ( B ) NSCs were fixed with or without IR at 180 min post exposure, co-stained with rabbit anti-RAD51 (green) and mouse anti-γH2AX (red) antibodies, and counterstained with DAPI to visualize nuclei. Representative pictures for colocalization of RAD51 and γH2AX in merged images are shown with separated pictures. Representative cells from two experiments are shown. (C) Quantification of cells with the RAD51 foci at 180 minutes after IR (mean ± SEM, n=5). P values determined using unpaired t test. ( D ) Detection of RAD51 expression level by Western blot. Total cell lysates were prepared from NSCs with or without IR at 180 min post exposure and levels of RAD51 and β-actin (loading control) were detected by Western blot.
    Figure Legend Snippet: Defects of RAD51 focus formation in Mrg15 deficient NSCs after IR exposure Wild-type ( A ) and Mrg15 deficient ( B ) NSCs were fixed with or without IR at 180 min post exposure, co-stained with rabbit anti-RAD51 (green) and mouse anti-γH2AX (red) antibodies, and counterstained with DAPI to visualize nuclei. Representative pictures for colocalization of RAD51 and γH2AX in merged images are shown with separated pictures. Representative cells from two experiments are shown. (C) Quantification of cells with the RAD51 foci at 180 minutes after IR (mean ± SEM, n=5). P values determined using unpaired t test. ( D ) Detection of RAD51 expression level by Western blot. Total cell lysates were prepared from NSCs with or without IR at 180 min post exposure and levels of RAD51 and β-actin (loading control) were detected by Western blot.

    Techniques Used: Staining, Expressing, Western Blot

    p21 protein accumulation in NSC cultures A representative Western blot of p21 is shown. Total cell lysates were prepared from first or sixth passage of neurospheres from three wild-type and three Mrg15 deficient embryos. Equal amounts of protein was loaded, transferred to nitrocellulose membrane, and probed with antibodies for p21 and β-actin (loading control).
    Figure Legend Snippet: p21 protein accumulation in NSC cultures A representative Western blot of p21 is shown. Total cell lysates were prepared from first or sixth passage of neurospheres from three wild-type and three Mrg15 deficient embryos. Equal amounts of protein was loaded, transferred to nitrocellulose membrane, and probed with antibodies for p21 and β-actin (loading control).

    Techniques Used: Western Blot

    p21 shRNA rescues cell proliferation in early passage (1st) Mrg15 deficient NSCs and late passage (6th) wild-type NSCs (A) Cells expressing empty vector (EV) or p21 shRNA were analyzed by Western blot to p21, β-actin (loading control), GFP (indication of infection efficiency), and MRG15. (B, C) Representative BrdU immunostaining in Mrg15 deficient cells (B) at first passage and wild-type cells (C) at sixth passage. Single cells were plated on poly-L-lysine- coated coverslips, grown for 48 h, and incubated with 10 μM BrdU for 1 h. Incorporated BrdU was detected by mouse anti-BrdU antibody followed by incubation with biotinylated anti-mouse IgG and positive cells identified by DAB staining. The percentage of positive cells was determined by counting under a light microscope. Error bars represent standard error of mean (SEM) of triplicate counts and P values determined using unpaired t test. (D, E, F, G) Cell cycle distribution of GEF-positive Mrg15 deficient and wild-type NSCs after infection with a GFP-expressing lentivirus containing empty vector or a p21 shRNA construct. (D) Mrg15 deficient NSCs with empty vector. (E) Mrg15 deficient NSCs with p21 shRNA construct. (F) wild-type NSCs with empty vector. (G) wild-type NSCs with p21 shRNA construct.
    Figure Legend Snippet: p21 shRNA rescues cell proliferation in early passage (1st) Mrg15 deficient NSCs and late passage (6th) wild-type NSCs (A) Cells expressing empty vector (EV) or p21 shRNA were analyzed by Western blot to p21, β-actin (loading control), GFP (indication of infection efficiency), and MRG15. (B, C) Representative BrdU immunostaining in Mrg15 deficient cells (B) at first passage and wild-type cells (C) at sixth passage. Single cells were plated on poly-L-lysine- coated coverslips, grown for 48 h, and incubated with 10 μM BrdU for 1 h. Incorporated BrdU was detected by mouse anti-BrdU antibody followed by incubation with biotinylated anti-mouse IgG and positive cells identified by DAB staining. The percentage of positive cells was determined by counting under a light microscope. Error bars represent standard error of mean (SEM) of triplicate counts and P values determined using unpaired t test. (D, E, F, G) Cell cycle distribution of GEF-positive Mrg15 deficient and wild-type NSCs after infection with a GFP-expressing lentivirus containing empty vector or a p21 shRNA construct. (D) Mrg15 deficient NSCs with empty vector. (E) Mrg15 deficient NSCs with p21 shRNA construct. (F) wild-type NSCs with empty vector. (G) wild-type NSCs with p21 shRNA construct.

    Techniques Used: shRNA, Expressing, Plasmid Preparation, Western Blot, Infection, Immunostaining, Incubation, Staining, Light Microscopy, Construct

    Accumulation of activated p53 in Mrg15 deficient NSC cultures and effects of p53 shRNA knockdown (A) A representative Western blot analysis of phosphorylated p53 at Ser15 is shown. Total cell lysates were prepared from early passage neurospheres from three wild-type and five Mrg15 deficient embryos. Equal amounts of protein was loaded, transferred to nitrocellulose membrane, and probed with antibodies for phospho-p53 (Ser15), p53, p21, MRG15, and β-actin (loading control). (B) Mrg15 deficient NSCs expressing empty vector (EV) or p53 shRNA were analyzed by Western blot to p53 and β-actin (loading control). (C) Percentage of BrdU positive cells in early passage of Mrg15 deficient NSCs after lentivirus infection expressing EV or p53 shRNA. The percentage of BrdU positive cells by immunostaining was determined by counting under a light microscope. Error bars represent standard error of mean (SEM) of counts from ten fields and P values determined using unpaired t test. (D) Percentage of p21 positive cells in early passage of Mrg15 deficient NSCs after lentivirus infection expressing EV or p53 shRNA. The percentage of p21 positive cells by immunostaining was determined by counting under a light microscope. Error bars represent standard error of mean (SEM) of counts from ten fields and P values determined using unpaired t test.
    Figure Legend Snippet: Accumulation of activated p53 in Mrg15 deficient NSC cultures and effects of p53 shRNA knockdown (A) A representative Western blot analysis of phosphorylated p53 at Ser15 is shown. Total cell lysates were prepared from early passage neurospheres from three wild-type and five Mrg15 deficient embryos. Equal amounts of protein was loaded, transferred to nitrocellulose membrane, and probed with antibodies for phospho-p53 (Ser15), p53, p21, MRG15, and β-actin (loading control). (B) Mrg15 deficient NSCs expressing empty vector (EV) or p53 shRNA were analyzed by Western blot to p53 and β-actin (loading control). (C) Percentage of BrdU positive cells in early passage of Mrg15 deficient NSCs after lentivirus infection expressing EV or p53 shRNA. The percentage of BrdU positive cells by immunostaining was determined by counting under a light microscope. Error bars represent standard error of mean (SEM) of counts from ten fields and P values determined using unpaired t test. (D) Percentage of p21 positive cells in early passage of Mrg15 deficient NSCs after lentivirus infection expressing EV or p53 shRNA. The percentage of p21 positive cells by immunostaining was determined by counting under a light microscope. Error bars represent standard error of mean (SEM) of counts from ten fields and P values determined using unpaired t test.

    Techniques Used: shRNA, Western Blot, Expressing, Plasmid Preparation, Infection, Immunostaining, Light Microscopy

    Increased expression of p21, but not p16/p19 expression, in early passage E10.5 Mrg15 deficient NSC cultures mRNA expression levels of p21 ( A ), p16INK4a (B ), and 19ARF ( C ) genes was measured by qRT-PCR from three wild-type and three Mrg15 deficient NSC cultures. Data was normalized to expression levels of the β-actin gene. Each data represents the average of three independent assays (mean ± SEM).
    Figure Legend Snippet: Increased expression of p21, but not p16/p19 expression, in early passage E10.5 Mrg15 deficient NSC cultures mRNA expression levels of p21 ( A ), p16INK4a (B ), and 19ARF ( C ) genes was measured by qRT-PCR from three wild-type and three Mrg15 deficient NSC cultures. Data was normalized to expression levels of the β-actin gene. Each data represents the average of three independent assays (mean ± SEM).

