anti beta actin  (Abcam)

 
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  • 99
    Name:
    Anti beta Actin antibody
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    Catalog Number:
    ab16039
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    Structured Review

    Abcam anti beta actin
    MLN4924 suppress cullin 1 neddylation in patient-derived glioblastoma stem cells. ( A ) Schematic diagram of obtaining PDC from glioblastoma patient tissue. ( B ) IC 50 values of 15 different patient-derived glioblastoma stem cells treated with different concentrations (0.04–30 μM) of MLN4924 for 7 d. ( C ) AUC values of 15 different patient-derived glioblastoma stem cells treated with different concentrations (0.04–30 μM) of MLN4924 for 7 d. ( D ) Immunofluorescence staining of Caspase 3/7 induced by MLN4924 (0.1 μM for 7 d) treated cells were demonstrated. Nuclei were labeled with DAPI. Cell images were captured with Operetta High-Content Imaging System. ( E ) Cells were treated with MLN4924 and Bortezomib for 12 h at the indicated doses. Neddylation pathway related protein levels were examined by western blotting. <t>Beta</t> actin was used as a loading control. Similar results were obtained in three independent experiments.

    https://www.bioz.com/result/anti beta actin/product/Abcam
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    Images

    1) Product Images from "The Protein Neddylation Inhibitor MLN4924 Suppresses Patient-Derived Glioblastoma Cells via Inhibition of ERK and AKT Signaling"

    Article Title: The Protein Neddylation Inhibitor MLN4924 Suppresses Patient-Derived Glioblastoma Cells via Inhibition of ERK and AKT Signaling

    Journal: Cancers

    doi: 10.3390/cancers11121849

    MLN4924 suppress cullin 1 neddylation in patient-derived glioblastoma stem cells. ( A ) Schematic diagram of obtaining PDC from glioblastoma patient tissue. ( B ) IC 50 values of 15 different patient-derived glioblastoma stem cells treated with different concentrations (0.04–30 μM) of MLN4924 for 7 d. ( C ) AUC values of 15 different patient-derived glioblastoma stem cells treated with different concentrations (0.04–30 μM) of MLN4924 for 7 d. ( D ) Immunofluorescence staining of Caspase 3/7 induced by MLN4924 (0.1 μM for 7 d) treated cells were demonstrated. Nuclei were labeled with DAPI. Cell images were captured with Operetta High-Content Imaging System. ( E ) Cells were treated with MLN4924 and Bortezomib for 12 h at the indicated doses. Neddylation pathway related protein levels were examined by western blotting. Beta actin was used as a loading control. Similar results were obtained in three independent experiments.
    Figure Legend Snippet: MLN4924 suppress cullin 1 neddylation in patient-derived glioblastoma stem cells. ( A ) Schematic diagram of obtaining PDC from glioblastoma patient tissue. ( B ) IC 50 values of 15 different patient-derived glioblastoma stem cells treated with different concentrations (0.04–30 μM) of MLN4924 for 7 d. ( C ) AUC values of 15 different patient-derived glioblastoma stem cells treated with different concentrations (0.04–30 μM) of MLN4924 for 7 d. ( D ) Immunofluorescence staining of Caspase 3/7 induced by MLN4924 (0.1 μM for 7 d) treated cells were demonstrated. Nuclei were labeled with DAPI. Cell images were captured with Operetta High-Content Imaging System. ( E ) Cells were treated with MLN4924 and Bortezomib for 12 h at the indicated doses. Neddylation pathway related protein levels were examined by western blotting. Beta actin was used as a loading control. Similar results were obtained in three independent experiments.

    Techniques Used: Derivative Assay, Immunofluorescence, Staining, Labeling, Imaging, Western Blot

    Sensitivity of MLN4924 is associated with upregulation of ERK and AKT signaling. ( A ) Immunofluorescence staining of pERK and pAKT were demonstrated in cells induced by MLN4924 (1 μM) treatment. Nuclei were labeled with DAPI. Cell images were captured with Operetta High-Content Imaging System. ( B ) PDC1 and PDC15 cells were treated with MLN4924 for 12 h at the indicated concentrations. AKT, pAKT, ERK, and pERK levels were examined by western blotting. Beta actin was used as a loading control. Similar results were obtained in three independent experiments.
    Figure Legend Snippet: Sensitivity of MLN4924 is associated with upregulation of ERK and AKT signaling. ( A ) Immunofluorescence staining of pERK and pAKT were demonstrated in cells induced by MLN4924 (1 μM) treatment. Nuclei were labeled with DAPI. Cell images were captured with Operetta High-Content Imaging System. ( B ) PDC1 and PDC15 cells were treated with MLN4924 for 12 h at the indicated concentrations. AKT, pAKT, ERK, and pERK levels were examined by western blotting. Beta actin was used as a loading control. Similar results were obtained in three independent experiments.

    Techniques Used: Immunofluorescence, Staining, Labeling, Imaging, Western Blot

    2) Product Images from "High Interstitial Fluid Pressure Is Associated with Low Tumour Penetration of Diagnostic Monoclonal Antibodies Applied for Molecular Imaging Purposes"

    Article Title: High Interstitial Fluid Pressure Is Associated with Low Tumour Penetration of Diagnostic Monoclonal Antibodies Applied for Molecular Imaging Purposes

    Journal: PLoS ONE

    doi: 10.1371/journal.pone.0036258

    EpCAM expression of human malignant cells. (A) The mRNA of the malignant cell lines 5061, 5072 (pancreatic cancer), LNCAP, PC3 (prostate cancer), FemX-1, MEWO (melanoma), T47D, MCF7 (breast cancer), HT29 (colon cancer) and OH-1 (small cell lung cancer) were relatively quantified by qPCR, using GAPDH for normalization. 5072, LNCAP, PC3, T47D, MCF7, Caco2 and HT29 showed high expression levels of EpCAM mRNA. (B) EpCAM could be detected by Western blot analysis of HT29 cell lysate with a specific binding to antibody MOC31. Beta-actin was used as loading control. (C) EpCAM could positively be detected by flow cytometry analysis with MOC31 on all cancer cell lines, except of FemX-1 and MEWO. Isotype controls are shown as dotted lines.
    Figure Legend Snippet: EpCAM expression of human malignant cells. (A) The mRNA of the malignant cell lines 5061, 5072 (pancreatic cancer), LNCAP, PC3 (prostate cancer), FemX-1, MEWO (melanoma), T47D, MCF7 (breast cancer), HT29 (colon cancer) and OH-1 (small cell lung cancer) were relatively quantified by qPCR, using GAPDH for normalization. 5072, LNCAP, PC3, T47D, MCF7, Caco2 and HT29 showed high expression levels of EpCAM mRNA. (B) EpCAM could be detected by Western blot analysis of HT29 cell lysate with a specific binding to antibody MOC31. Beta-actin was used as loading control. (C) EpCAM could positively be detected by flow cytometry analysis with MOC31 on all cancer cell lines, except of FemX-1 and MEWO. Isotype controls are shown as dotted lines.

    Techniques Used: Expressing, Real-time Polymerase Chain Reaction, Western Blot, Binding Assay, Flow Cytometry, Cytometry

    3) Product Images from "Expression of the neuroprotective slow Wallerian degeneration (WldS) gene in non-neuronal tissues"

    Article Title: Expression of the neuroprotective slow Wallerian degeneration (WldS) gene in non-neuronal tissues

    Journal: BMC Neuroscience

    doi: 10.1186/1471-2202-10-148

    Expression of Wld S protein and mRNA in non-neuronal tissue . A - Representative examples of bands obtained with quantitative fluorescent western blots from wild-type and Wld S mouse liver, spleen and cerebellum probed with antibodies against Wld S protein (Wld-18) and beta-actin (loading control). B - Wld S protein levels in organs from Wld S mice expressed as fold change in protein relative to wild-type tissue. Note that all organs except for the liver showed significant levels of Wld S protein, but none to the same magnitude as found in the cerebellum. C - Wld S RNA levels in organs from Wld S mice shown as relative expression normalised to wild-type. Note that RNA levels did not always match protein expression levels (c.f. Panel A). A minimum of 3 mice per genotype were used for all experiments.
    Figure Legend Snippet: Expression of Wld S protein and mRNA in non-neuronal tissue . A - Representative examples of bands obtained with quantitative fluorescent western blots from wild-type and Wld S mouse liver, spleen and cerebellum probed with antibodies against Wld S protein (Wld-18) and beta-actin (loading control). B - Wld S protein levels in organs from Wld S mice expressed as fold change in protein relative to wild-type tissue. Note that all organs except for the liver showed significant levels of Wld S protein, but none to the same magnitude as found in the cerebellum. C - Wld S RNA levels in organs from Wld S mice shown as relative expression normalised to wild-type. Note that RNA levels did not always match protein expression levels (c.f. Panel A). A minimum of 3 mice per genotype were used for all experiments.

