mouse anti actin  (Millipore)


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    Structured Review

    Millipore mouse anti actin
    Antisense GT insertions upstream of <t>LRP6</t> reduce LRP6 protein expression and impair WNT signaling. (A) The histogram indicates the number and orientation of GT insertions mapped to LRP6 and to the region ~12.5 kbp upstream of the TSS in unsorted cells and in the sorted cells from the WNT positive regulator low stringency screen. See legend to Fig 4A for details. The x-axis represents contiguous 250 bp bins to which insertions were mapped (Chromosome 12, 12116000–12279249 bp). (B) The histogram shows an expanded view of the 5’ end of LRP6 and the region ~12.5 kbp upstream of the TSS (left of the vertical dotted line), with traces for GT insertions mapped in unsorted cells and in the sorted cells from the WNT positive regulator low stringency screen. The x-axis represents contiguous 250 bp bins to which insertions were mapped (Chromosome 12, 12262500–12279249 bp). The green rectangle above the gene track indicates the location of the LRP6 promoter according to Ensembl and the black rectangle indicates the location of the bin identified in the upstream insertion enrichment analyses of the WNT positive regulator low stringency and high stringency screens. The black and orange stars denote the positions of the antisense GT insertions (located at NC_000012.13:g.12268371_12268372insGenetrap (Dec.2013: hg38, GRCh38) and NC_000012.13:g.12269383_12269384insGenetrap (Dec.2013: hg38, GRCh38) respectively [ 10 ]; see S2 File ) in the LRP6 GT -1(Up) and LRP6 GT -2(Up) clonal cell lines, respectively, and the blue star denotes the position of the sense GT insertion (located at NC_000012.13:g.12266072_12266073insGenetrap (Dec.2013: hg38, GRCh38); see S2 File ) in the LRP6 GT -3(Int) cell line. The inverted histogram below the RefSeq gene track for LRP6 indicates the maximum CAGE read count found in any tissue sample from the FANTOM5 database [ 11 ]. (C) Fold-induction in WNT reporter (median +/- SEM EGFP fluorescence from 20,000 cells) following treatment with 50% WNT3A CM. (D) Fold-induction in AXIN2 mRNA (average +/- SD of AXIN2 mRNA normalized to HPRT1 mRNA, each measured in triplicate qPCR reactions) following treatment with 50% WNT3A CM. (E) Quantification of immunoblot analysis of total LRP6 protein (average +/- SD LRP6 intensity normalized to <t>ACTIN</t> intensity from samples run in duplicate) shown as percentage of WT HAP1-7TGP. The blot used for quantification is shown in C in S3 Fig . (F) Cell surface LRP6 protein (median +/- SEM cell surface LRP6 immunofluorescence from 20,000 cells) shown as percentage of WT HAP1-7TGP. (G) LRP6 mRNA (average +/- SD of LRP6 mRNA, measured using two different primer pairs, normalized to HPRT1 mRNA, each measured in triplicate qPCR reactions) shown relative to WT HAP1-7TGP cells.
    Mouse Anti Actin, supplied by Millipore, used in various techniques. Bioz Stars score: 99/100, based on 19 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/mouse anti actin/product/Millipore
    Average 99 stars, based on 19 article reviews
    Price from $9.99 to $1999.99
    mouse anti actin - by Bioz Stars, 2020-09
    99/100 stars

    Images

    1) Product Images from "Discovery of gene regulatory elements through a new bioinformatics analysis of haploid genetic screens"

    Article Title: Discovery of gene regulatory elements through a new bioinformatics analysis of haploid genetic screens