    Techniques Used: Expressing, Quantitative RT-PCR

    3) Product Images from "Local Translation of Extranuclear Lamin B Promotes Axon Maintenance"

    Article Title: Local Translation of Extranuclear Lamin B Promotes Axon Maintenance

    Journal: Cell

    doi: 10.1016/j.cell.2011.11.064

    Axonal Translation of lb2 mRNA Is Selectively Regulated, Related to Figure 4 (A–C) One hour En-1 stimulation does not induce translation of β-actin mRNA, which is localized to RGC axons. ns: not significant; unpaired t test. (D) Lb2 mRNA is expressed at a similar level in the eye to other mRNAs encoding nuclear proteins as revealed by quantitatve RT-PCR. (E) Axon-TRAP analysis shows that other lamin mRNAs are not associated with ribosomes in RGC axons in vivo. Scale bar, 5 μm.
    Figure Legend Snippet: Axonal Translation of lb2 mRNA Is Selectively Regulated, Related to Figure 4 (A–C) One hour En-1 stimulation does not induce translation of β-actin mRNA, which is localized to RGC axons. ns: not significant; unpaired t test. (D) Lb2 mRNA is expressed at a similar level in the eye to other mRNAs encoding nuclear proteins as revealed by quantitatve RT-PCR. (E) Axon-TRAP analysis shows that other lamin mRNAs are not associated with ribosomes in RGC axons in vivo. Scale bar, 5 μm.

    Techniques Used: Reverse Transcription Polymerase Chain Reaction, In Vivo

    4) Product Images from "Suitability of Nicotinic Acetylcholine Receptor α7 and Muscarinic Acetylcholine Receptor 3 Antibodies for Immune Detection"

    Article Title: Suitability of Nicotinic Acetylcholine Receptor α7 and Muscarinic Acetylcholine Receptor 3 Antibodies for Immune Detection

    Journal: Journal of Histochemistry and Cytochemistry

    doi: 10.1369/0022155415575028

    Chrna7 (ab23832) Antibody Shows the Same Staining Pattern as That for β-actin, but Not for β-enolase, in Mast Cells
    Figure Legend Snippet: Chrna7 (ab23832) Antibody Shows the Same Staining Pattern as That for β-actin, but Not for β-enolase, in Mast Cells

    Techniques Used: Staining

    5) Product Images from "Macroautophagy Proteins Assist Epstein Barr Virus Production and Get Incorporated Into the Virus Particles"

    Article Title: Macroautophagy Proteins Assist Epstein Barr Virus Production and Get Incorporated Into the Virus Particles

    Journal: EBioMedicine

    doi: 10.1016/j.ebiom.2014.11.007

    Autophagic membrane accumulation in EBV producing cells. (A) Human AKBM cells were incubated with anti-human IgG F(ab) 2 fragments for 2 h. Atg8/LC3 and β-actin protein levels were assessed after 20 h by Western blot. In parallel, 50 μM chloroquine (CQ) was supplemented during the final 6 h of incubation. Numbers below blots indicate fold change of LC3-II/β-actin ratio normalized to latent AKBM sample. Blot represents 12 individual experiments. (B) Densitometry quantification of LC3-II bands normalized to their corresponding β-actin levels in latent (− IgG) and lytic (+ IgG) AKBM cells (n = 12). Data are expressed as means ± SD; paired t test; *, P
    Figure Legend Snippet: Autophagic membrane accumulation in EBV producing cells. (A) Human AKBM cells were incubated with anti-human IgG F(ab) 2 fragments for 2 h. Atg8/LC3 and β-actin protein levels were assessed after 20 h by Western blot. In parallel, 50 μM chloroquine (CQ) was supplemented during the final 6 h of incubation. Numbers below blots indicate fold change of LC3-II/β-actin ratio normalized to latent AKBM sample. Blot represents 12 individual experiments. (B) Densitometry quantification of LC3-II bands normalized to their corresponding β-actin levels in latent (− IgG) and lytic (+ IgG) AKBM cells (n = 12). Data are expressed as means ± SD; paired t test; *, P

    Techniques Used: Incubation, Western Blot

    6) Product Images from "Motor dysfunction in cerebellar Purkinje cell-specific vesicular GABA transporter knockout mice"

    Article Title: Motor dysfunction in cerebellar Purkinje cell-specific vesicular GABA transporter knockout mice

    Journal: Frontiers in Cellular Neuroscience

    doi: 10.3389/fncel.2013.00286

    Significant reduction in VGAT protein and unaltered levels of other pre- and postsynaptic proteins in the L7-VGAT DCN. Western blot analyses of GAT3, β-actin, calbindin, gephyrin, GABA A Rα1, and parvalbumin proteins in the crude fractions from control and L7-VGAT DCN and cerebellar cortices at P40W. DCN, deep cerebellar nuclei; and CC, cerebellar cortex.
    Figure Legend Snippet: Significant reduction in VGAT protein and unaltered levels of other pre- and postsynaptic proteins in the L7-VGAT DCN. Western blot analyses of GAT3, β-actin, calbindin, gephyrin, GABA A Rα1, and parvalbumin proteins in the crude fractions from control and L7-VGAT DCN and cerebellar cortices at P40W. DCN, deep cerebellar nuclei; and CC, cerebellar cortex.

    Techniques Used: Western Blot

    7) Product Images from "CSB interacts with SNM1A and promotes DNA interstrand crosslink processing"

    Article Title: CSB interacts with SNM1A and promotes DNA interstrand crosslink processing

    Journal: Nucleic Acids Research

    doi: 10.1093/nar/gku1279

    Sensitivity of cycling and non-cycling CSB-deficient SH-SY5Y cells to DNA-damaging agents. ( A ) Expression of CSB protein in cycling and non-cycling scramble shRNA or CSB shRNA SH-SY5Y cells. CSB protein level was determined in whole cell extracts (μg amount designated) by western blotting (left), in comparison to GAPDH and β-actin. The relative ratio of CSB to the indicated standard is shown (right; from a representative gel), with the scramble control line being set as 1. ( B ) UV sensitivity of cycling and non-cycling scramble shRNA and CSB shRNA SH-SY5Y cells. Cell viability was quantified after UVC irradiation (0, 2.5, 5, 7.5 or 10 J/m 2 ) by hemocytometer analysis. Reported is the ratio of the cell count determined at the indicated UVC dose in comparison to the untreated control sample. ( C ) Viability of cycling and non-cycling scramble shRNA and CSB shRNA SH-SY5Y cells treated with angelicin (cycling cells, 0.04–20 μM; non-cycling cells, 0.08–20 μM) and UVA. Viability was measured using a WST-8 assay 72 h after treatment. Results are presented as the ratio of the value obtained at the indicated concentration of angelicin relative to that of the untreated (UVA only) cells. ( D ) Viability of cycling and non-cycling scramble shRNA and CSB shRNA SH-SY5Y cells treated with trioxsalen (cycling cells, 0.15–20 nM; non-cycling cells, 1.25–80 nM) and UVA. See panel C for further details. The data in panels B–D represent the mean ± SD from three independent experiments. The statistical analysis of each graph was performed by two-way ANOVA followed by the Bonferroni post hoc test (* P
    Figure Legend Snippet: Sensitivity of cycling and non-cycling CSB-deficient SH-SY5Y cells to DNA-damaging agents. ( A ) Expression of CSB protein in cycling and non-cycling scramble shRNA or CSB shRNA SH-SY5Y cells. CSB protein level was determined in whole cell extracts (μg amount designated) by western blotting (left), in comparison to GAPDH and β-actin. The relative ratio of CSB to the indicated standard is shown (right; from a representative gel), with the scramble control line being set as 1. ( B ) UV sensitivity of cycling and non-cycling scramble shRNA and CSB shRNA SH-SY5Y cells. Cell viability was quantified after UVC irradiation (0, 2.5, 5, 7.5 or 10 J/m 2 ) by hemocytometer analysis. Reported is the ratio of the cell count determined at the indicated UVC dose in comparison to the untreated control sample. ( C ) Viability of cycling and non-cycling scramble shRNA and CSB shRNA SH-SY5Y cells treated with angelicin (cycling cells, 0.04–20 μM; non-cycling cells, 0.08–20 μM) and UVA. Viability was measured using a WST-8 assay 72 h after treatment. Results are presented as the ratio of the value obtained at the indicated concentration of angelicin relative to that of the untreated (UVA only) cells. ( D ) Viability of cycling and non-cycling scramble shRNA and CSB shRNA SH-SY5Y cells treated with trioxsalen (cycling cells, 0.15–20 nM; non-cycling cells, 1.25–80 nM) and UVA. See panel C for further details. The data in panels B–D represent the mean ± SD from three independent experiments. The statistical analysis of each graph was performed by two-way ANOVA followed by the Bonferroni post hoc test (* P