    Techniques Used: Expressing, Western Blot, Mouse Assay

    4) Product Images from "A p53-independent apoptotic mechanism of adenoviral mutant E1A was involved in its selective antitumor activity for human cancer"

    Article Title: A p53-independent apoptotic mechanism of adenoviral mutant E1A was involved in its selective antitumor activity for human cancer

    Journal: Oncotarget

    doi: 10.18632/oncotarget.10221

    Ad-DC315-mE1A or Ad-DC315-E1A induced inactive p53 expression HCT116 p53+/+, HCT116 p53−/−, H1299, Hela, HepG2 and U2OS cells were infected with Ad-DC315, Ad-DC315-E1A, Ad-DC315-mE1A or Ad-DC315-EGFP at MOI=20 for 48h. The level of p53, p21, mdm2, Bax, Bcl-2, PARP and E1A proteins were analysed by western blotting. Beta-actin was assayed as a loading control.
    Figure Legend Snippet: Ad-DC315-mE1A or Ad-DC315-E1A induced inactive p53 expression HCT116 p53+/+, HCT116 p53−/−, H1299, Hela, HepG2 and U2OS cells were infected with Ad-DC315, Ad-DC315-E1A, Ad-DC315-mE1A or Ad-DC315-EGFP at MOI=20 for 48h. The level of p53, p21, mdm2, Bax, Bcl-2, PARP and E1A proteins were analysed by western blotting. Beta-actin was assayed as a loading control.

    Techniques Used: Expressing, Infection, Western Blot

    Ad-DC315-mE1A or Ad-DC315-E1A affected cellular p21 localization A. H1299, HeLa, U2OS and HepG2 cells were infected with Ad-DC315-E1A or Ad-DC315-mE1A at indicated MOIs for 72h. p21 and E1A levels were determined by immunoblot analysis. Beta-actin was used as a loading control. B. H1299, HeLa, U2OS and HepG2 cells were treated with adenoviruses at a MOI=20 for 48h. Cellular fractionation was performed. The p21 was detected in cytoplasmic and nuclear fraction (N, nuclear fraction; C, cytoplasmic fraction; T, total cell lysates.). H1 was used as a nuclear marker and btea-actin was a cytoplasm marker.
    Figure Legend Snippet: Ad-DC315-mE1A or Ad-DC315-E1A affected cellular p21 localization A. H1299, HeLa, U2OS and HepG2 cells were infected with Ad-DC315-E1A or Ad-DC315-mE1A at indicated MOIs for 72h. p21 and E1A levels were determined by immunoblot analysis. Beta-actin was used as a loading control. B. H1299, HeLa, U2OS and HepG2 cells were treated with adenoviruses at a MOI=20 for 48h. Cellular fractionation was performed. The p21 was detected in cytoplasmic and nuclear fraction (N, nuclear fraction; C, cytoplasmic fraction; T, total cell lysates.). H1 was used as a nuclear marker and btea-actin was a cytoplasm marker.

    Techniques Used: Infection, Cell Fractionation, Marker

    5) Product Images from "Phosphoproteomic analysis reveals Smarcb1 dependent EGFR signaling in Malignant Rhabdoid tumor cells"

    Article Title: Phosphoproteomic analysis reveals Smarcb1 dependent EGFR signaling in Malignant Rhabdoid tumor cells

    Journal: Molecular Cancer

    doi: 10.1186/s12943-015-0439-5

    Smarcb1 dependent EGFR phosphorylation and transcriptional de-regulation. a Western blot demonstrating constitutive phosphorylation of Tyr-1092 of the EGFR in Smarcb1 deficient cells, and down-regulation of the total-EGFR protein. b Smarcb1 dependent transcriptional regulation of the ErbB family receptors and the EGF ligand. Graph shows RNA levels relative to beta actin as estimated by qRT-PCR. Note that the Y axis of the right panel is two orders of magnitude lower, indicating that expression levels of ErbB3, 4 and EGF are significantly low. In both cell lines Egfr and ErbB3 showed reduced expression in Smarcb1 proficient cells. * Fold change pMIG/ Smarcb1 167 = 2.4, 365 = 4.5; T -test P.V; 167 = 0.00058, 365 = 0.0098. ** Fold change pMIG/ Smarcb1 167 = 8.2, 365 = 6.8; T -test P.V; 167 = 0.0078, 365 = 0.013
    Figure Legend Snippet: Smarcb1 dependent EGFR phosphorylation and transcriptional de-regulation. a Western blot demonstrating constitutive phosphorylation of Tyr-1092 of the EGFR in Smarcb1 deficient cells, and down-regulation of the total-EGFR protein. b Smarcb1 dependent transcriptional regulation of the ErbB family receptors and the EGF ligand. Graph shows RNA levels relative to beta actin as estimated by qRT-PCR. Note that the Y axis of the right panel is two orders of magnitude lower, indicating that expression levels of ErbB3, 4 and EGF are significantly low. In both cell lines Egfr and ErbB3 showed reduced expression in Smarcb1 proficient cells. * Fold change pMIG/ Smarcb1 167 = 2.4, 365 = 4.5; T -test P.V; 167 = 0.00058, 365 = 0.0098. ** Fold change pMIG/ Smarcb1 167 = 8.2, 365 = 6.8; T -test P.V; 167 = 0.0078, 365 = 0.013

    Techniques Used: Western Blot, Quantitative RT-PCR, Expressing

    Phosphoproteomic profiling reveals robust Smarcb1 dependent changes in protein phosphorylation. Matching Smarcb1 proficient and deficient tumor cells were generated by re-introducing SMARCB1 (pMIG- Smarcb1 ) or an empty vector as control (pMIG) [ 14 ]. a The outline of the phosphoproteomic study. Two triple-SILAC experiments were conducted. The first set allowed evaluation of Smarcb1 dependent changes when cultured in normal serum whilst the second set allowed for the evaluation under serum starvation. Smarcb1 proficient cells grown in normal serum and light isotopic labeling were included in both sets to allow comparison between the two sets. b Western blot demonstrating differential AKT phosphorylation in Smarcb1 deficient versus proficient cells. Bar graph shows quantification of western blot presented as fold change in AKT phosphorylation in pMIG/ Smarcb1 cells normalized to beta-actin. c Volcano plot depicting Smarcb1 dependent changes in site phosphorylation across the two sets. X-axis is the log 2 ratio of the abundances of specific residues between Smarcb1 proficient and deficient cells. Negative values for highly phosphorylated in Smarcb1 deficient cells. Y-axis is the logarithmic scale for the P -value of the fold change. For P.V
    Figure Legend Snippet: Phosphoproteomic profiling reveals robust Smarcb1 dependent changes in protein phosphorylation. Matching Smarcb1 proficient and deficient tumor cells were generated by re-introducing SMARCB1 (pMIG- Smarcb1 ) or an empty vector as control (pMIG) [ 14 ]. a The outline of the phosphoproteomic study. Two triple-SILAC experiments were conducted. The first set allowed evaluation of Smarcb1 dependent changes when cultured in normal serum whilst the second set allowed for the evaluation under serum starvation. Smarcb1 proficient cells grown in normal serum and light isotopic labeling were included in both sets to allow comparison between the two sets. b Western blot demonstrating differential AKT phosphorylation in Smarcb1 deficient versus proficient cells. Bar graph shows quantification of western blot presented as fold change in AKT phosphorylation in pMIG/ Smarcb1 cells normalized to beta-actin. c Volcano plot depicting Smarcb1 dependent changes in site phosphorylation across the two sets. X-axis is the log 2 ratio of the abundances of specific residues between Smarcb1 proficient and deficient cells. Negative values for highly phosphorylated in Smarcb1 deficient cells. Y-axis is the logarithmic scale for the P -value of the fold change. For P.V

    Techniques Used: Generated, Plasmid Preparation, Cell Culture, Isotopic Labeling, Western Blot

    6) Product Images from "Neutrophil extracellular traps enriched in oxidized mitochondrial DNA are interferogenic and contribute to lupus-like disease"

    Article Title: Neutrophil extracellular traps enriched in oxidized mitochondrial DNA are interferogenic and contribute to lupus-like disease

    Journal: Nature medicine

    doi: 10.1038/nm.4027

    In vivo administration of a mito-ROS scavenger attenuates lupus-like disease in mice Effect of 7-week continuous, systemic administration of MitoTEMPO versus vehicle on the phenotype of female MRL/ lpr mice ( n = 10/ group). ( a ) Spontaneous NETosis in bone marrow neutrophils at euthanasia quantified by Sytox plate assay in triplicate. ( b ) Albumin: creatinine ratio at 13 and 17 weeks of age. ( c ) Anti-dsDNA levels quantified at 15 and 17 weeks of age. IgG (red) and complement C3 (green) deposition in glomeruli of ( d ) vehicle and ( e ) MitoTEMPO treated mice harvested at euthanasia. Nuclei were stained blue with Hoechst. ( f ) Fluorescence intensity scored in renal tissue sections from 8 vehicle- and 8 MitoTEMPO-treated mice. ( g ) Gene expression in MRL/ lpr splenocytes at euthanasia. Results represent mean ± SEM of 10 mice / group and bar graph results represent downregulation adjusted for results found in vehicle-treated mice (normalized to a value of 1). ( h ) Total and active caspase-1 and IL-18 in renal protein extracts; beta-actin is loading control. Each line depicts an individual mouse treated with either saline or MitoTEMPO as indicated in the figure. Bar graphs show densitometry data for caspase-1 and IL-18 activation ratios. For statistical analysis, unpaired t-test ( a, c, f ), Mann-Whitney ( g, f ); * P
    Figure Legend Snippet: In vivo administration of a mito-ROS scavenger attenuates lupus-like disease in mice Effect of 7-week continuous, systemic administration of MitoTEMPO versus vehicle on the phenotype of female MRL/ lpr mice ( n = 10/ group). ( a ) Spontaneous NETosis in bone marrow neutrophils at euthanasia quantified by Sytox plate assay in triplicate. ( b ) Albumin: creatinine ratio at 13 and 17 weeks of age. ( c ) Anti-dsDNA levels quantified at 15 and 17 weeks of age. IgG (red) and complement C3 (green) deposition in glomeruli of ( d ) vehicle and ( e ) MitoTEMPO treated mice harvested at euthanasia. Nuclei were stained blue with Hoechst. ( f ) Fluorescence intensity scored in renal tissue sections from 8 vehicle- and 8 MitoTEMPO-treated mice. ( g ) Gene expression in MRL/ lpr splenocytes at euthanasia. Results represent mean ± SEM of 10 mice / group and bar graph results represent downregulation adjusted for results found in vehicle-treated mice (normalized to a value of 1). ( h ) Total and active caspase-1 and IL-18 in renal protein extracts; beta-actin is loading control. Each line depicts an individual mouse treated with either saline or MitoTEMPO as indicated in the figure. Bar graphs show densitometry data for caspase-1 and IL-18 activation ratios. For statistical analysis, unpaired t-test ( a, c, f ), Mann-Whitney ( g, f ); * P