    Journal: PLoS ONE

    doi: 10.1371/journal.pone.0198463

    Antisense GT insertions upstream of LRP6 reduce LRP6 protein expression and impair WNT signaling. (A) The histogram indicates the number and orientation of GT insertions mapped to LRP6 and to the region ~12.5 kbp upstream of the TSS in unsorted cells and in the sorted cells from the WNT positive regulator low stringency screen. See legend to Fig 4A for details. The x-axis represents contiguous 250 bp bins to which insertions were mapped (Chromosome 12, 12116000–12279249 bp). (B) The histogram shows an expanded view of the 5’ end of LRP6 and the region ~12.5 kbp upstream of the TSS (left of the vertical dotted line), with traces for GT insertions mapped in unsorted cells and in the sorted cells from the WNT positive regulator low stringency screen. The x-axis represents contiguous 250 bp bins to which insertions were mapped (Chromosome 12, 12262500–12279249 bp). The green rectangle above the gene track indicates the location of the LRP6 promoter according to Ensembl and the black rectangle indicates the location of the bin identified in the upstream insertion enrichment analyses of the WNT positive regulator low stringency and high stringency screens. The black and orange stars denote the positions of the antisense GT insertions (located at NC_000012.13:g.12268371_12268372insGenetrap (Dec.2013: hg38, GRCh38) and NC_000012.13:g.12269383_12269384insGenetrap (Dec.2013: hg38, GRCh38) respectively [ 10 ]; see S2 File ) in the LRP6 GT -1(Up) and LRP6 GT -2(Up) clonal cell lines, respectively, and the blue star denotes the position of the sense GT insertion (located at NC_000012.13:g.12266072_12266073insGenetrap (Dec.2013: hg38, GRCh38); see S2 File ) in the LRP6 GT -3(Int) cell line. The inverted histogram below the RefSeq gene track for LRP6 indicates the maximum CAGE read count found in any tissue sample from the FANTOM5 database [ 11 ]. (C) Fold-induction in WNT reporter (median +/- SEM EGFP fluorescence from 20,000 cells) following treatment with 50% WNT3A CM. (D) Fold-induction in AXIN2 mRNA (average +/- SD of AXIN2 mRNA normalized to HPRT1 mRNA, each measured in triplicate qPCR reactions) following treatment with 50% WNT3A CM. (E) Quantification of immunoblot analysis of total LRP6 protein (average +/- SD LRP6 intensity normalized to ACTIN intensity from samples run in duplicate) shown as percentage of WT HAP1-7TGP. The blot used for quantification is shown in C in S3 Fig . (F) Cell surface LRP6 protein (median +/- SEM cell surface LRP6 immunofluorescence from 20,000 cells) shown as percentage of WT HAP1-7TGP. (G) LRP6 mRNA (average +/- SD of LRP6 mRNA, measured using two different primer pairs, normalized to HPRT1 mRNA, each measured in triplicate qPCR reactions) shown relative to WT HAP1-7TGP cells.
    Figure Legend Snippet: Antisense GT insertions upstream of LRP6 reduce LRP6 protein expression and impair WNT signaling. (A) The histogram indicates the number and orientation of GT insertions mapped to LRP6 and to the region ~12.5 kbp upstream of the TSS in unsorted cells and in the sorted cells from the WNT positive regulator low stringency screen. See legend to Fig 4A for details. The x-axis represents contiguous 250 bp bins to which insertions were mapped (Chromosome 12, 12116000–12279249 bp). (B) The histogram shows an expanded view of the 5’ end of LRP6 and the region ~12.5 kbp upstream of the TSS (left of the vertical dotted line), with traces for GT insertions mapped in unsorted cells and in the sorted cells from the WNT positive regulator low stringency screen. The x-axis represents contiguous 250 bp bins to which insertions were mapped (Chromosome 12, 12262500–12279249 bp). The green rectangle above the gene track indicates the location of the LRP6 promoter according to Ensembl and the black rectangle indicates the location of the bin identified in the upstream insertion enrichment analyses of the WNT positive regulator low stringency and high stringency screens. The black and orange stars denote the positions of the antisense GT insertions (located at NC_000012.13:g.12268371_12268372insGenetrap (Dec.2013: hg38, GRCh38) and NC_000012.13:g.12269383_12269384insGenetrap (Dec.2013: hg38, GRCh38) respectively [ 10 ]; see S2 File ) in the LRP6 GT -1(Up) and LRP6 GT -2(Up) clonal cell lines, respectively, and the blue star denotes the position of the sense GT insertion (located at NC_000012.13:g.12266072_12266073insGenetrap (Dec.2013: hg38, GRCh38); see S2 File ) in the LRP6 GT -3(Int) cell line. The inverted histogram below the RefSeq gene track for LRP6 indicates the maximum CAGE read count found in any tissue sample from the FANTOM5 database [ 11 ]. (C) Fold-induction in WNT reporter (median +/- SEM EGFP fluorescence from 20,000 cells) following treatment with 50% WNT3A CM. (D) Fold-induction in AXIN2 mRNA (average +/- SD of AXIN2 mRNA normalized to HPRT1 mRNA, each measured in triplicate qPCR reactions) following treatment with 50% WNT3A CM. (E) Quantification of immunoblot analysis of total LRP6 protein (average +/- SD LRP6 intensity normalized to ACTIN intensity from samples run in duplicate) shown as percentage of WT HAP1-7TGP. The blot used for quantification is shown in C in S3 Fig . (F) Cell surface LRP6 protein (median +/- SEM cell surface LRP6 immunofluorescence from 20,000 cells) shown as percentage of WT HAP1-7TGP. (G) LRP6 mRNA (average +/- SD of LRP6 mRNA, measured using two different primer pairs, normalized to HPRT1 mRNA, each measured in triplicate qPCR reactions) shown relative to WT HAP1-7TGP cells.