    Techniques Used: Expressing, shRNA, Western Blot, Irradiation, Cell Counting, Concentration Assay

    8) Product Images from "Altered Sensory Experience Exacerbates Stable Dendritic Spine and Synapse Loss in a Mouse Model of Huntington's Disease"

    Article Title: Altered Sensory Experience Exacerbates Stable Dendritic Spine and Synapse Loss in a Mouse Model of Huntington's Disease

    Journal: The Journal of Neuroscience

    doi: 10.1523/JNEUROSCI.0244-14.2015

    Reduced level of postsynaptic scaffolding protein PSD-95 in the R6/2 mice compared with the wild-type littermates. A , B , Quantification of normalized total PSD-95 protein: normalized to β-actin ( A ) and to α-tubulin ( B ) in the barrel cortex of R6/2 and wild-type mice at 6, 8, and 12 weeks. Data from deprived (contralateral hemisphere) and spared (ipsilateral hemisphere) cortices are pooled, since no significant differences were observed between the hemispheres. At all ages analyzed, R6/2 mice display significant reduction in PSD-95 protein levels compared with the wild-type littermates. Notice that already at week 6 (presymptomatic phase), R6/2 mice display significant reductions in PSD-95 levels compared with the wild-types littermates. C , Quantification of normalized total β-actin levels in the barrel cortex of R6/2 and wild-type mice at 6, 8, and 12 weeks. Data from deprived (contralateral hemisphere) and spared (ipsilateral hemisphere) cortices are pooled, since no significant differences were observed between the hemispheres. Note that at all ages analyzed, there is no significant difference in the expression of β-actin protein (relative to α-tubulin) in the brain samples of R6/2 mice compared with wild-type littermates. D , Western blot image comparing PSD-95 and β-actin protein levels (relative to α-tubulin levels) independently at different ages, as follows: 6, 8, and 12 weeks in the deprived and spared cortices of wild-type and R6/2 mice. A reduced level of PSD-95 is evident at weeks 6, 8, and 12 in both the deprived barrel cortex as well as the spared barrel cortex of R6/2 mice (no difference between hemispheres) compared with wild-type mice. Dpr, Deprived cortex; Spr, spared cortex. E , F , Quantification of normalized PSD-95 ( E ) and β-actin ( F ) levels in the synaptosomal fraction of R6/2 mice compared with wild-type littermates at weeks 6, 8, and 12. PSD-95 and β-actin levels are normalized to α-tubulin. Significant reductions in PSD-95 and β-actin protein levels are evident in the synaptosome of R6/2 mice compared with wild-type littermates at all ages. G–I , Western blot image representing the expression level of PSD-95 and β-actin (relative to α-tubulin) in the synaptosomal fraction of R6/2 mice compared with wild-type littermates at weeks 6 ( G ), 8 ( H ), and 12 ( I ). At all ages, significantly lower levels of PSD-95 and β-actin are observed in the synaptosome of R6/2 mice compared with the wild-type littermates. N = 3 mice/group. Data are presented as the mean ± SEM. Means were considered to be statistically significant at p
    Figure Legend Snippet: Reduced level of postsynaptic scaffolding protein PSD-95 in the R6/2 mice compared with the wild-type littermates. A , B , Quantification of normalized total PSD-95 protein: normalized to β-actin ( A ) and to α-tubulin ( B ) in the barrel cortex of R6/2 and wild-type mice at 6, 8, and 12 weeks. Data from deprived (contralateral hemisphere) and spared (ipsilateral hemisphere) cortices are pooled, since no significant differences were observed between the hemispheres. At all ages analyzed, R6/2 mice display significant reduction in PSD-95 protein levels compared with the wild-type littermates. Notice that already at week 6 (presymptomatic phase), R6/2 mice display significant reductions in PSD-95 levels compared with the wild-types littermates. C , Quantification of normalized total β-actin levels in the barrel cortex of R6/2 and wild-type mice at 6, 8, and 12 weeks. Data from deprived (contralateral hemisphere) and spared (ipsilateral hemisphere) cortices are pooled, since no significant differences were observed between the hemispheres. Note that at all ages analyzed, there is no significant difference in the expression of β-actin protein (relative to α-tubulin) in the brain samples of R6/2 mice compared with wild-type littermates. D , Western blot image comparing PSD-95 and β-actin protein levels (relative to α-tubulin levels) independently at different ages, as follows: 6, 8, and 12 weeks in the deprived and spared cortices of wild-type and R6/2 mice. A reduced level of PSD-95 is evident at weeks 6, 8, and 12 in both the deprived barrel cortex as well as the spared barrel cortex of R6/2 mice (no difference between hemispheres) compared with wild-type mice. Dpr, Deprived cortex; Spr, spared cortex. E , F , Quantification of normalized PSD-95 ( E ) and β-actin ( F ) levels in the synaptosomal fraction of R6/2 mice compared with wild-type littermates at weeks 6, 8, and 12. PSD-95 and β-actin levels are normalized to α-tubulin. Significant reductions in PSD-95 and β-actin protein levels are evident in the synaptosome of R6/2 mice compared with wild-type littermates at all ages. G–I , Western blot image representing the expression level of PSD-95 and β-actin (relative to α-tubulin) in the synaptosomal fraction of R6/2 mice compared with wild-type littermates at weeks 6 ( G ), 8 ( H ), and 12 ( I ). At all ages, significantly lower levels of PSD-95 and β-actin are observed in the synaptosome of R6/2 mice compared with the wild-type littermates. N = 3 mice/group. Data are presented as the mean ± SEM. Means were considered to be statistically significant at p

    Techniques Used: Scaffolding, Mouse Assay, Expressing, Western Blot, SPR Assay

    9) Product Images from "Investigation of 3T3-L1 Cell Differentiation to Adipocyte, Affected by Aqueous Seed Extract of Phoenix Dactylifera L"

    Article Title: Investigation of 3T3-L1 Cell Differentiation to Adipocyte, Affected by Aqueous Seed Extract of Phoenix Dactylifera L

    Journal: Reports of Biochemistry & Molecular Biology

    doi: 10.29252/rbmb.9.1.14

    Effect of extract on protein expression of GLUT4, Akt2, and phospho-Akt2. Differentiated 3T3-L1 cells in medium with or without extract (0.312-1.25 mg/ml). On day 12, GLUT4, Akt2, and phospho-Akt2 levels were assessed via western blot on PVDF membranes. (A) Representative blots are shown. Results demonstrate no effect of extract (0.312, 0.625, and 1.25 mg/ml) on GLUT4, Akt2 and phospho-Akt2 levels in treated groups (B). Data are represented as the mean ± SD of three independent experiments and were normalized to β-actin levels.
    Figure Legend Snippet: Effect of extract on protein expression of GLUT4, Akt2, and phospho-Akt2. Differentiated 3T3-L1 cells in medium with or without extract (0.312-1.25 mg/ml). On day 12, GLUT4, Akt2, and phospho-Akt2 levels were assessed via western blot on PVDF membranes. (A) Representative blots are shown. Results demonstrate no effect of extract (0.312, 0.625, and 1.25 mg/ml) on GLUT4, Akt2 and phospho-Akt2 levels in treated groups (B). Data are represented as the mean ± SD of three independent experiments and were normalized to β-actin levels.