    Techniques Used: In Vivo, Mouse Assay, Staining, Fluorescence, Expressing, Activation Assay, MANN-WHITNEY

    7) Product Images from "Effects of Tamarindus indica Fruit Pulp Extract on Abundance of HepG2 Cell Lysate Proteins and Their Possible Consequential Impact on Metabolism and Inflammation"

    Article Title: Effects of Tamarindus indica Fruit Pulp Extract on Abundance of HepG2 Cell Lysate Proteins and Their Possible Consequential Impact on Metabolism and Inflammation

    Journal: BioMed Research International

    doi: 10.1155/2013/459017

    Western blot analyses of NDUFA10, PCYT2, and UQCRC2 of HepG2 cells. (a) Western blot cropped images of NDUFA10, PCYT2, UQCRC2, and beta actin bands detected by antisera against the respective proteins; (b) densitometry analyses of Western blot using ImageJ software. Assay was done in triplicate and data are represented as mean ± standard deviation.
    Figure Legend Snippet: Western blot analyses of NDUFA10, PCYT2, and UQCRC2 of HepG2 cells. (a) Western blot cropped images of NDUFA10, PCYT2, UQCRC2, and beta actin bands detected by antisera against the respective proteins; (b) densitometry analyses of Western blot using ImageJ software. Assay was done in triplicate and data are represented as mean ± standard deviation.

    Techniques Used: Western Blot, Software, Standard Deviation

    IPA graphical representation of the molecular relationships between HepG2 secreted and cytosolic proteins after treatment. The network is displayed graphically as nodes (proteins) and edges (the biological relationships between the nodes). Nodes in red indicate up-regulated proteins while those in green represent down-regulated proteins. Nodes without colors indicate unaltered expression. Various shapes of the nodes represent functional class of the proteins. Edges are displayed with various labels that describe the nature of the relationship between the nodes. Transthyretin, TTR; thyroglobulin, TG; interleukin-1 beta, IL1B; tumour necrosis factor, TNF; apolipoprotein A-1, APOA1; apolipoprotein C-1, APOC1; lecithin cholesterol acyltransferase, LCAT; endothelial lipase, LIPG; haptoglobin, HP; phospholipase A2, PLA2G2A; cholesterylester transfer protein, CETP; ATP-binding cassette transporter sub-family C member 9, ABCC9; ATP-sensitive inward rectifier potassium channel 11, KCNJ11; ectonucleotide pyrophosphatase/phosphodiesterase family member 1, ENPP1; amyloid precursor protein, APP; glyceraldehyde-3-phosphate dehydrogenase, GAPDH; alpha enolase, ENO1; adenylate kinase, AK1; ubiquinol-cytochrome-c reductase complex core protein 2, UQCRC2; xanthine dehydrogenase, XDH; cystathionine beta-synthase, CBS; methionine adenosyltransferase I, alpha, MAT1A; rab GDP dissociation inhibitor beta, GDI2; NLR (nucleotide-binding domain and leucine rich repeat containing family) family, pyrin domain containing 3, NLRP3; Vacuolar ATP synthase subunit E, ATP6V1E1; elongation factor Tu, TUFM; prohibitin, PHB; choline-phosphate cytidylyltransferase A, PCYT1A; uridine 5′-monophosphate synthase, UMPS; NADH dehydrogenase (ubiquinone) 1 alpha subcomplex subunit 10, NDUFA10; NADH dehydrogenase (ubiquinone) flavoprotein 1, NDUFV1; mediator of RNA polymerase III transcription subunit 30, MED30; transcription factor E2F1, E2F1; suppressor of G2 allele of SKP1 homolog, SUGT1.
    Figure Legend Snippet: IPA graphical representation of the molecular relationships between HepG2 secreted and cytosolic proteins after treatment. The network is displayed graphically as nodes (proteins) and edges (the biological relationships between the nodes). Nodes in red indicate up-regulated proteins while those in green represent down-regulated proteins. Nodes without colors indicate unaltered expression. Various shapes of the nodes represent functional class of the proteins. Edges are displayed with various labels that describe the nature of the relationship between the nodes. Transthyretin, TTR; thyroglobulin, TG; interleukin-1 beta, IL1B; tumour necrosis factor, TNF; apolipoprotein A-1, APOA1; apolipoprotein C-1, APOC1; lecithin cholesterol acyltransferase, LCAT; endothelial lipase, LIPG; haptoglobin, HP; phospholipase A2, PLA2G2A; cholesterylester transfer protein, CETP; ATP-binding cassette transporter sub-family C member 9, ABCC9; ATP-sensitive inward rectifier potassium channel 11, KCNJ11; ectonucleotide pyrophosphatase/phosphodiesterase family member 1, ENPP1; amyloid precursor protein, APP; glyceraldehyde-3-phosphate dehydrogenase, GAPDH; alpha enolase, ENO1; adenylate kinase, AK1; ubiquinol-cytochrome-c reductase complex core protein 2, UQCRC2; xanthine dehydrogenase, XDH; cystathionine beta-synthase, CBS; methionine adenosyltransferase I, alpha, MAT1A; rab GDP dissociation inhibitor beta, GDI2; NLR (nucleotide-binding domain and leucine rich repeat containing family) family, pyrin domain containing 3, NLRP3; Vacuolar ATP synthase subunit E, ATP6V1E1; elongation factor Tu, TUFM; prohibitin, PHB; choline-phosphate cytidylyltransferase A, PCYT1A; uridine 5′-monophosphate synthase, UMPS; NADH dehydrogenase (ubiquinone) 1 alpha subcomplex subunit 10, NDUFA10; NADH dehydrogenase (ubiquinone) flavoprotein 1, NDUFV1; mediator of RNA polymerase III transcription subunit 30, MED30; transcription factor E2F1, E2F1; suppressor of G2 allele of SKP1 homolog, SUGT1.

    Techniques Used: Indirect Immunoperoxidase Assay, Expressing, Functional Assay, Binding Assay

    8) Product Images from "Amyloid β Induces Early Changes in the Ribosomal Machinery, Cytoskeletal Organization and Oxidative Phosphorylation in Retinal Photoreceptor Cells"

    Article Title: Amyloid β Induces Early Changes in the Ribosomal Machinery, Cytoskeletal Organization and Oxidative Phosphorylation in Retinal Photoreceptor Cells

    Journal: Frontiers in Molecular Neuroscience

    doi: 10.3389/fnmol.2019.00024

    661 W Cells (1 × 10 6 ) were cultured in plates and treated with 5 μM and 25 μM Aβ concentrations and harvested after 6 h and 24 h respectively. Cells were washed with ice cold 1× PBS, homogenized and subjected to (A) western blotting and probed with indicated antibodies- pGSK3β Ser9 (1:1,000), GSK3β (1:1,000), Anti-beta Actin (1:10,000). Blots were subjected to chemiluminescent substrate detection for HRP linked secondary antibody and (B) quantified by densitometric analysis (*** p
    Figure Legend Snippet: 661 W Cells (1 × 10 6 ) were cultured in plates and treated with 5 μM and 25 μM Aβ concentrations and harvested after 6 h and 24 h respectively. Cells were washed with ice cold 1× PBS, homogenized and subjected to (A) western blotting and probed with indicated antibodies- pGSK3β Ser9 (1:1,000), GSK3β (1:1,000), Anti-beta Actin (1:10,000). Blots were subjected to chemiluminescent substrate detection for HRP linked secondary antibody and (B) quantified by densitometric analysis (*** p

    Techniques Used: Cell Culture, Western Blot

    661 W Cells (1 × 10 6 ) were cultured in plates and treated with 5 μM and 25 μM Aβ concentrations and harvested after 6 h and 24 h respectively. Cells were washed with ice cold 1× PBS, homogenized and subjected to (A) western blotting and probed with indicated antibodies- pTau Ser202/Thr205 (1:1,000), Tau (Tau46, 1:1,000) Anti-beta Actin (1:10,000). Blots were subjected to chemiluminescent substrate detection for HRP linked secondary antibody and (B) quantified by densitometric analysis (** p
    Figure Legend Snippet: 661 W Cells (1 × 10 6 ) were cultured in plates and treated with 5 μM and 25 μM Aβ concentrations and harvested after 6 h and 24 h respectively. Cells were washed with ice cold 1× PBS, homogenized and subjected to (A) western blotting and probed with indicated antibodies- pTau Ser202/Thr205 (1:1,000), Tau (Tau46, 1:1,000) Anti-beta Actin (1:10,000). Blots were subjected to chemiluminescent substrate detection for HRP linked secondary antibody and (B) quantified by densitometric analysis (** p