    Techniques Used: Expressing, Fluorescence, Real-time Polymerase Chain Reaction, Immunofluorescence

    2) Product Images from "Comparative genetic screens in human cells reveal new regulatory mechanisms in WNT signaling"

    Article Title: Comparative genetic screens in human cells reveal new regulatory mechanisms in WNT signaling

    Journal: eLife

    doi: 10.7554/eLife.21459

    AXIN1 and AXIN2 are redundant in haploid human cells ( A–B ), and CTNNB1 protein is stabilized normally in AXIN2 ∆C cells ( C ). ( A ) Immunoblots of total AXIN1, AXIN2 and GAPDH in various AXIN1 and/or AXIN2 deletion and/or truncation cell lines. GAPDH loading controls are shown below their respective blots. Single WT and AXIN1 KO ; AXIN2 KO clonal cell lines, and two independent clonal cell lines for all other genotypes were analyzed. Genotypes are indicated above the blots. Cells were treated with 10 μM CHIR-99021 to increase AXIN2 expression, since under unstimulated conditions AXIN2 levels were almost undetectable. Both AXIN1 and AXIN2 are expressed in HAP1-7TGP cells. Disruption of AXIN1 led to a marked increase in full-length and truncated AXIN2 protein abundance. ( B ) WNT reporter activity (median EGFP fluorescence from 10,000 cells), relative to untreated WT cells. Cells were treated with 50% WNT3A CM where indicated. Each circle represents a unique clonal cell line (see Supplementary file 2 ). Single WT and AXIN1 KO ; AXIN2 KO cell lines were analyzed. For AXIN2 KO and AXIN1 KO cells, the average of two independent clonal cell lines is indicated by a horizontal line. The top graph shows an expanded view of the y-axis to clearly show low levels of reporter activity for untreated cells. AXIN2 and AXIN1 are functionally redundant in HAP1-7TGP cells. ( C ) Representative immunoblots of soluble CTNNB1 and ACTIN used for quantification in Figure 3D . Two WT and two AXIN2 ∆C clonal cell lines were analyzed. Cells were treated with 50% WNT3A CM (‘W’) or 10 μM CHIR-99021 (‘C’) where indicated. CTNNB1 protein was stabilized normally in AXIN2 ∆C cells following both treatments. DOI: http://dx.doi.org/10.7554/eLife.21459.008
    Figure Legend Snippet: AXIN1 and AXIN2 are redundant in haploid human cells ( A–B ), and CTNNB1 protein is stabilized normally in AXIN2 ∆C cells ( C ). ( A ) Immunoblots of total AXIN1, AXIN2 and GAPDH in various AXIN1 and/or AXIN2 deletion and/or truncation cell lines. GAPDH loading controls are shown below their respective blots. Single WT and AXIN1 KO ; AXIN2 KO clonal cell lines, and two independent clonal cell lines for all other genotypes were analyzed. Genotypes are indicated above the blots. Cells were treated with 10 μM CHIR-99021 to increase AXIN2 expression, since under unstimulated conditions AXIN2 levels were almost undetectable. Both AXIN1 and AXIN2 are expressed in HAP1-7TGP cells. Disruption of AXIN1 led to a marked increase in full-length and truncated AXIN2 protein abundance. ( B ) WNT reporter activity (median EGFP fluorescence from 10,000 cells), relative to untreated WT cells. Cells were treated with 50% WNT3A CM where indicated. Each circle represents a unique clonal cell line (see Supplementary file 2 ). Single WT and AXIN1 KO ; AXIN2 KO cell lines were analyzed. For AXIN2 KO and AXIN1 KO cells, the average of two independent clonal cell lines is indicated by a horizontal line. The top graph shows an expanded view of the y-axis to clearly show low levels of reporter activity for untreated cells. AXIN2 and AXIN1 are functionally redundant in HAP1-7TGP cells. ( C ) Representative immunoblots of soluble CTNNB1 and ACTIN used for quantification in Figure 3D . Two WT and two AXIN2 ∆C clonal cell lines were analyzed. Cells were treated with 50% WNT3A CM (‘W’) or 10 μM CHIR-99021 (‘C’) where indicated. CTNNB1 protein was stabilized normally in AXIN2 ∆C cells following both treatments. DOI: http://dx.doi.org/10.7554/eLife.21459.008