    Techniques Used: Expressing, Western Blot

    Effect of extract on the gene expression of adipocyte-specific genes during differentiation of 3T3-L1 cells into mature adipocytes. 3T3-L1 cells differentiation in medium with or without extract (0.312, 0.625, and 1.25 mg/ml). On day 5, 8, 12, mRNA was extracted and the gene expression of PPAR-γ, CEBP-α, aP2, FAS, ACACA, and UCP1 genes were evaluated using Q-PCR; PPAR-γ: peroxisome proliferator-activated receptor-γ; CEBP-α: CCAAT/enhancer-binding protein-alpha; aP2: Adipocyte protein 2; ACACA: Acetyl-CoA Carboxylase- Alpha; FAS: Fatty acid synthase; UCP1; uncoupling protein. Data are represented as the mean ± SD of three independent experiments and were normalized to β-actin levels (*p
    Figure Legend Snippet: Effect of extract on the gene expression of adipocyte-specific genes during differentiation of 3T3-L1 cells into mature adipocytes. 3T3-L1 cells differentiation in medium with or without extract (0.312, 0.625, and 1.25 mg/ml). On day 5, 8, 12, mRNA was extracted and the gene expression of PPAR-γ, CEBP-α, aP2, FAS, ACACA, and UCP1 genes were evaluated using Q-PCR; PPAR-γ: peroxisome proliferator-activated receptor-γ; CEBP-α: CCAAT/enhancer-binding protein-alpha; aP2: Adipocyte protein 2; ACACA: Acetyl-CoA Carboxylase- Alpha; FAS: Fatty acid synthase; UCP1; uncoupling protein. Data are represented as the mean ± SD of three independent experiments and were normalized to β-actin levels (*p

    Techniques Used: Expressing, Polymerase Chain Reaction, Binding Assay

    10) Product Images from "Neurodevelopmental Role for VGLUT2 in Pyramidal Neuron Plasticity, Dendritic Refinement, and in Spatial Learning"

    Article Title: Neurodevelopmental Role for VGLUT2 in Pyramidal Neuron Plasticity, Dendritic Refinement, and in Spatial Learning

    Journal: The Journal of neuroscience : the official journal of the Society for Neuroscience

    doi: 10.1523/JNEUROSCI.4505-11.2012

    Reduced hippocampal expression of VGLUT1 and spinophilin in adult Emx1-Cre +/+ /VGLUT2 fx/fx mice. A, Western blot of vesicle-enriched membranes (μg membrane protein) from (1) VGLUT1 (2 μg), (2) VIAAT (4 μg), (3) spinophilin (50 μg), (4) GAD67 (50 μg), (5) PSD95 (50 μg), and (6) β-actin (4 μg). Total hippocampal protein extracts were prepared from 3 mice in each group. B, Quantitation of bands by densitometry. Results are expressed as a ratio of VGLUT1, VIAAT, spinophilin, and GAD67 against β-actin or against PSD95, which did not differ between adult Emx1-Cre +/+ /VGLUT2 fx/fx and control VGLUT2 fx/fx mice. Error bars represent s.e.m. * P
    Figure Legend Snippet: Reduced hippocampal expression of VGLUT1 and spinophilin in adult Emx1-Cre +/+ /VGLUT2 fx/fx mice. A, Western blot of vesicle-enriched membranes (μg membrane protein) from (1) VGLUT1 (2 μg), (2) VIAAT (4 μg), (3) spinophilin (50 μg), (4) GAD67 (50 μg), (5) PSD95 (50 μg), and (6) β-actin (4 μg). Total hippocampal protein extracts were prepared from 3 mice in each group. B, Quantitation of bands by densitometry. Results are expressed as a ratio of VGLUT1, VIAAT, spinophilin, and GAD67 against β-actin or against PSD95, which did not differ between adult Emx1-Cre +/+ /VGLUT2 fx/fx and control VGLUT2 fx/fx mice. Error bars represent s.e.m. * P

    Techniques Used: Expressing, Mouse Assay, Western Blot, Quantitation Assay

    11) Product Images from "DDX5 promotes gastric cancer cell proliferation in vitro and in vivo through mTOR signaling pathway"

    Article Title: DDX5 promotes gastric cancer cell proliferation in vitro and in vivo through mTOR signaling pathway

    Journal: Scientific Reports

    doi: 10.1038/srep42876

    Expression of DDX5 positively correlated with p-mTOR in gastric cancer specimens. ( A ) Representative images of immunoblots of DDX5 and p-mTOR(S2448) in 65 gastric cancer specimens. β-actin was used as loading control. ( B ) Correlation analysis of the relative expression of DDX5 and p-mTOR(S2448).
    Figure Legend Snippet: Expression of DDX5 positively correlated with p-mTOR in gastric cancer specimens. ( A ) Representative images of immunoblots of DDX5 and p-mTOR(S2448) in 65 gastric cancer specimens. β-actin was used as loading control. ( B ) Correlation analysis of the relative expression of DDX5 and p-mTOR(S2448).

    Techniques Used: Expressing, Western Blot

    DDX5 regulates the mTOR signaling in gastric cancer cells. ( A ) Western blot analysis of the expression of DDX5, p-mTOR(S2448), mTOR, p-S6K1(T389) and S6K1 in the indicated gastric cancer cells in response to DDX5 up-regulation or down-regulation. β-actin was used as loading control. ( B ) Relative quantification of the indicated proteins by densitometric analysis of the bands. All the experiments were performed in triplicate. *p
    Figure Legend Snippet: DDX5 regulates the mTOR signaling in gastric cancer cells. ( A ) Western blot analysis of the expression of DDX5, p-mTOR(S2448), mTOR, p-S6K1(T389) and S6K1 in the indicated gastric cancer cells in response to DDX5 up-regulation or down-regulation. β-actin was used as loading control. ( B ) Relative quantification of the indicated proteins by densitometric analysis of the bands. All the experiments were performed in triplicate. *p

    Techniques Used: Western Blot, Expressing

    Suppression of mTOR signaling abrogates DDX5-induced cell proliferation. ( A,B ) Western blot analysis of DDX5, p-mTOR(S2448), mTOR, p-S6K1(T389) and S6K1 in DDX5 or Vector transfected KATO III and NCI-N87 cells incubated with the indicated concentration of everolimus (EVE) or DMSO for 48 hr. β-actin was used as loading control. ( C,D ) CCK-8 analysis of gastric cancer cell proliferation in the presence or absence of everolimus for 48 hr (*p
    Figure Legend Snippet: Suppression of mTOR signaling abrogates DDX5-induced cell proliferation. ( A,B ) Western blot analysis of DDX5, p-mTOR(S2448), mTOR, p-S6K1(T389) and S6K1 in DDX5 or Vector transfected KATO III and NCI-N87 cells incubated with the indicated concentration of everolimus (EVE) or DMSO for 48 hr. β-actin was used as loading control. ( C,D ) CCK-8 analysis of gastric cancer cell proliferation in the presence or absence of everolimus for 48 hr (*p

    Techniques Used: Western Blot, Plasmid Preparation, Transfection, Incubation, Concentration Assay, CCK-8 Assay

    12) Product Images from "Downregulation of Glutathione S-transferase A1 suppressed tumor growth and induced cell apoptosis in A549 cell line"

    Article Title: Downregulation of Glutathione S-transferase A1 suppressed tumor growth and induced cell apoptosis in A549 cell line