    Techniques Used: Cell Culture, Western Blot

    9) Product Images from "The S2 Subunit of Infectious Bronchitis Virus Beaudette Is a Determinant of Cellular Tropism"

    Article Title: The S2 Subunit of Infectious Bronchitis Virus Beaudette Is a Determinant of Cellular Tropism

    Journal: Journal of Virology

    doi: 10.1128/JVI.01044-18

    Proteolytic cleavage of rIBVs at the S2′ site is dependent on the Beaudette-specific motif. Chick kidney cells in 6-well plates were mock infected (lane 1) or infected with Beau-R (lane 2), M41-CK (lane 3), BeauR-M41(S) (lane 4), BeauR-S-MM P 3 -CK (lanes 5 and 6), or BeauR-M41-S-BSM P 3 -CK (lanes 7 and 8). Cells were lysed at 24 h postinfection, and spike glycoproteins were analyzed by Western blotting with anti-S2 antibody. Actin was detected with anti-beta-actin antibody. Two replicates of BeauR-S-MM P 3 -CK and BeauR-M41-S-BSM P 3 -CK were used. Bands corresponding to uncleaved spike, the S2 subunit, and the S2′ cleavage product are labeled. The S2′ cleavage product was detected in lanes 2, 7, and 8 only.
    Figure Legend Snippet: Proteolytic cleavage of rIBVs at the S2′ site is dependent on the Beaudette-specific motif. Chick kidney cells in 6-well plates were mock infected (lane 1) or infected with Beau-R (lane 2), M41-CK (lane 3), BeauR-M41(S) (lane 4), BeauR-S-MM P 3 -CK (lanes 5 and 6), or BeauR-M41-S-BSM P 3 -CK (lanes 7 and 8). Cells were lysed at 24 h postinfection, and spike glycoproteins were analyzed by Western blotting with anti-S2 antibody. Actin was detected with anti-beta-actin antibody. Two replicates of BeauR-S-MM P 3 -CK and BeauR-M41-S-BSM P 3 -CK were used. Bands corresponding to uncleaved spike, the S2 subunit, and the S2′ cleavage product are labeled. The S2′ cleavage product was detected in lanes 2, 7, and 8 only.

    Techniques Used: Infection, Western Blot, Labeling

    10) Product Images from "Function of HNRNPC in breast cancer cells by controlling the dsRNA‐induced interferon response"

    Article Title: Function of HNRNPC in breast cancer cells by controlling the dsRNA‐induced interferon response

    Journal: The EMBO Journal

    doi: 10.15252/embj.201899017

    Up‐regulated ISG expression and suppressed MCF 7 and T47D proliferation upon HNRNPC repression mediated via the interferon beta signaling pathway In the siRNA‐transfected MCF7 (left) or T47D cells (right), the interferon signaling pathway was blocked at different stages by means of IFNβ neutralization (A), IFNAR2 neutralization (B), or JAK‐STAT inhibition (C). The expressions of the ISGs were measured by qPCR. Each sample has three replicates. Data represent mean ± SD. Growth curves of the MCF7 (D) or T47D cells (E) upon HNRNPC knock‐down but with the interferon response blocked with the IFNβ antibody. Each sample has three replicates. Data represent mean ± SD. Growth curves of the MCF7 (left) or T47D (right) cells upon HNRNPC knock‐down and JAK‐STAT inhibition with ruxolitinib (5 μM). siNC: non‐targeting siRNA as a negative control, siLMNA: siRNA for LMNA as another negative control, siHN‐1: siRNA sequence 1 for HNRNPC, siHN‐2: siRNA sequence 2 for HNRNPC. Each sample has three replicates. Data represent mean ± SD.
    Figure Legend Snippet: Up‐regulated ISG expression and suppressed MCF 7 and T47D proliferation upon HNRNPC repression mediated via the interferon beta signaling pathway In the siRNA‐transfected MCF7 (left) or T47D cells (right), the interferon signaling pathway was blocked at different stages by means of IFNβ neutralization (A), IFNAR2 neutralization (B), or JAK‐STAT inhibition (C). The expressions of the ISGs were measured by qPCR. Each sample has three replicates. Data represent mean ± SD. Growth curves of the MCF7 (D) or T47D cells (E) upon HNRNPC knock‐down but with the interferon response blocked with the IFNβ antibody. Each sample has three replicates. Data represent mean ± SD. Growth curves of the MCF7 (left) or T47D (right) cells upon HNRNPC knock‐down and JAK‐STAT inhibition with ruxolitinib (5 μM). siNC: non‐targeting siRNA as a negative control, siLMNA: siRNA for LMNA as another negative control, siHN‐1: siRNA sequence 1 for HNRNPC, siHN‐2: siRNA sequence 2 for HNRNPC. Each sample has three replicates. Data represent mean ± SD.

    Techniques Used: Expressing, Transfection, Neutralization, Inhibition, Real-time Polymerase Chain Reaction, Negative Control, Sequencing

    11) Product Images from "Beta-sheet assembly of Tau and neurodegeneration in Drosophila melanogaster"

    Article Title: Beta-sheet assembly of Tau and neurodegeneration in Drosophila melanogaster

    Journal: Neurobiology of Aging

    doi: 10.1016/j.neurobiolaging.2018.07.022

    Expression of human Tau in Drosophila . (A) Western blot for hTau (antibody T46) of the heads of 30-day-old flies. Beta-actin served as the control. (B) Wild-type Tau-383 and Δ(306–311) Tau-383 flies expressed similar levels of transgenic human protein (n = 3, different crosses). (C) Immunohistochemistry with anti-Tau antibody HT7 of brain using 4 μm frontal paraffin sections of 30-day-old flies. Wild-type (ELAV-Gal4) and transgenic (ELAV-Gal4;hTau WT and ELAV-Gal4;hTAU Δ(306−311) flies were used.
    Figure Legend Snippet: Expression of human Tau in Drosophila . (A) Western blot for hTau (antibody T46) of the heads of 30-day-old flies. Beta-actin served as the control. (B) Wild-type Tau-383 and Δ(306–311) Tau-383 flies expressed similar levels of transgenic human protein (n = 3, different crosses). (C) Immunohistochemistry with anti-Tau antibody HT7 of brain using 4 μm frontal paraffin sections of 30-day-old flies. Wild-type (ELAV-Gal4) and transgenic (ELAV-Gal4;hTau WT and ELAV-Gal4;hTAU Δ(306−311) flies were used.

    Techniques Used: Expressing, Western Blot, Transgenic Assay, Immunohistochemistry

    Δ (306–311) in Tau-383 flies reduces Tau phosphorylation. (A) Western blot and (B) quantitation of hTau phosphorylation. The following anti-Tau antibodies were used: Tau46, AT270, AT8, and AT180. Beta-actin served as the control. Two-way ANOVA followed by Turkey's post hoc test: **** p
    Figure Legend Snippet: Δ (306–311) in Tau-383 flies reduces Tau phosphorylation. (A) Western blot and (B) quantitation of hTau phosphorylation. The following anti-Tau antibodies were used: Tau46, AT270, AT8, and AT180. Beta-actin served as the control. Two-way ANOVA followed by Turkey's post hoc test: **** p

    Techniques Used: Western Blot, Quantitation Assay

    12) Product Images from "Extensive epigenomic integration of the glucocorticoid response in primary human monocytes and in vitro derived macrophages"

    Article Title: Extensive epigenomic integration of the glucocorticoid response in primary human monocytes and in vitro derived macrophages

    Journal: Scientific Reports

    doi: 10.1038/s41598-019-39395-9

    Genome-wide GR localisation patterns and underlying TF motif analysis. ( a ) Glucocorticoid receptor (GR) protein levels in Mo and Mf, treated or not with 1 μM TA for 4 hours. Beta-actin was used as internal loading control antigen. ( b ) RNA-seq signal at the NR3C1 gene, which codes for GR, in Mo and Mf exposed for four hours to TA. ( c ) GR ChIP-seq signal intensity in Mo and Mf at 877 high confidence GR ChIP-seq peaks was used to define four sets of GR peaks (MoMf, Mo, Mf and ‘Weak’). Overlap with a previously determined set of Mo and Mf DHS 43 is indicated by darker shading. The inset indicates the percentage of peaks that overlap with these DHS. ( d ) Enriched motifs in the four types of GR-bound regions sorted as a function of the TF superfamily they relate to. Colouring is based on the fractional difference between background and target frequencies. ( e ) Motif localisation density in the 401 MoMf-GR peaks, depicted as 40 bins of 20 bp.
    Figure Legend Snippet: Genome-wide GR localisation patterns and underlying TF motif analysis. ( a ) Glucocorticoid receptor (GR) protein levels in Mo and Mf, treated or not with 1 μM TA for 4 hours. Beta-actin was used as internal loading control antigen. ( b ) RNA-seq signal at the NR3C1 gene, which codes for GR, in Mo and Mf exposed for four hours to TA. ( c ) GR ChIP-seq signal intensity in Mo and Mf at 877 high confidence GR ChIP-seq peaks was used to define four sets of GR peaks (MoMf, Mo, Mf and ‘Weak’). Overlap with a previously determined set of Mo and Mf DHS 43 is indicated by darker shading. The inset indicates the percentage of peaks that overlap with these DHS. ( d ) Enriched motifs in the four types of GR-bound regions sorted as a function of the TF superfamily they relate to. Colouring is based on the fractional difference between background and target frequencies. ( e ) Motif localisation density in the 401 MoMf-GR peaks, depicted as 40 bins of 20 bp.