    Techniques Used: Western Blot, Expressing, Activity Assay, Fluorescence

    3) Product Images from "HDAC1 and HDAC2 independently regulate common and specific intrinsic responses in murine enteroids"

    Article Title: HDAC1 and HDAC2 independently regulate common and specific intrinsic responses in murine enteroids

    Journal: Scientific Reports

    doi: 10.1038/s41598-019-41842-6

    Hdac1 or Hdac2 depletion alters the expression of specific metabolic and inflammatory related genes. Total protein extracts from control, Hdac1 - or Hdac2 -deficient enteroids were separated on SDS-PAGE gels for Western blot analysis, and selected proteins were revealed with specific antibodies against phosphorylated and total STAT3 ( A ), against HMGCS2 ( C ), and against β-ACTIN as a loading control ( A , C ) (n = 3). Densitometric analysis of Phospho-STAT3 compared to STAT3 is indicated (**p ≤ 0.01; ****p ≤ 0.001). Cropped images for Phospho-STAT3, STAT3 and β-ACTIN are from immunoblotting experiments on the same membrane. Cropped images for HMGCS2 and β-ACTIN are from immunoblotting experiments on another membrane. Samples for ( A , C ) derive from the same experiments. Full-length blots are presented in Supplementary Fig. S8 . ( A ). Total RNAs were isolated from 5-day cultured control, Hdac1 - or Hdac2 -deficient enteroids. Expression levels of Hmgcs2 and Creb3l1 ( B ), Nox1 and Xdh ( D ), St3gal4 , Bcl2l15 and Il18 ( E ) were determined by qPCR, with Pbgd as a control (n = 4–7). Results represent the mean ± SEM (*p ≤ 0.05; **p ≤ 0.01; ***p ≤ 0.005; ****p ≤ 0.001).
    Figure Legend Snippet: Hdac1 or Hdac2 depletion alters the expression of specific metabolic and inflammatory related genes. Total protein extracts from control, Hdac1 - or Hdac2 -deficient enteroids were separated on SDS-PAGE gels for Western blot analysis, and selected proteins were revealed with specific antibodies against phosphorylated and total STAT3 ( A ), against HMGCS2 ( C ), and against β-ACTIN as a loading control ( A , C ) (n = 3). Densitometric analysis of Phospho-STAT3 compared to STAT3 is indicated (**p ≤ 0.01; ****p ≤ 0.001). Cropped images for Phospho-STAT3, STAT3 and β-ACTIN are from immunoblotting experiments on the same membrane. Cropped images for HMGCS2 and β-ACTIN are from immunoblotting experiments on another membrane. Samples for ( A , C ) derive from the same experiments. Full-length blots are presented in Supplementary Fig. S8 . ( A ). Total RNAs were isolated from 5-day cultured control, Hdac1 - or Hdac2 -deficient enteroids. Expression levels of Hmgcs2 and Creb3l1 ( B ), Nox1 and Xdh ( D ), St3gal4 , Bcl2l15 and Il18 ( E ) were determined by qPCR, with Pbgd as a control (n = 4–7). Results represent the mean ± SEM (*p ≤ 0.05; **p ≤ 0.01; ***p ≤ 0.005; ****p ≤ 0.001).