    Journal: Oncology Letters

    doi: 10.3892/ol.2018.8608

    GSTA1 protein and mRNA expression in si-GSTA1 and si-control A549 cells. (A) The expression of GSTA1 was determined by western blot analysis. β-actin served as a loading control. (B) GSTA1 mRNA levels in si-GSTA1 and si-control A549 cells were detected by a reverse transcription-quantitative polymerase chain reaction assay. GAPDH served as a loading control. Data are presented as the mean + standard deviation. *P
    Figure Legend Snippet: GSTA1 protein and mRNA expression in si-GSTA1 and si-control A549 cells. (A) The expression of GSTA1 was determined by western blot analysis. β-actin served as a loading control. (B) GSTA1 mRNA levels in si-GSTA1 and si-control A549 cells were detected by a reverse transcription-quantitative polymerase chain reaction assay. GAPDH served as a loading control. Data are presented as the mean + standard deviation. *P

    Techniques Used: Expressing, Western Blot, Real-time Polymerase Chain Reaction, Standard Deviation

    GSTA1 protein, mRNA expression in GSTA1 and vector A549 cells. (A) The expression of GSTA1 was determined by western blot analysis. β-actin served as a loading control. (B) GSTA1 mRNA levels in GSTA1 and vector A549 cells were detected by a reverse transcription-quantitative polymerase chain reaction assay. GAPDH served as a loading control. Data are presented as the mean + standard deviation. *P
    Figure Legend Snippet: GSTA1 protein, mRNA expression in GSTA1 and vector A549 cells. (A) The expression of GSTA1 was determined by western blot analysis. β-actin served as a loading control. (B) GSTA1 mRNA levels in GSTA1 and vector A549 cells were detected by a reverse transcription-quantitative polymerase chain reaction assay. GAPDH served as a loading control. Data are presented as the mean + standard deviation. *P

    Techniques Used: Expressing, Plasmid Preparation, Western Blot, Real-time Polymerase Chain Reaction, Standard Deviation

    GSTA1 protein and mRNA expression levels of tumors in vivo . The four groups included vector, GSTA1, si-control and si-GSTA1. (A) GSTA1 protein expression levels were detected by western blotting. β-actin served as a loading control. (B) Reverse transcription-quantitative polymerase chain reaction was applied to detect the relative GSTA1 mRNA expression in vivo . Data are presented as the mean + standard deviation, *P
    Figure Legend Snippet: GSTA1 protein and mRNA expression levels of tumors in vivo . The four groups included vector, GSTA1, si-control and si-GSTA1. (A) GSTA1 protein expression levels were detected by western blotting. β-actin served as a loading control. (B) Reverse transcription-quantitative polymerase chain reaction was applied to detect the relative GSTA1 mRNA expression in vivo . Data are presented as the mean + standard deviation, *P

    Techniques Used: Expressing, In Vivo, Plasmid Preparation, Western Blot, Real-time Polymerase Chain Reaction, Standard Deviation

    13) Product Images from "The co-chaperone p23 promotes prostate cancer motility and metastasis"

    Article Title: The co-chaperone p23 promotes prostate cancer motility and metastasis

    Journal: Molecular Oncology

    doi: 10.1016/j.molonc.2014.08.014

    p23 levels do not affect cell growth. (A) LNCaP_p23 cells were treated with 100 nM doxycycline (DOX) for 48 h prior to seeding in 96-well plates for cell viability assessment. Twenty microlitres of MTT reagent was added to each well, incubated for 2 h at 37 °C and absorbance measured at 490 nm at the specified time points. To verify p23 ectopic expression, cells were treated as above and lysates collected, harvested and resolved by Western blotting. Gels were transferred onto nitrocellulose membranes and probed with specific antibodies against p23 and β-actin. (B) LNCaP cells were transfected with individual siRNAs against p23 or a scrambled control for 72 h prior to seeding in 96-well plates for cell viability assessment, performed as in (A). To verify p23 knockdown cells were transfected and collected at the indicated time points. Lysates were resolved by SDS-PAGE, transferred onto nitrocellulose membranes and probed with specific antibodies against p23 and β-actin. Results are the mean ± 1 STDEV of two independent experiments performed in triplicate.
    Figure Legend Snippet: p23 levels do not affect cell growth. (A) LNCaP_p23 cells were treated with 100 nM doxycycline (DOX) for 48 h prior to seeding in 96-well plates for cell viability assessment. Twenty microlitres of MTT reagent was added to each well, incubated for 2 h at 37 °C and absorbance measured at 490 nm at the specified time points. To verify p23 ectopic expression, cells were treated as above and lysates collected, harvested and resolved by Western blotting. Gels were transferred onto nitrocellulose membranes and probed with specific antibodies against p23 and β-actin. (B) LNCaP cells were transfected with individual siRNAs against p23 or a scrambled control for 72 h prior to seeding in 96-well plates for cell viability assessment, performed as in (A). To verify p23 knockdown cells were transfected and collected at the indicated time points. Lysates were resolved by SDS-PAGE, transferred onto nitrocellulose membranes and probed with specific antibodies against p23 and β-actin. Results are the mean ± 1 STDEV of two independent experiments performed in triplicate.

    Techniques Used: MTT Assay, Incubation, Expressing, Western Blot, Transfection, SDS Page

    p23 levels affect cell migration. (A) LNCaP_p23 cells were treated with 100 nM doxycycline (DOX) for 48 h prior to seeding at a density of 1.5 × 10 4 in serum free medium in the upper chamber of transwells pre-coated with collagen for 2 h. Full media was placed in the lower chamber and used as a chemoattractant. After 24 h, cells in the lower chamber were fixed, stained and migration quantified using ImageJ. To verify p23 ectopic expression cells were harvested and lysates resolved by Western Blotting and probed with specific antibodies against p23 and β-actin. Results are the mean ± 1 STDEV of a representative experiment performed in triplicate. (B) LNCaP cells were transfected with siRNA against p23 or non-targeting control. Seventy-two hours after cells were seeded to confluency in a 6-well plate and 24 h after monolayers were scratched with a pipette tip, washed with PBS twice and incubated in hormone-depleted media for further 36 h. Recovery of the wound was monitored and images were taken at the specified time points after scratching. The wound area was measured for each time point and condition using ImageJ and values were made relative to the corresponding wound at 0 h and expressed as a percentage. C4-2.
    Figure Legend Snippet: p23 levels affect cell migration. (A) LNCaP_p23 cells were treated with 100 nM doxycycline (DOX) for 48 h prior to seeding at a density of 1.5 × 10 4 in serum free medium in the upper chamber of transwells pre-coated with collagen for 2 h. Full media was placed in the lower chamber and used as a chemoattractant. After 24 h, cells in the lower chamber were fixed, stained and migration quantified using ImageJ. To verify p23 ectopic expression cells were harvested and lysates resolved by Western Blotting and probed with specific antibodies against p23 and β-actin. Results are the mean ± 1 STDEV of a representative experiment performed in triplicate. (B) LNCaP cells were transfected with siRNA against p23 or non-targeting control. Seventy-two hours after cells were seeded to confluency in a 6-well plate and 24 h after monolayers were scratched with a pipette tip, washed with PBS twice and incubated in hormone-depleted media for further 36 h. Recovery of the wound was monitored and images were taken at the specified time points after scratching. The wound area was measured for each time point and condition using ImageJ and values were made relative to the corresponding wound at 0 h and expressed as a percentage. C4-2.