    Techniques Used: Genome Wide, RNA Sequencing Assay, Chromatin Immunoprecipitation

    13) Product Images from "The S2 Subunit of Infectious Bronchitis Virus Beaudette Is a Determinant of Cellular Tropism"

    Article Title: The S2 Subunit of Infectious Bronchitis Virus Beaudette Is a Determinant of Cellular Tropism

    Journal: Journal of Virology

    doi: 10.1128/JVI.01044-18

    Proteolytic cleavage of rIBVs at the S2′ site is dependent on the Beaudette-specific motif. Chick kidney cells in 6-well plates were mock infected (lane 1) or infected with Beau-R (lane 2), M41-CK (lane 3), BeauR-M41(S) (lane 4), BeauR-S-MM P 3 -CK (lanes 5 and 6), or BeauR-M41-S-BSM P 3 -CK (lanes 7 and 8). Cells were lysed at 24 h postinfection, and spike glycoproteins were analyzed by Western blotting with anti-S2 antibody. Actin was detected with anti-beta-actin antibody. Two replicates of BeauR-S-MM P 3 -CK and BeauR-M41-S-BSM P 3 -CK were used. Bands corresponding to uncleaved spike, the S2 subunit, and the S2′ cleavage product are labeled. The S2′ cleavage product was detected in lanes 2, 7, and 8 only.
    Figure Legend Snippet: Proteolytic cleavage of rIBVs at the S2′ site is dependent on the Beaudette-specific motif. Chick kidney cells in 6-well plates were mock infected (lane 1) or infected with Beau-R (lane 2), M41-CK (lane 3), BeauR-M41(S) (lane 4), BeauR-S-MM P 3 -CK (lanes 5 and 6), or BeauR-M41-S-BSM P 3 -CK (lanes 7 and 8). Cells were lysed at 24 h postinfection, and spike glycoproteins were analyzed by Western blotting with anti-S2 antibody. Actin was detected with anti-beta-actin antibody. Two replicates of BeauR-S-MM P 3 -CK and BeauR-M41-S-BSM P 3 -CK were used. Bands corresponding to uncleaved spike, the S2 subunit, and the S2′ cleavage product are labeled. The S2′ cleavage product was detected in lanes 2, 7, and 8 only.

    Techniques Used: Infection, Western Blot, Labeling

    14) Product Images from "Differential Expressions of Synaptogenic Markers between Primary Cultured Cortical and Hippocampal Neurons"

    Article Title: Differential Expressions of Synaptogenic Markers between Primary Cultured Cortical and Hippocampal Neurons

    Journal: Experimental Neurobiology

    doi: 10.5607/en.2012.21.2.61

    Western blotting of GAP43 and synaptophysin in cortical and hippocampal neurons. In this figure, GAP43 and synaptophysin bands are digitized and appeared on the graphs as volules of intensities according to beta actins respectively. Expression levels of GAP43 (A) and synaptophysin (B) according to the time courses of in vitro are shown in hippocampal and cortical neurons.
    Figure Legend Snippet: Western blotting of GAP43 and synaptophysin in cortical and hippocampal neurons. In this figure, GAP43 and synaptophysin bands are digitized and appeared on the graphs as volules of intensities according to beta actins respectively. Expression levels of GAP43 (A) and synaptophysin (B) according to the time courses of in vitro are shown in hippocampal and cortical neurons.

    Techniques Used: Western Blot, Expressing, In Vitro

    15) Product Images from "Beta-sheet assembly of Tau and neurodegeneration in Drosophila melanogaster"

    Article Title: Beta-sheet assembly of Tau and neurodegeneration in Drosophila melanogaster

    Journal: Neurobiology of Aging

    doi: 10.1016/j.neurobiolaging.2018.07.022

    Expression of human Tau in Drosophila . (A) Western blot for hTau (antibody T46) of the heads of 30-day-old flies. Beta-actin served as the control. (B) Wild-type Tau-383 and Δ(306–311) Tau-383 flies expressed similar levels of transgenic human protein (n = 3, different crosses). (C) Immunohistochemistry with anti-Tau antibody HT7 of brain using 4 μm frontal paraffin sections of 30-day-old flies. Wild-type (ELAV-Gal4) and transgenic (ELAV-Gal4;hTau WT and ELAV-Gal4;hTAU Δ(306−311) flies were used.
    Figure Legend Snippet: Expression of human Tau in Drosophila . (A) Western blot for hTau (antibody T46) of the heads of 30-day-old flies. Beta-actin served as the control. (B) Wild-type Tau-383 and Δ(306–311) Tau-383 flies expressed similar levels of transgenic human protein (n = 3, different crosses). (C) Immunohistochemistry with anti-Tau antibody HT7 of brain using 4 μm frontal paraffin sections of 30-day-old flies. Wild-type (ELAV-Gal4) and transgenic (ELAV-Gal4;hTau WT and ELAV-Gal4;hTAU Δ(306−311) flies were used.

    Techniques Used: Expressing, Western Blot, Transgenic Assay, Immunohistochemistry

    Δ (306–311) in Tau-383 flies reduces Tau phosphorylation. (A) Western blot and (B) quantitation of hTau phosphorylation. The following anti-Tau antibodies were used: Tau46, AT270, AT8, and AT180. Beta-actin served as the control. Two-way ANOVA followed by Turkey's post hoc test: **** p
    Figure Legend Snippet: Δ (306–311) in Tau-383 flies reduces Tau phosphorylation. (A) Western blot and (B) quantitation of hTau phosphorylation. The following anti-Tau antibodies were used: Tau46, AT270, AT8, and AT180. Beta-actin served as the control. Two-way ANOVA followed by Turkey's post hoc test: **** p

    Techniques Used: Western Blot, Quantitation Assay

    16) Product Images from "Identification of cell surface glycoprotein markers for glioblastoma-derived stem-like cells using a lectin microarray and LC-MS/MS approach"

    Article Title: Identification of cell surface glycoprotein markers for glioblastoma-derived stem-like cells using a lectin microarray and LC-MS/MS approach

    Journal: Journal of proteome research

    doi: 10.1021/pr100012p

    Western blotting analysis of selected proteins Twenty micrograms of proteins from HSR-GBM1, U373, U87 and T98G cells were separated by 4–20% SDS-PAGE and transferred to PVDF membranes. The blots were probed with antibodies against Podocalyxin-like protein 1 (PODXL), Chondroitin sulfate proteoglycan NG2 (NG2), Tenascin-C (TNC), Receptor-type tyrosine-protein phosphatase zeta (PTPRZ1), CD90, CD44 and Beta-actin. GBM1 represents HSR-GBM1.
    Figure Legend Snippet: Western blotting analysis of selected proteins Twenty micrograms of proteins from HSR-GBM1, U373, U87 and T98G cells were separated by 4–20% SDS-PAGE and transferred to PVDF membranes. The blots were probed with antibodies against Podocalyxin-like protein 1 (PODXL), Chondroitin sulfate proteoglycan NG2 (NG2), Tenascin-C (TNC), Receptor-type tyrosine-protein phosphatase zeta (PTPRZ1), CD90, CD44 and Beta-actin. GBM1 represents HSR-GBM1.

    Techniques Used: Western Blot, SDS Page

    17) Product Images from "High Expression of Galectin-3 in Patients with IgG4-Related Disease: A Proteomic Approach"

    Article Title: High Expression of Galectin-3 in Patients with IgG4-Related Disease: A Proteomic Approach

    Journal: Pathology Research International

    doi: 10.1155/2017/9312142

    Validation of galectin-3 expression in patients' tissues . (a) LGALS-3 expression was higher in IgG4-related pancreatitis patients compared to controls. Data are presented as the mean relative expression ratio between the mRNA levels of the LGALS3 gene and the expression of GAPDH . Error bars, standard error of the mean (SEM). (b) Immunoblot analysis showing higher galectin-3 protein levels in IgG4-related pancreatitis samples ( n = 5) compared with those in the normal pancreas samples ( n = 4). (c) Quantification of the immunoblot presented in panel (b). Mean band intensity ratio was measured as intensity of galectin-3 band divided by the intensity of the corresponding beta actin band. Bar graphs represent mean values. Error bars, SEM. (d, e) Immunolocalization of galectin-3 in IgG4-RD samples ((d) pancreas; (e) submandibular gland). Note that lymphoid cells in (d) were negative for galectin-3. Scale bar, 20 μ m. (f) Average galectin-3 positive cells in the stroma in different organs in IgG4-RD patients. Positive cells were counted in 3HPF. Numbers in parentheses represent the number of cases. Bar graphs represent mean values. Error bars, SEM.
    Figure Legend Snippet: Validation of galectin-3 expression in patients' tissues . (a) LGALS-3 expression was higher in IgG4-related pancreatitis patients compared to controls. Data are presented as the mean relative expression ratio between the mRNA levels of the LGALS3 gene and the expression of GAPDH . Error bars, standard error of the mean (SEM). (b) Immunoblot analysis showing higher galectin-3 protein levels in IgG4-related pancreatitis samples ( n = 5) compared with those in the normal pancreas samples ( n = 4). (c) Quantification of the immunoblot presented in panel (b). Mean band intensity ratio was measured as intensity of galectin-3 band divided by the intensity of the corresponding beta actin band. Bar graphs represent mean values. Error bars, SEM. (d, e) Immunolocalization of galectin-3 in IgG4-RD samples ((d) pancreas; (e) submandibular gland). Note that lymphoid cells in (d) were negative for galectin-3. Scale bar, 20 μ m. (f) Average galectin-3 positive cells in the stroma in different organs in IgG4-RD patients. Positive cells were counted in 3HPF. Numbers in parentheses represent the number of cases. Bar graphs represent mean values. Error bars, SEM.