    Techniques Used: Expressing, SDS Page, Western Blot, Isolation, Cell Culture, Real-time Polymerase Chain Reaction

    Hdac1 or Hdac2 depletion reduces enteroid histone deacetylase activity. ( A ) Total RNA was isolated from 5-day cultured control, Hdac1 - and Hdac2 -deficient enteroids. Hdac1 and Hdac2 mRNA levels were determined by semi-quantitative RT-PCR, with Gapdh as a loading control. ( B ) Total protein extracts from control, Hdac1 - and Hdac2 -deficient enteroids were separated on SDS-PAGE gels for Western blot analysis, and selected proteins were revealed with specific antibodies against HDAC1 and HDAC2, and against β-ACTIN as a loading control. Cropped images for HDAC1 and β-ACTIN are from immunoblotting experiments on the same membrane. Cropped images for HDAC2 and β-ACTIN are from immunoblotting experiments on another membrane. Full-length blots are presented in Supplementary Fig. S8 (n = 3). ( C ) 7.5 µg of nuclear proteins from control, Hdac1 - and Hdac2 -deficient enteroids were used to measure deacetylase activity with a colorimetric HDAC assay kit. Treatment with Trichostatin A, a pan-inhibitor of HDAC activity, was used as a control (n = 3; 2 or 3 wells for each). Results represent the mean ± SD (*p ≤ 0.05; ****p ≤ 0.0001).
    Figure Legend Snippet: Hdac1 or Hdac2 depletion reduces enteroid histone deacetylase activity. ( A ) Total RNA was isolated from 5-day cultured control, Hdac1 - and Hdac2 -deficient enteroids. Hdac1 and Hdac2 mRNA levels were determined by semi-quantitative RT-PCR, with Gapdh as a loading control. ( B ) Total protein extracts from control, Hdac1 - and Hdac2 -deficient enteroids were separated on SDS-PAGE gels for Western blot analysis, and selected proteins were revealed with specific antibodies against HDAC1 and HDAC2, and against β-ACTIN as a loading control. Cropped images for HDAC1 and β-ACTIN are from immunoblotting experiments on the same membrane. Cropped images for HDAC2 and β-ACTIN are from immunoblotting experiments on another membrane. Full-length blots are presented in Supplementary Fig. S8 (n = 3). ( C ) 7.5 µg of nuclear proteins from control, Hdac1 - and Hdac2 -deficient enteroids were used to measure deacetylase activity with a colorimetric HDAC assay kit. Treatment with Trichostatin A, a pan-inhibitor of HDAC activity, was used as a control (n = 3; 2 or 3 wells for each). Results represent the mean ± SD (*p ≤ 0.05; ****p ≤ 0.0001).

    Techniques Used: Histone Deacetylase Assay, Activity Assay, Isolation, Cell Culture, Quantitative RT-PCR, SDS Page, Western Blot

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    Incubation:

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    Article Snippet: .. Membranes were blocked with 5% nonfat skim milk in PBS-Tween and were incubated with either, 1/1000 mouse NOS-I (BD Transduction), 1/1000 mouse NOS-III (BD Transduction) 1/50,000 mouse β-ACTIN (Sigma), 1/50,000 mouse α-ACTIN (Sigma), 1/1000 rabbit GAPDH (Cell Signaling) antibodies, overnight at 4°C. .. Membranes were incubated with 1/2000 or 1/80,000 chicken anti-mouse (Santa Cruz) or 1/2000 chicken anti-rabbit (Santa Cruz) secondary antibody for 1.5 hours.

    other:

    Article Title: West Nile virus capsid protein induces p53‐mediated apoptosis via the sequestration of HDM2 to the nucleolus
    Article Snippet: The monoclonal anti‐FLAG (M2) and anti‐actin mouse antibodies, and PI were obtained from Sigma.

    Article Title: Focal Adhesion Remodeling Is Crucial for Glucose-Stimulated Insulin Secretion and Involves Activation of Focal Adhesion Kinase and Paxillin
    Article Snippet: Primary antibodies (Abs) were as follows: rabbit anti-FAK polyclonal (p)Ab (Santa Cruz Biotechnology, Santa Cruz, CA), rabbit anti–phospho-(Y397)FAK pAb and rabbit anti–phospho-(Y118)paxillin pAb (Invitrogen), mouse anti-paxillin monoclonal (m)Ab (BD Transduction Laboratories, San Jose, CA), rabbit anti-ERK1/2 pAb and rabbit anti–phospho-(T202/Y204)ERK1/2 pAb (Cell Signaling Technology, Beverly, MA), mouse antiactin mAb (Millipore, Temecula, CA).