    Techniques Used: Migration, Staining, Expressing, Western Blot, Transfection, Transferring, Incubation

    p23 regulation. (A) LNCaP cells were stripped for 72 h prior to treatment with 10 nM mibolerone (Mib) or 1 μM bicalutamide (Bic) for the indicated time points. Cells were harvested and lysates resolved by Western blotting, transferred onto PVDF and membranes probed with specific antibodies against HSP90, p23 and α–tubulin. (B) Graphs for HSP90 and p23 represent densitometry performed on Western-blot images for each of the treatments and normalised against the signal obtained for α-tubulin. Mib and Bic treated samples were then normalised against the corresponding untreated control for each time point, hence vehicle treated results have been removed from graphs for clarity. Results presented are the mean ± 1 standard error of three experiments. LNCaP cells stably transfected with scrambled (C) or shRNA against AR (D) were treated with 2 μM doxycycline (DOX) for 48 h. Cells were lysed at the indicated time points and proteins resolved by SDS-PAGE and probed with antibodies against AR, p23 and β-actin. Figures are a representative result of four experimental replicates. Graphs for either the scrambled (C) or shRNA transfected line (D) represent densitometry performed on western results, normalising against signal obtained for β-actin. The shading is the same for both C and D. Results presented are the mean ± 1 standard error of four independent experiments. * = p ≤ 0.05; ** = p ≤ 0.005 (Student's test).
    Figure Legend Snippet: p23 regulation. (A) LNCaP cells were stripped for 72 h prior to treatment with 10 nM mibolerone (Mib) or 1 μM bicalutamide (Bic) for the indicated time points. Cells were harvested and lysates resolved by Western blotting, transferred onto PVDF and membranes probed with specific antibodies against HSP90, p23 and α–tubulin. (B) Graphs for HSP90 and p23 represent densitometry performed on Western-blot images for each of the treatments and normalised against the signal obtained for α-tubulin. Mib and Bic treated samples were then normalised against the corresponding untreated control for each time point, hence vehicle treated results have been removed from graphs for clarity. Results presented are the mean ± 1 standard error of three experiments. LNCaP cells stably transfected with scrambled (C) or shRNA against AR (D) were treated with 2 μM doxycycline (DOX) for 48 h. Cells were lysed at the indicated time points and proteins resolved by SDS-PAGE and probed with antibodies against AR, p23 and β-actin. Figures are a representative result of four experimental replicates. Graphs for either the scrambled (C) or shRNA transfected line (D) represent densitometry performed on western results, normalising against signal obtained for β-actin. The shading is the same for both C and D. Results presented are the mean ± 1 standard error of four independent experiments. * = p ≤ 0.05; ** = p ≤ 0.005 (Student's test).

    Techniques Used: Western Blot, Stable Transfection, Transfection, shRNA, SDS Page

    p23 regulates AR expression in the absence of hormone. (A) LNCaP-p23 cells were treated with 100 nM doxycycline (DOX) for 48 h followed by a 48 h hormone-depletion also in the presence of DOX. Cell lysates were collected at the indicated time points, harvested, resolved by Western blotting and transferred to PVDF membranes, which were probed using specific antibodies against AR, p23 and β–actin. Densitometry was performed on Western Blotting results normalising against signal obtained for β–actin. (B) LNCaP cells were transfected with specific siRNA against p23 collected at the indicated time points, harvested and resolved by Western Blotting. Gels were transferred onto PVDF membranes and probed with specific antibodies against p23, AR and β-actin. Densitometry performed on Western results as above. Results presented are the mean ± 1 STDEV of three independent experiments. * p value ≤0.05 ** p value ≤0.005 *** p value ≤0.0005 (Student's t test).
    Figure Legend Snippet: p23 regulates AR expression in the absence of hormone. (A) LNCaP-p23 cells were treated with 100 nM doxycycline (DOX) for 48 h followed by a 48 h hormone-depletion also in the presence of DOX. Cell lysates were collected at the indicated time points, harvested, resolved by Western blotting and transferred to PVDF membranes, which were probed using specific antibodies against AR, p23 and β–actin. Densitometry was performed on Western Blotting results normalising against signal obtained for β–actin. (B) LNCaP cells were transfected with specific siRNA against p23 collected at the indicated time points, harvested and resolved by Western Blotting. Gels were transferred onto PVDF membranes and probed with specific antibodies against p23, AR and β-actin. Densitometry performed on Western results as above. Results presented are the mean ± 1 STDEV of three independent experiments. * p value ≤0.05 ** p value ≤0.005 *** p value ≤0.0005 (Student's t test).

    Techniques Used: Expressing, Western Blot, Transfection

    14) Product Images from "Identification and characterization of alternative splice variants of the mouse Trek2/Kcnk10 gene"

    Article Title: Identification and characterization of alternative splice variants of the mouse Trek2/Kcnk10 gene

    Journal: Neuroscience

    doi: 10.1016/j.neuroscience.2011.07.064

    Whole-cell and plasma membrane expression levels of Trek2 splice variants A) Representative immunoblot of total Trek2 protein from HEK 293 cells expressing Trek2a, Trek2b, or Trek2c. Three separate transfections per Trek2 variant were performed, and the levels of both the Trek2 variant and β-actin were determined in each sample. B) Representative immunoblot of Trek2 splice variants found in samples of biotinylated surface proteins. C) Summary plot depicting the level of total Trek2 protein expressed in HEK293 cells, normalized to the level of β-actin (N=10). ANOVA revealed a statistically greater amount of Trek2b total protein compared to both Trek2a and Trek2c (n=10, F (2,27) =21.45: P
    Figure Legend Snippet: Whole-cell and plasma membrane expression levels of Trek2 splice variants A) Representative immunoblot of total Trek2 protein from HEK 293 cells expressing Trek2a, Trek2b, or Trek2c. Three separate transfections per Trek2 variant were performed, and the levels of both the Trek2 variant and β-actin were determined in each sample. B) Representative immunoblot of Trek2 splice variants found in samples of biotinylated surface proteins. C) Summary plot depicting the level of total Trek2 protein expressed in HEK293 cells, normalized to the level of β-actin (N=10). ANOVA revealed a statistically greater amount of Trek2b total protein compared to both Trek2a and Trek2c (n=10, F (2,27) =21.45: P

    Techniques Used: Expressing, Transfection, Variant Assay

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    Article Title: Activation of PERK Signaling Attenuates A?-Mediated ER Stress
    Article Snippet: .. The blots were washed three times with TBS, and then incubated at room temperature overnight with Anti-KDEL (1∶1000, Assay designs), anti-GADD153/CHOP (1∶1000, Santa Cruz Biotechnology), anti-phospho-PERK (1∶800, Santa Cruz Biotechnology), anti-phospho-eIF2α (1∶1000, Cell Signaling), anti-phospho-Ire1α from (1∶800, Abcam), anti-ATF6α (1∶1000, Santa Cruz Biotechnology), or β-actin (1∶2000, Abcam) were used for primary antibodies in TBST (10 mM Tris, pH 7.5, 100 mM NaCl, 0.05% Tween 20) containing 1% nonfat dry milk. .. The next day, the blots were washed three times with TBST, and then incubated for 1 h at room temperature with horseradish peroxidase (HRP)-conjugated secondary antibodies (1∶2000 dilution) (Santa Cruz Biotechology) in TBST containing 1% nonfat dry milk.

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    Article Title: Effects of taxol resistance gene 1 on the cisplatin response in gastric cancer
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    Abcam anti β actin antibody
    Protein expression levels of PERK, IRE1α and ATF6 in ovaries of aged mice. Representative western blot images (a) and quantification of PERK, IRE1α and ATF6 protein expression levels (b). <t>β-ACTIN</t> served as an internal control. Data are expressed as the mean ± SEM, expressed by error bars.
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    In vitro Trypanosoma cruzi infection induces expression of Wnt proteins, Frizzled (Fzd) receptors, and β-catenin macrophages. Bone marrow-derived macrophages were in vitro infected with T. cruzi trypomastigotes or left uninfected (NI) and then evaluated for expression of Wnt proteins and Fzd receptors at different times post-infection (pi). (A) Expression of Wnt3a and Wnt5a mRNA (relative to <t>β-actin)</t> was determined by quantitative real-time-PCR. (B) The relative abundance of Wnt3, Wnt5a, and β-actin in the cell lysates were determined by Western blot and densitometry at 12 h pi. Representative Western blot and the ratio of Wnt3a or Wnt5a to β-actin are shown. (C) Expression of Fzd4, Fzd8, Fzd9, and Fzd6 mRNA (relative to β-actin) was determined by q-PCR. The results are expressed as the average of three independent experiments ± SEM. Abbreviation: AU, arbitrary units (* P
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    Protein expression levels of PERK, IRE1α and ATF6 in ovaries of aged mice. Representative western blot images (a) and quantification of PERK, IRE1α and ATF6 protein expression levels (b). β-ACTIN served as an internal control. Data are expressed as the mean ± SEM, expressed by error bars.