    Techniques Used: Expressing

    18) Product Images from "RTKN2 Induces NF-KappaB Dependent Resistance to Intrinsic Apoptosis in HEK Cells and Regulates BCL-2 Genes in Human CD4+ Lymphocytes"

    Article Title: RTKN2 Induces NF-KappaB Dependent Resistance to Intrinsic Apoptosis in HEK Cells and Regulates BCL-2 Genes in Human CD4+ Lymphocytes

    Journal: Journal of Cell Death

    doi:

    Western blot analysis of phosphorylated NF-KappaB. Three days following passage of the cells CAT control and RTKN2 cells were lysed for protein analysis. The total protein was estimated and approximately 20 ug of each sample was denatured and run under reducing conditions on a 4%–20% gradient SDS PAGE gel, before transfer and blotting with anti-phospho NF-KappaB, and anti-rabbit HRP, The protein loading was quantitated using anti-beta actin. The HRP was visualized using ECL reagent and imaged using the UVP ChemiDoc-It Imaging System (DKSH). The level of phospho-NF-KappaB was greater in the RTKN2 cells.
    Figure Legend Snippet: Western blot analysis of phosphorylated NF-KappaB. Three days following passage of the cells CAT control and RTKN2 cells were lysed for protein analysis. The total protein was estimated and approximately 20 ug of each sample was denatured and run under reducing conditions on a 4%–20% gradient SDS PAGE gel, before transfer and blotting with anti-phospho NF-KappaB, and anti-rabbit HRP, The protein loading was quantitated using anti-beta actin. The HRP was visualized using ECL reagent and imaged using the UVP ChemiDoc-It Imaging System (DKSH). The level of phospho-NF-KappaB was greater in the RTKN2 cells.

    Techniques Used: Western Blot, SDS Page, Imaging

    19) Product Images from "The transcription factor STAT5 catalyzes Mannich ligation reactions yielding inhibitors of leukemic cell proliferation"

    Article Title: The transcription factor STAT5 catalyzes Mannich ligation reactions yielding inhibitors of leukemic cell proliferation

    Journal: Nature Communications

    doi: 10.1038/s41467-018-07923-2

    Activity, target occupancy, and functional effects of STAT5 inhibitor 16 tested in STAT5-dependent cells. a 16 blocks tyrosine phosphorylation of STAT5 in a dose-dependent manner as shown by western blot analysis in BaF3/FLT3-ITD cells after 6 h treatment. Relative STAT5 phosphorylation levels were plotted as after quantification using Image J software. Immunoblotting for beta-actin was used as a control for uniform protein loading ( n = 3). b Compound 16 inhibits transcriptional activity of STAT5 in BaF3/FLT3-ITD cells as measured by normalized Fluc/Rluc ratio in dual luciferase reporter assay ( n = 3). c Expression of downstream targets of STAT5 Pim1,BcL-xL and Cis was reduced after 18 h of treatment with compound 16 . Gene expression was quantified by quantitative PCR ( n = 3). d Compound 16 inhibits the proliferation of BaF3/FLT3-ITD cells after 48 h as determined by the Alamar Blue assay ( n = 3). e , i BaF3/FLT3-ITD cells were treated with compound 16 after which annexin-V/propidium iodide staining and flow cytometry were performed (gating strategy as in Supplementary Figure 11a , data shown are one representative of n = 3); ( ii ) Intracellular levels of phosphorylated STAT5 were evaluated by flow cytometry after 6 h exposure of cells to compound 16 for 50 µ m (gating strategy as in Supplementary Figure 11b , data shown are one representative of n = 3). f–g , In-cell occupancy of STAT5a and STAT5b by compound 16 in BaF3/FLT3-ITD, determined using ITDRF. ITDRF of compound 16 on STAT5a and STAT5b denaturization at 60 °C for 3 min based on raw data from western blotting chemiluminescence readings ( n = 3). CETSA, cellular thermal shift assay; ITDRF, isothermal dose–response fingerprint; OC 50 , the concentration at which 50% of the STAT5 in the cell was occupied by inhibitor. For an uncropped image of panels f and g see Supplementary Figure 10. Error bars denote mean ± S.D. and p values are considered as follows: ** p value
    Figure Legend Snippet: Activity, target occupancy, and functional effects of STAT5 inhibitor 16 tested in STAT5-dependent cells. a 16 blocks tyrosine phosphorylation of STAT5 in a dose-dependent manner as shown by western blot analysis in BaF3/FLT3-ITD cells after 6 h treatment. Relative STAT5 phosphorylation levels were plotted as after quantification using Image J software. Immunoblotting for beta-actin was used as a control for uniform protein loading ( n = 3). b Compound 16 inhibits transcriptional activity of STAT5 in BaF3/FLT3-ITD cells as measured by normalized Fluc/Rluc ratio in dual luciferase reporter assay ( n = 3). c Expression of downstream targets of STAT5 Pim1,BcL-xL and Cis was reduced after 18 h of treatment with compound 16 . Gene expression was quantified by quantitative PCR ( n = 3). d Compound 16 inhibits the proliferation of BaF3/FLT3-ITD cells after 48 h as determined by the Alamar Blue assay ( n = 3). e , i BaF3/FLT3-ITD cells were treated with compound 16 after which annexin-V/propidium iodide staining and flow cytometry were performed (gating strategy as in Supplementary Figure 11a , data shown are one representative of n = 3); ( ii ) Intracellular levels of phosphorylated STAT5 were evaluated by flow cytometry after 6 h exposure of cells to compound 16 for 50 µ m (gating strategy as in Supplementary Figure 11b , data shown are one representative of n = 3). f–g , In-cell occupancy of STAT5a and STAT5b by compound 16 in BaF3/FLT3-ITD, determined using ITDRF. ITDRF of compound 16 on STAT5a and STAT5b denaturization at 60 °C for 3 min based on raw data from western blotting chemiluminescence readings ( n = 3). CETSA, cellular thermal shift assay; ITDRF, isothermal dose–response fingerprint; OC 50 , the concentration at which 50% of the STAT5 in the cell was occupied by inhibitor. For an uncropped image of panels f and g see Supplementary Figure 10. Error bars denote mean ± S.D. and p values are considered as follows: ** p value

    Techniques Used: Activity Assay, Functional Assay, Western Blot, Software, Luciferase, Reporter Assay, Expressing, Real-time Polymerase Chain Reaction, Alamar Blue Assay, Staining, Flow Cytometry, Cytometry, Thermal Shift Assay, Concentration Assay

    20) Product Images from "Targeting Superoxide Dismutase to Endothelial Caveolae Profoundly Alleviates Inflammation Caused by Endotoxin"

    Article Title: Targeting Superoxide Dismutase to Endothelial Caveolae Profoundly Alleviates Inflammation Caused by Endotoxin

    Journal: Journal of controlled release : official journal of the Controlled Release Society

    doi: 10.1016/j.jconrel.2017.12.025

    Protection by Plvap Ab/SOD conjugate against systemic inflammation Mice were injected i.v. with Ab/SOD (75 µg) 15 min prior LPS (0.8 µg/kg). After 5 h blood was collected and markers of systemic inflammation interferon-beta (a), interferon-gamma (B) and IL-27 (C) were measured in plasma using flow cytometry. n≥3; *P
    Figure Legend Snippet: Protection by Plvap Ab/SOD conjugate against systemic inflammation Mice were injected i.v. with Ab/SOD (75 µg) 15 min prior LPS (0.8 µg/kg). After 5 h blood was collected and markers of systemic inflammation interferon-beta (a), interferon-gamma (B) and IL-27 (C) were measured in plasma using flow cytometry. n≥3; *P

    Techniques Used: Mouse Assay, Injection, Flow Cytometry, Cytometry

    21) Product Images from "Effect of Rat Medicated Serum Containing Zuo Gui Wan and/or You Gui Wan on the Differentiation of Stem Cells Derived from Human First Trimester Umbilical Cord into Oocyte-Like Cells In Vitro"

    Article Title: Effect of Rat Medicated Serum Containing Zuo Gui Wan and/or You Gui Wan on the Differentiation of Stem Cells Derived from Human First Trimester Umbilical Cord into Oocyte-Like Cells In Vitro

    Journal: Evidence-based Complementary and Alternative Medicine : eCAM

    doi: 10.1155/2015/825805

    Western blot analysis of protein expression. (a), (b), and (c) show western blotting of expressions of Oct4 (MW = 45 kd), Stella (MW = 23 kd), GDF9 (MW = 51 kd), and ZP1 (MW = 70 kd) on day 0, day 7, and day 24 after treatment with the rat medicated serums containing common ingredients of ZGW/YGW, YGW, and ZGW, respectively. (d) shows western blotting of expressions of Oct4, Stella, GDF9, and ZP1 in stems cells treated with normal rat serum. Beta-actin (MW = 42 kd) was used as an internal control.
    Figure Legend Snippet: Western blot analysis of protein expression. (a), (b), and (c) show western blotting of expressions of Oct4 (MW = 45 kd), Stella (MW = 23 kd), GDF9 (MW = 51 kd), and ZP1 (MW = 70 kd) on day 0, day 7, and day 24 after treatment with the rat medicated serums containing common ingredients of ZGW/YGW, YGW, and ZGW, respectively. (d) shows western blotting of expressions of Oct4, Stella, GDF9, and ZP1 in stems cells treated with normal rat serum. Beta-actin (MW = 42 kd) was used as an internal control.