    Western Blot:

    Article Title: The F-BAR protein pacsin2 inhibits asymmetric VE-cadherin internalization from tensile adherens junctions
    Article Snippet: .. Antibodies and reagents Mouse monoclonal anti-actin (clone AC-40, Cat # A3853, diluted 1/3,000 for western) anti-vinculin antibody hVIN-1 (Cat # V9131, diluted 1/100 for immunofluorescence (IF)), rabbit anti-α-catenin serum (Cat # C2081, diluted 1/400 for IF) and anti-β-catenin serum (Cat # C2206, diluted 1/400 for IF) were obtained from Sigma-Aldrich. .. Mouse monoclonal anti-p120-catenin antibody (clone 98/pp120, Cat # 610133, diluted 1/100 for IF), anti-β-catenin (clone 14, Cat # 610154, diluted 1/100 for IF), anti-N-cadherin (clone 32, Cat # 610920, diluted 1/100 for IF) and anti-Rho GDI (Cat # 610255, diluted 1/5,000 for western) were from BD Bioscience.

    Article Title: Genome-wide RNAi Screen Reveals a New Role of a WNT/CTNNB1 Signaling Pathway as Negative Regulator of Virus-induced Innate Immune Responses
    Article Snippet: .. Western blot analysis was performed using mouse anti-WNT2B (Santa Cruz), anti-ACTIN (Chemicon International), anti-CTNNB1 active (Millipore), anti-FLAG (Sigma), anti-IRF3 (Santa Cruz), anti-NS3 (HCV, Abcam), anti-p65 (Santa Cruz) and rabbit anti-CTNNB1 total (Epitomics), anti-CTNNB1-P-Ser552 (Cell Signaling), anti-IFIT2 (Novus Biologicals), anti-IFIT1 (Novus Biologicals), anti-SeV (HN) , anti-WNT9B (Aviva systems biology) and anti-NFKBIA-P-Ser32 (Cell Signaling). .. HRP-conjugated secondary antibodies were from Bio-Rad.

    Staining:

    Article Title: NFAT is required for spontaneous pulmonary hypertension in superoxide dismutase 1 knockout mice
    Article Snippet: .. Lung cryostat sections (10 μm) were stained with primary rabbit polyclonal anti-NFATc3 or NFATc2 (Santa Cruz Biotechnology, Santa Cruz, CA) and mouse anti-α-actin (Sigma) followed by donkey anti-rabbit Cy5 and anti-mouse Cy3 (Jackson ImmunoResearch Laboratories, Bar Harbor, ME) as previously described ( , , , ). .. Nuclei were stained using SYTOX green (Life Technologies). α-Actin staining was used to detect NFAT nuclear accumulation in PASMC.

    Binding Assay:

    Article Title: Manganese Binds to Clostridium difficile Fbp68 and Is Essential for Fibronectin Binding *
    Article Snippet: .. 120-kDa cell binding domain (CBD) or 40-kDa domain of Fn, mouse anti-fibronectin, and mouse anti-α-actin were purchased from Chemicon International (Temecula, CA). ..

    Immunofluorescence:

    Article Title: The F-BAR protein pacsin2 inhibits asymmetric VE-cadherin internalization from tensile adherens junctions
    Article Snippet: .. Antibodies and reagents Mouse monoclonal anti-actin (clone AC-40, Cat # A3853, diluted 1/3,000 for western) anti-vinculin antibody hVIN-1 (Cat # V9131, diluted 1/100 for immunofluorescence (IF)), rabbit anti-α-catenin serum (Cat # C2081, diluted 1/400 for IF) and anti-β-catenin serum (Cat # C2206, diluted 1/400 for IF) were obtained from Sigma-Aldrich. .. Mouse monoclonal anti-p120-catenin antibody (clone 98/pp120, Cat # 610133, diluted 1/100 for IF), anti-β-catenin (clone 14, Cat # 610154, diluted 1/100 for IF), anti-N-cadherin (clone 32, Cat # 610920, diluted 1/100 for IF) and anti-Rho GDI (Cat # 610255, diluted 1/5,000 for western) were from BD Bioscience.