    Journal: The Journal of Veterinary Medical Science

    Article Title: Intravenous human endothelial progenitor cell administration into aged mice enhances embryo development and oocyte quality by reducing inflammation, endoplasmic reticulum stress and apoptosis

    doi: 10.1292/jvms.18-0242

    Figure Lengend Snippet: Protein expression levels of PERK, IRE1α and ATF6 in ovaries of aged mice. Representative western blot images (a) and quantification of PERK, IRE1α and ATF6 protein expression levels (b). β-ACTIN served as an internal control. Data are expressed as the mean ± SEM, expressed by error bars.

    Article Snippet: The loading and blotting of the amount of protein was verified by reprobing the membrane with anti-β actin antibody (1:5,000; Abcam) followed by Coomassie Blue staining.

    Techniques: Expressing, Mouse Assay, Western Blot

    Gastrodin (GSTD) increased osteogenic transcription Runx2, decreased adipogenic factor peroxisome proliferator-activated receptor (PPAR)γ isoform 2 and activated nuclear factor-like 2 (NRF2) pathway protein expression levels. Representative western blot analyses for total protein was analyzed by western blotting in dexamethasone (DEX)-treated MC3T3-E1 cells with or without GSTD pretreatment at different doses. The relative protein expression levels were measured using the fold-change in each protein relative to β-actin from the same sample. The data are expressed as the mean ± standard deviation. ## P

    Journal: International Journal of Molecular Medicine

    Article Title: Gastrodin protects MC3T3-E1 osteoblasts from dexamethasone-induced cellular dysfunction and promotes bone formation via induction of the NRF2 signaling pathway

    doi: 10.3892/ijmm.2018.3414

    Figure Lengend Snippet: Gastrodin (GSTD) increased osteogenic transcription Runx2, decreased adipogenic factor peroxisome proliferator-activated receptor (PPAR)γ isoform 2 and activated nuclear factor-like 2 (NRF2) pathway protein expression levels. Representative western blot analyses for total protein was analyzed by western blotting in dexamethasone (DEX)-treated MC3T3-E1 cells with or without GSTD pretreatment at different doses. The relative protein expression levels were measured using the fold-change in each protein relative to β-actin from the same sample. The data are expressed as the mean ± standard deviation. ## P

    Article Snippet: Rabbit anti-HO-1 (cat. no. ab68477; 1:1,000), rabbit anti-NQO-1 (cat. no. ab76956; 1:1,000), and mouse anti-β-actin (cat. no. ab8245; 1:1,000), Anti-OCN (cat. no. ab93876; 1:1,000) monoclonal antibodies were purchased from Abcam (Cambridge, MA, USA).

    Techniques: Expressing, Western Blot, Standard Deviation

    The effect of vasoactive intestinal peptide (VIP) and pituitary adenylate cyclase-activating polypeptide (PACAP) on HIV-1 replication is dependent on protein kinases A (PKA) and C (PKC). (A,B) Uninfected macrophages were treated with VIP or PACAP (10 nM) and levels of PKA and pPKA (A) , PKCα and pPKCα (B) were analyzed by western blot at different time-points; figures show the ratios between band densitometry normalized based on β-actin intensity ( n = 3). (C–E) Infected macrophages were treated with VIP or PACAP (10 nM) in the presence or not of signaling inhibitors (PKAi, H89; PKCi, Gö 6983; Pan-protein kinase inhibitor, H7, 50 nM each one) for 30 min; cells were washed before neuropeptide addition [in (C) , results are shown normalized to medium to rule out any possible inhibitor interference on HIV-1 replication]. (D,E) Treatment with VIP (D) or PACAP (E) plus inhibitors; results are shown normalized to respective controls [shown in (C) ], to compare the individual inhibitory effects. Supernatants were collected after 12 days and viral replication was measured ( n = 5). (F,G) Infected macrophages were treated with VIP or PACAP (10 nM) in the presence or not of signaling inhibitors as above, for 30 min; cells were washed before neuropeptide addition. After 48 h, supernatants were collected and production of MIP-1α (F) and IL-10 (G) were analyzed by ELISA ( n = 4). * p

    Journal: Frontiers in Immunology

    Article Title: The Neuropeptides Vasoactive Intestinal Peptide and Pituitary Adenylate Cyclase-Activating Polypeptide Control HIV-1 Infection in Macrophages Through Activation of Protein Kinases A and C

    doi: 10.3389/fimmu.2018.01336

    Figure Lengend Snippet: The effect of vasoactive intestinal peptide (VIP) and pituitary adenylate cyclase-activating polypeptide (PACAP) on HIV-1 replication is dependent on protein kinases A (PKA) and C (PKC). (A,B) Uninfected macrophages were treated with VIP or PACAP (10 nM) and levels of PKA and pPKA (A) , PKCα and pPKCα (B) were analyzed by western blot at different time-points; figures show the ratios between band densitometry normalized based on β-actin intensity ( n = 3). (C–E) Infected macrophages were treated with VIP or PACAP (10 nM) in the presence or not of signaling inhibitors (PKAi, H89; PKCi, Gö 6983; Pan-protein kinase inhibitor, H7, 50 nM each one) for 30 min; cells were washed before neuropeptide addition [in (C) , results are shown normalized to medium to rule out any possible inhibitor interference on HIV-1 replication]. (D,E) Treatment with VIP (D) or PACAP (E) plus inhibitors; results are shown normalized to respective controls [shown in (C) ], to compare the individual inhibitory effects. Supernatants were collected after 12 days and viral replication was measured ( n = 5). (F,G) Infected macrophages were treated with VIP or PACAP (10 nM) in the presence or not of signaling inhibitors as above, for 30 min; cells were washed before neuropeptide addition. After 48 h, supernatants were collected and production of MIP-1α (F) and IL-10 (G) were analyzed by ELISA ( n = 4). * p

    Article Snippet: Nonspecific binding was blocked with 5% (w/v) skimmed milk powder in TTBS (Tween 20 tris-buffered saline) for 1 h, followed by incubation with rabbit polyclonal anti-phospo-PKA (1:1,000; sc-32968, Santa Cruz Biotechnology), mouse monoclonal anti-PKA (1:1,000; sc-390548, Santa Cruz Biotechnology), rabbit polyclonal anti-phospho-PKC (1:1,000; ab23513, Abcam), mouse monoclonal anti-PKC (1:1,000; ab23511, Abcam), or mouse monoclonal anti-β-actin antibody (1:3,000; ab8226, Abcam), overnight at 4°C.

    Techniques: Western Blot, Infection, Enzyme-linked Immunosorbent Assay

    In vitro Trypanosoma cruzi infection induces expression of Wnt proteins, Frizzled (Fzd) receptors, and β-catenin macrophages. Bone marrow-derived macrophages were in vitro infected with T. cruzi trypomastigotes or left uninfected (NI) and then evaluated for expression of Wnt proteins and Fzd receptors at different times post-infection (pi). (A) Expression of Wnt3a and Wnt5a mRNA (relative to β-actin) was determined by quantitative real-time-PCR. (B) The relative abundance of Wnt3, Wnt5a, and β-actin in the cell lysates were determined by Western blot and densitometry at 12 h pi. Representative Western blot and the ratio of Wnt3a or Wnt5a to β-actin are shown. (C) Expression of Fzd4, Fzd8, Fzd9, and Fzd6 mRNA (relative to β-actin) was determined by q-PCR. The results are expressed as the average of three independent experiments ± SEM. Abbreviation: AU, arbitrary units (* P

    Journal: Frontiers in Immunology

    Article Title: Trypanosoma cruzi Exploits Wnt Signaling Pathway to Promote Its Intracellular Replication in Macrophages

    doi: 10.3389/fimmu.2018.00859

    Figure Lengend Snippet: In vitro Trypanosoma cruzi infection induces expression of Wnt proteins, Frizzled (Fzd) receptors, and β-catenin macrophages. Bone marrow-derived macrophages were in vitro infected with T. cruzi trypomastigotes or left uninfected (NI) and then evaluated for expression of Wnt proteins and Fzd receptors at different times post-infection (pi). (A) Expression of Wnt3a and Wnt5a mRNA (relative to β-actin) was determined by quantitative real-time-PCR. (B) The relative abundance of Wnt3, Wnt5a, and β-actin in the cell lysates were determined by Western blot and densitometry at 12 h pi. Representative Western blot and the ratio of Wnt3a or Wnt5a to β-actin are shown. (C) Expression of Fzd4, Fzd8, Fzd9, and Fzd6 mRNA (relative to β-actin) was determined by q-PCR. The results are expressed as the average of three independent experiments ± SEM. Abbreviation: AU, arbitrary units (* P

    Article Snippet: Anti-β-actin (mAbcam8226, Abcam) was used as loading control.