    Techniques Used: Western Blot, Expressing

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    Expressing:

    Article Title: MicroRNA-21 regulates the proliferation and apoptosis of cervical cancer cells via tumor necrosis factor-α
    Article Snippet: .. Expression levels of TNF-α were analyzed with β-actin (1:2,500; Abcam; cat. no. ab8227) serving as an internal control. .. The cell suspension was counted after transfected cells were seeded into 96-well plates at a density of 1×104 cells/well.

    Bradford Protein Assay:

    Article Title: Divergent effects of RIP1 or RIP3 blockade in murine models of acute liver injury
    Article Snippet: .. After determining total protein by Bradford protein assay, 10% polyacrylamide gels (NuPage, Invitrogen, Grand Island, NY, USA) were equiloaded, electrophoresed at 200 V, electrotransferred to PVDF membranes, and probed with monoclonal antibodies to β -actin (no. ab8227), c-FLIP (no. ab8421), FADD (no. ab24533), RIP3 (no. ab152130, all Abcam), RIP1 (no. 3493), Caspase 1 (no. 2225), Caspase 3 (no. 9664S), and Caspase 8 (no. 4790). .. Blots were developed by ECL (Thermo Scientific, Ashvile, NC, USA).

    SDS Page:

    Article Title: HNF1B expression regulates ECI2 gene expression, potentially serving a role in prostate cancer progression
    Article Snippet: .. The protein samples were separated by SDS-PAGE on a 12% gel, at 50 V for 3 h, transferred to a polyvinylidene difluoride membrane, and blocked in 3% BSA in TBS with Tween-20 at room temperature for 1 h. The membrane was probed with anti-HNF1B antibody (cat. no. CL0374; Abnova; 1:300 dilution), anti-ECI2 antibody (cat. no. 201243; Creative Diagnostics; 1:500 dilution) or anti-β-actin antibody (cat. no. ab8227; Abcam; 1:1,000 dilution) overnight at 4°C. .. Following washing three times with 1X PBS with Tween 20, the membrane was incubated with a specific HRP-conjugated secondary antibody (anti-mouse IgG HRP; Abcam; cat. no. ab6789; 1:5,000 dilution) or (anti-rabbit IgG HRP; Abcam; cat. no. ab6721; 1:4,000 dilution) at room temperature for 2 h. Following incubation, the membrane was washed with 1X PBST and developed using a diaminobenzidine substrate kit (Abcam; cat. no. ab64238).

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    Abcam rabbit anti mouse α sma
    Candidate stem cell marker CD146 associated with small blood vessels in the odontoblast layer are reduced in the Bmp2-cKO Sp7-Cre-EGFP model, and αSma + stem cells in the cervical and apical regions of the periodontium are also greatly reduced in the Bmp2-cKO Sp7-Cre-EGFP model. ( a – d ) Candidate stem cell marker CD146 immunocytochemistry localized within the dental pulp ( a – d , purple arrows) and in association with blood vessels adjacent to the odontoblast layer ( a – d , blue arrows) on capillaries. CD146 protein expression is greatly reduced in the Bmp2-cKO Sp7-Cre-EGFP in 1-month-old mice (×200). a and b are from the third molars, and c and d are from incisor cervical loop region. Candidate stem cells, marked with <t>α-SMA</t> immunocytochemistry are noted all within the periodontium of the first and second molars (data shown in Supplementary Figure S7 ) and in the less developed dental follicle cells of the third molars ( e and f , black arrow), and apical papilla region ( g and h , black arrow). Expression of α-SMA stem cell marker is greatly reduced in the Bmp2-cKO Sp7-Cre-EGFP mice ( h ) as compared to control ( g ), example from the second molar, 1 month of age, and shown at ×200. Bmp2, bone morphogenetic protein-2.
    Rabbit Anti Mouse α Sma, supplied by Abcam, used in various techniques. Bioz Stars score: 88/100, based on 7 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Abcam antibodies targeting α sma
    GPER is expressed in primary and immortalized breast CAFs. (A) CAFs were identified by immunofluorescent staining with <t>α-SMA</t> and FAP. ERs were detected in primary breast CAFs, immortalized CAFs (CAF-hTERT), and MCF-7 cells as positive controls. Scale bars: 25 μm. (B) ER mRNA expression was evaluated by quantitative real-time RT-PCR in primary CAFs, CAF-hTERT cells, and MCF-7 cells. Gene expression was normalized to GAPDH , and results are shown as fold changes of mRNA levels compared with MCF-7 cells. The data are shown as means± s.d . for three independent experiments.
    Antibodies Targeting α Sma, supplied by Abcam, used in various techniques. Bioz Stars score: 86/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Abcam mouse anti human β actin
    PRKDC knockdown in NGP cells confirms DNA-PKcs-dependent radiosensitizing activity of NU7026. (A) PRKDC mRNA expression in NGP cells at 144 h after transduction with nonspecific control shRNA (SHC002) or PRKDC shRNA. PRKDC mRNA levels were determined by qPCR and ΔCt values were normalized to the household gene <t>β-actin.</t> Normalized ΔCt values of untreated non-transduced NGP cells (no virus) were set at zero, giving ΔΔCt. Data represent the mean (n = 4) +/- SD. (B) FACS analysis of the effects of treatment with 0.63 Gy IR on the sub-G1 fraction of normal NGP cells and NGP cells transduced with SHC002 or PRKDC shRNA. Results are obtained at 96 h after IR-exposure of the cells. (C) Sub-G1 fraction of NGP cells transduced with SHC002 or PRKDC shRNA after non-treatment and after treatment with 0.63 Gy IR, at 48, 72 and 96 h after irradiation. (D) Western Blot analysis of protein levels of DNA-PKcs and cleaved PARP in non-irradiated and irradiated normal NGP cells and NGP cells transduced with SHC002 or PRKDC shRNA. Results were obtained at 120 h after irradiation, which was equal to 168 h after transduction. β-actin protein levels were used as loading control.
    Mouse Anti Human β Actin, supplied by Abcam, used in various techniques. Bioz Stars score: 92/100, based on 18 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Abcam β actin
    Rat islet quality was improved with M101 use for pancreas preservation when injected in the organ. M101 was added in the preservation solution (A, B, C, D, E, F) and injected in the pancreas (D, E, F). A, D, Islets were counted using Islets Equivalents (IEQ) just after isolation (n = 5). B, E, p38 activation (phosphorylated <t>protein/β‐actin</t> ratio) was analysed by Western blot in islets (n = 3). C, F, Amount of insulin secreted by islets under glucose stimulation was quantified by ELISA (n = 5). ** P
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    Candidate stem cell marker CD146 associated with small blood vessels in the odontoblast layer are reduced in the Bmp2-cKO Sp7-Cre-EGFP model, and αSma + stem cells in the cervical and apical regions of the periodontium are also greatly reduced in the Bmp2-cKO Sp7-Cre-EGFP model. ( a – d ) Candidate stem cell marker CD146 immunocytochemistry localized within the dental pulp ( a – d , purple arrows) and in association with blood vessels adjacent to the odontoblast layer ( a – d , blue arrows) on capillaries. CD146 protein expression is greatly reduced in the Bmp2-cKO Sp7-Cre-EGFP in 1-month-old mice (×200). a and b are from the third molars, and c and d are from incisor cervical loop region. Candidate stem cells, marked with α-SMA immunocytochemistry are noted all within the periodontium of the first and second molars (data shown in Supplementary Figure S7 ) and in the less developed dental follicle cells of the third molars ( e and f , black arrow), and apical papilla region ( g and h , black arrow). Expression of α-SMA stem cell marker is greatly reduced in the Bmp2-cKO Sp7-Cre-EGFP mice ( h ) as compared to control ( g ), example from the second molar, 1 month of age, and shown at ×200. Bmp2, bone morphogenetic protein-2.

    Journal: International Journal of Oral Science

    Article Title: Bone morphogenetic protein-2 gene controls tooth root development in coordination with formation of the periodontium

    doi: 10.1038/ijos.2013.41

    Figure Lengend Snippet: Candidate stem cell marker CD146 associated with small blood vessels in the odontoblast layer are reduced in the Bmp2-cKO Sp7-Cre-EGFP model, and αSma + stem cells in the cervical and apical regions of the periodontium are also greatly reduced in the Bmp2-cKO Sp7-Cre-EGFP model. ( a – d ) Candidate stem cell marker CD146 immunocytochemistry localized within the dental pulp ( a – d , purple arrows) and in association with blood vessels adjacent to the odontoblast layer ( a – d , blue arrows) on capillaries. CD146 protein expression is greatly reduced in the Bmp2-cKO Sp7-Cre-EGFP in 1-month-old mice (×200). a and b are from the third molars, and c and d are from incisor cervical loop region. Candidate stem cells, marked with α-SMA immunocytochemistry are noted all within the periodontium of the first and second molars (data shown in Supplementary Figure S7 ) and in the less developed dental follicle cells of the third molars ( e and f , black arrow), and apical papilla region ( g and h , black arrow). Expression of α-SMA stem cell marker is greatly reduced in the Bmp2-cKO Sp7-Cre-EGFP mice ( h ) as compared to control ( g ), example from the second molar, 1 month of age, and shown at ×200. Bmp2, bone morphogenetic protein-2.