    Techniques: In Vitro, Infection, Expressing, Derivative Assay, Real-time Polymerase Chain Reaction, Western Blot, Polymerase Chain Reaction

    Trypanosoma cruzi infection induces early β-catenin activation in macrophages. Bone marrow-derived macrophages were in vitro infected with trypomastigotes of T. cruzi or left uninfected (NI) and then evaluated for β-catenin activation. (A) mRNA and protein expression levels of β-catenin by q-PCR and Western blot at different times post-infection (pi). β-Catenin mRNA relative to β-actin is shown. A representative Western blot and the ratio of β-catenin to β-actin are shown. The results are expressed as the average of three independent experiments ± SEM. Abbreviation: AU, arbitrary units. (B) Expression and localization of β-catenin by immunofluorescence and confocal microscopy. (C) mRNA relative expression of β-catenin target genes Axin1, Wisp1, and Ccnd1 by q-PCR. mRNA expression levels normalized over the expression of β-actin are expressed as the average of three independent experiments ± SEM. (D) Peritoneal macrophages were obtained from uninfected or infected mice at 24 h pi, and the levels of expression and localization of β-catenin were evaluated by immunofluorescence and confocal microscopy. In panels (B,D) , a representative field for each group is shown [ (B,D) .” Green, β-catenin; red, DAPI (* P

    Journal: Frontiers in Immunology

    Article Title: Trypanosoma cruzi Exploits Wnt Signaling Pathway to Promote Its Intracellular Replication in Macrophages

    doi: 10.3389/fimmu.2018.00859

    Figure Lengend Snippet: Trypanosoma cruzi infection induces early β-catenin activation in macrophages. Bone marrow-derived macrophages were in vitro infected with trypomastigotes of T. cruzi or left uninfected (NI) and then evaluated for β-catenin activation. (A) mRNA and protein expression levels of β-catenin by q-PCR and Western blot at different times post-infection (pi). β-Catenin mRNA relative to β-actin is shown. A representative Western blot and the ratio of β-catenin to β-actin are shown. The results are expressed as the average of three independent experiments ± SEM. Abbreviation: AU, arbitrary units. (B) Expression and localization of β-catenin by immunofluorescence and confocal microscopy. (C) mRNA relative expression of β-catenin target genes Axin1, Wisp1, and Ccnd1 by q-PCR. mRNA expression levels normalized over the expression of β-actin are expressed as the average of three independent experiments ± SEM. (D) Peritoneal macrophages were obtained from uninfected or infected mice at 24 h pi, and the levels of expression and localization of β-catenin were evaluated by immunofluorescence and confocal microscopy. In panels (B,D) , a representative field for each group is shown [ (B,D) .” Green, β-catenin; red, DAPI (* P

    Article Snippet: Anti-β-actin (mAbcam8226, Abcam) was used as loading control.

    Techniques: Infection, Activation Assay, Derivative Assay, In Vitro, Expressing, Polymerase Chain Reaction, Western Blot, Immunofluorescence, Confocal Microscopy, Mouse Assay

    Trypanosoma cruzi infection induces late Wnt/Ca +2 pathway activation in macrophages. Bone marrow-derived macrophages were in vitro infected with trypomastigotes (Tps) of T. cruzi or left uninfected (NI) and then evaluated for calcium/calmodulin-dependent kinase II (CaMKII) phosphorylated at Thr286 expression and NFATc1 expression and localization at different times post-infection (pi). Phosphorylated CAMKII (p-CAMKII) expression (A) and NFATc1 expression (B) were assessed by Western blot and normalized to β-actin. (C) .” Green, NFATc1; red, DAPI. (D,E) Bone marrow-derived macrophages (BMM) were treated for 24 h with the PORCN inhibitor (IWP-L6) or left untreated (control), infected with T. cruzi Tps and assayed for p-CaMKII and NFATc1 expression at 24 h pi. Ionomycin-activated BMM (20 min, 1 µM) were used as a positive control. In panels (A,B,D,E) , a representative Western blot and the ratio of protein expression to β-actin are shown. The results are expressed as the average of three independent experiments ± SEM. Abbreviation: AU, arbitrary units (* P

    Journal: Frontiers in Immunology

    Article Title: Trypanosoma cruzi Exploits Wnt Signaling Pathway to Promote Its Intracellular Replication in Macrophages

    doi: 10.3389/fimmu.2018.00859

    Figure Lengend Snippet: Trypanosoma cruzi infection induces late Wnt/Ca +2 pathway activation in macrophages. Bone marrow-derived macrophages were in vitro infected with trypomastigotes (Tps) of T. cruzi or left uninfected (NI) and then evaluated for calcium/calmodulin-dependent kinase II (CaMKII) phosphorylated at Thr286 expression and NFATc1 expression and localization at different times post-infection (pi). Phosphorylated CAMKII (p-CAMKII) expression (A) and NFATc1 expression (B) were assessed by Western blot and normalized to β-actin. (C) .” Green, NFATc1; red, DAPI. (D,E) Bone marrow-derived macrophages (BMM) were treated for 24 h with the PORCN inhibitor (IWP-L6) or left untreated (control), infected with T. cruzi Tps and assayed for p-CaMKII and NFATc1 expression at 24 h pi. Ionomycin-activated BMM (20 min, 1 µM) were used as a positive control. In panels (A,B,D,E) , a representative Western blot and the ratio of protein expression to β-actin are shown. The results are expressed as the average of three independent experiments ± SEM. Abbreviation: AU, arbitrary units (* P

    Article Snippet: Anti-β-actin (mAbcam8226, Abcam) was used as loading control.

    Techniques: Infection, Activation Assay, Derivative Assay, In Vitro, Expressing, Western Blot, Positive Control

    Experimental Trypanosoma cruzi infection induces the expression of Wnt pathway proteins. Western blot analysis of Wnt3a, Wnt5a, and β-catenin expression in spleen mononuclear cell homogenates derived from uninfected (NI) or T. cruzi -infected B6 mice at different times post-infection. Images show one representative NI and one infected mice by time point. Each bar represents the mean ± SEM of protein relative expression levels quantified by scanning the intensity of bands areas in the homogenates normalized to β-actin ( n = 5 mice per time point) (* P

    Journal: Frontiers in Immunology

    Article Title: Trypanosoma cruzi Exploits Wnt Signaling Pathway to Promote Its Intracellular Replication in Macrophages

    doi: 10.3389/fimmu.2018.00859

    Figure Lengend Snippet: Experimental Trypanosoma cruzi infection induces the expression of Wnt pathway proteins. Western blot analysis of Wnt3a, Wnt5a, and β-catenin expression in spleen mononuclear cell homogenates derived from uninfected (NI) or T. cruzi -infected B6 mice at different times post-infection. Images show one representative NI and one infected mice by time point. Each bar represents the mean ± SEM of protein relative expression levels quantified by scanning the intensity of bands areas in the homogenates normalized to β-actin ( n = 5 mice per time point) (* P

    Article Snippet: Anti-β-actin (mAbcam8226, Abcam) was used as loading control.

    Techniques: Infection, Expressing, Western Blot, Derivative Assay, Mouse Assay