    Article Snippet: Immunohistochemistry Immunohistochemistry was performed as previously described., Primary antibodies included polyclonal rabbit anti-mouse vascular endothelial growth factor A (VEGF-A), Ab9571 (1∶200), rabbit anti-mouse CD146, Ab75769 (1∶200) and rabbit anti-mouse α-SMA, Ab5694 (1∶200), were obtained from Abcam Limited (Boston, MA, USA).

    Techniques: Marker, Immunocytochemistry, Expressing, Mouse Assay

    GPER is expressed in primary and immortalized breast CAFs. (A) CAFs were identified by immunofluorescent staining with α-SMA and FAP. ERs were detected in primary breast CAFs, immortalized CAFs (CAF-hTERT), and MCF-7 cells as positive controls. Scale bars: 25 μm. (B) ER mRNA expression was evaluated by quantitative real-time RT-PCR in primary CAFs, CAF-hTERT cells, and MCF-7 cells. Gene expression was normalized to GAPDH , and results are shown as fold changes of mRNA levels compared with MCF-7 cells. The data are shown as means± s.d . for three independent experiments.

    Journal: Endocrine-Related Cancer

    Article Title: GPER-mediated proliferation and estradiol production in breast cancer-associated fibroblasts

    doi: 10.1530/ERC-13-0237

    Figure Lengend Snippet: GPER is expressed in primary and immortalized breast CAFs. (A) CAFs were identified by immunofluorescent staining with α-SMA and FAP. ERs were detected in primary breast CAFs, immortalized CAFs (CAF-hTERT), and MCF-7 cells as positive controls. Scale bars: 25 μm. (B) ER mRNA expression was evaluated by quantitative real-time RT-PCR in primary CAFs, CAF-hTERT cells, and MCF-7 cells. Gene expression was normalized to GAPDH , and results are shown as fold changes of mRNA levels compared with MCF-7 cells. The data are shown as means± s.d . for three independent experiments.

    Article Snippet: The cells were then incubated overnight at 4 °C with primary antibodies targeting α-SMA, FAP, and GPER (Abcam) and ERα and ERβ (ZSGB-BIO, Beijing, China); all dilutions were 1:150.

    Techniques: Staining, Expressing, Quantitative RT-PCR

    PRKDC knockdown in NGP cells confirms DNA-PKcs-dependent radiosensitizing activity of NU7026. (A) PRKDC mRNA expression in NGP cells at 144 h after transduction with nonspecific control shRNA (SHC002) or PRKDC shRNA. PRKDC mRNA levels were determined by qPCR and ΔCt values were normalized to the household gene β-actin. Normalized ΔCt values of untreated non-transduced NGP cells (no virus) were set at zero, giving ΔΔCt. Data represent the mean (n = 4) +/- SD. (B) FACS analysis of the effects of treatment with 0.63 Gy IR on the sub-G1 fraction of normal NGP cells and NGP cells transduced with SHC002 or PRKDC shRNA. Results are obtained at 96 h after IR-exposure of the cells. (C) Sub-G1 fraction of NGP cells transduced with SHC002 or PRKDC shRNA after non-treatment and after treatment with 0.63 Gy IR, at 48, 72 and 96 h after irradiation. (D) Western Blot analysis of protein levels of DNA-PKcs and cleaved PARP in non-irradiated and irradiated normal NGP cells and NGP cells transduced with SHC002 or PRKDC shRNA. Results were obtained at 120 h after irradiation, which was equal to 168 h after transduction. β-actin protein levels were used as loading control.

    Journal: PLoS ONE

    Article Title: DNA-Dependent Protein Kinase As Molecular Target for Radiosensitization of Neuroblastoma Cells

    doi: 10.1371/journal.pone.0145744

    Figure Lengend Snippet: PRKDC knockdown in NGP cells confirms DNA-PKcs-dependent radiosensitizing activity of NU7026. (A) PRKDC mRNA expression in NGP cells at 144 h after transduction with nonspecific control shRNA (SHC002) or PRKDC shRNA. PRKDC mRNA levels were determined by qPCR and ΔCt values were normalized to the household gene β-actin. Normalized ΔCt values of untreated non-transduced NGP cells (no virus) were set at zero, giving ΔΔCt. Data represent the mean (n = 4) +/- SD. (B) FACS analysis of the effects of treatment with 0.63 Gy IR on the sub-G1 fraction of normal NGP cells and NGP cells transduced with SHC002 or PRKDC shRNA. Results are obtained at 96 h after IR-exposure of the cells. (C) Sub-G1 fraction of NGP cells transduced with SHC002 or PRKDC shRNA after non-treatment and after treatment with 0.63 Gy IR, at 48, 72 and 96 h after irradiation. (D) Western Blot analysis of protein levels of DNA-PKcs and cleaved PARP in non-irradiated and irradiated normal NGP cells and NGP cells transduced with SHC002 or PRKDC shRNA. Results were obtained at 120 h after irradiation, which was equal to 168 h after transduction. β-actin protein levels were used as loading control.

    Article Snippet: After blocking, membranes were incubated with mouse anti-human β-actin (clone AC-15) monoclonal antibody (1:20000; Abcam) or mouse anti-human α-tubulin (clone DM1A) monoclonal antibody (1:10000) in OBB with 0.1% (v/v) Tween-20 (OBB-T) (overnight; 4°C).

    Techniques: Activity Assay, Expressing, Transduction, shRNA, Real-time Polymerase Chain Reaction, FACS, Irradiation, Western Blot

    Combination treatment with NU7026 and IR induces apoptosis in NGP cells. (A) Effects of NU7026 plus IR combination therapy versus monotherapy on the cell cycle status of NGP cells. For combination treatment, cells were pre-treated with 10 μM NU7026 for 1 h before exposure to 0.63 Gy IR. Samples were analyzed by FACS analysis at 96 h after treatment. (B) FACS analysis of the effects of combination therapy versus monotherapy on the sub-G1 fraction of cells at 48, 72 and 96 h after treatment. (C) Western Blot detection of total DNA-PKcs and activated DNA-PKcs (via phosphorylation at serine 2056) levels and PARP cleavage after combination therapy versus monotherapy with 10 μM NU7026 and/or 0.63 Gy IR, at 1 h and 96 h after IR-exposure, respectively. β-actin protein levels were used as loading control.

    Journal: PLoS ONE

    Article Title: DNA-Dependent Protein Kinase As Molecular Target for Radiosensitization of Neuroblastoma Cells

    doi: 10.1371/journal.pone.0145744

    Figure Lengend Snippet: Combination treatment with NU7026 and IR induces apoptosis in NGP cells. (A) Effects of NU7026 plus IR combination therapy versus monotherapy on the cell cycle status of NGP cells. For combination treatment, cells were pre-treated with 10 μM NU7026 for 1 h before exposure to 0.63 Gy IR. Samples were analyzed by FACS analysis at 96 h after treatment. (B) FACS analysis of the effects of combination therapy versus monotherapy on the sub-G1 fraction of cells at 48, 72 and 96 h after treatment. (C) Western Blot detection of total DNA-PKcs and activated DNA-PKcs (via phosphorylation at serine 2056) levels and PARP cleavage after combination therapy versus monotherapy with 10 μM NU7026 and/or 0.63 Gy IR, at 1 h and 96 h after IR-exposure, respectively. β-actin protein levels were used as loading control.

    Article Snippet: After blocking, membranes were incubated with mouse anti-human β-actin (clone AC-15) monoclonal antibody (1:20000; Abcam) or mouse anti-human α-tubulin (clone DM1A) monoclonal antibody (1:10000) in OBB with 0.1% (v/v) Tween-20 (OBB-T) (overnight; 4°C).

    Techniques: FACS, Western Blot

    Rat islet quality was improved with M101 use for pancreas preservation when injected in the organ. M101 was added in the preservation solution (A, B, C, D, E, F) and injected in the pancreas (D, E, F). A, D, Islets were counted using Islets Equivalents (IEQ) just after isolation (n = 5). B, E, p38 activation (phosphorylated protein/β‐actin ratio) was analysed by Western blot in islets (n = 3). C, F, Amount of insulin secreted by islets under glucose stimulation was quantified by ELISA (n = 5). ** P

    Journal: Journal of Cellular and Molecular Medicine

    Article Title: Beneficial effects of the novel marine oxygen carrier M101 during cold preservation of rat and human pancreas, et al. Beneficial effects of the novel marine oxygen carrier M101 during cold preservation of rat and human pancreas

    doi: 10.1111/jcmm.14666

    Figure Lengend Snippet: Rat islet quality was improved with M101 use for pancreas preservation when injected in the organ. M101 was added in the preservation solution (A, B, C, D, E, F) and injected in the pancreas (D, E, F). A, D, Islets were counted using Islets Equivalents (IEQ) just after isolation (n = 5). B, E, p38 activation (phosphorylated protein/β‐actin ratio) was analysed by Western blot in islets (n = 3). C, F, Amount of insulin secreted by islets under glucose stimulation was quantified by ELISA (n = 5). ** P

    Article Snippet: 2.1 Antibodies Primary antibodies against p‐AKT, AKT, p‐ERK1/2, ERK1/2, p‐p38, p38 (anti‐rabbit, 1:1000, Cell Signaling, Ozyme), β‐actin (anti‐rabbit, 1:10,000, Abcam) and HIF1‐α (antimouse, 1:100, Novus Biologicals) were used.

    Techniques: Preserving, Injection, Isolation, Activation Assay, Western Blot, Enzyme-linked Immunosorbent Assay