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    Millipore antibody against dbh
    Anti-dopamine-β-hydroxylase <t>(DBH)-conjugated</t> saporin (DSAP) produces glucocorticoid resistance in the paraventricular nucleus of the hypothalamus (PVH) of high-fat/high-sucrose choice (HFSC)-fed animals. A–G : combined adrenal weights ( A ), thymus weights ( B ), and corticotropin-releasing hormone (CRH) immunoreactivity (ir) in the PVH ( C and D–G ) in mouse IgG-saporin conjugate <t>(MSAP)</t> and DSAP animals given chow or a HFSC diet for 56 days. MGL, mean gray level. H–K : DBH immunoreactivity in the same sections stained for CRH immunoreactivity ( D–G ) in MSAP ( H and J ) and DSAP ( E and G ) animals. Scale bars = 150 μm. dp, PVH dorsal parvicellular part; mpd, PVH dorsal zone of the medial parvicellular part; mpv, PVH ventral zone of the medial parvicellular part; pm, PVH posterior magnocellular part; pv, PVH periventricular part; V3, 3rd ventricle. Values are means ± SE; n = 5 MSAP-chow and DSAP-HFSC and n = 8 DSAP-chow and MSAP-HFSC. ns, Not significant.
    Antibody Against Dbh, supplied by Millipore, used in various techniques. Bioz Stars score: 93/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/antibody against dbh/product/Millipore
    Average 93 stars, based on 1 article reviews
    Price from $9.99 to $1999.99
    antibody against dbh - by Bioz Stars, 2020-09
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    99
    Millipore mouse anti human β actin monoclonal antibody
    Effect of MSK1-mediated p65 Ser276 phosphorylation in IL-1β-induced SCF expression. A. Human lung fibroblasts in culture were transiently co-transfected with the pGL3e/SCF firefly luciferase construct and a Renilla luciferase construct (pRL-TK) as an internal control. Cells were pre-incubated for 1 h with a combination of SB202190 (SB; 3.5 µM) and PD98059 (PD; 20 µM) or with H89 (10 µM) and treated with IL-1β (20 U/ml). After 150 min, cells were harvested for luciferase activity measurement. The results are expressed as the level of pGL3e/SCF constructions' promoter-driven firefly luciferase expression after correcting for the transfection efficiency by pRL-TK luciferase measurements and represented as a percentage of control values. B. Fibroblasts were transfected with control and anti-MSK1 siRNA (100 nM), or transfection medium alone (control). After 48 hours, inhibition of MSK1 with siRNA was controlled by Western blotting in the cell lysate, using anti-MSK1, with <t>anti-β-actin</t> antibodies as a deposit control. Cells were treated with IL-1β (20 U/ml). SCF protein levels were assessed in the supernatant 5 hours after treatment by ELISA. C . Fibroblasts were transfected with WT or “kinase-dead” (KD) MSK1 plasmid (1 µg), WT or S276C p65 plasmids or transfection medium alone (control), and treated with IL-1β (20 U/ml). SCF protein levels were assessed by ELISA in the supernatant obtained 5 hours after treatment. Results are expressed as percentages of control values of three independent experiments performed in fibroblasts from three different donors.
    Mouse Anti Human β Actin Monoclonal Antibody, supplied by Millipore, used in various techniques. Bioz Stars score: 99/100, based on 17 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/mouse anti human β actin monoclonal antibody/product/Millipore
    Average 99 stars, based on 17 article reviews
    Price from $9.99 to $1999.99
    mouse anti human β actin monoclonal antibody - by Bioz Stars, 2020-09
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    99
    Millipore affinity purified mouse anti actin
    Synphilin-1 protein levels are increased in C3H mice. Cerebral cortical tissues were harvested from BL6 and C3H mice. Protein lysates were extracted from animals at ages 10 weeks ( A and B ) and 8 months ( C and D ). Equal amounts (18 ug) of high-salt protein extracts were loaded onto 10% polyacrylamide gels and analyzed by western blot analysis with the <t>affinity</t> <t>purified</t> polyclonal antibody, UPN79 to assess synphilin-1, as well as an <t>actin</t> antibody to confirm equal protein loading. Four samples were loaded, ea ch from separate mice of the indicated strains. The graphs in B and D show the average ratios of the levels of UPN79 to actin normalized to the values in BL6 animals at the respective aforementioned ages. E ) Total RNA was extracted from cerebral cortical tissues that were harvested from the same BL6 and C3H mice analyzed in C . Synphilin-1 and actin mRNA transcripts were quantified using two-step qRT-PCR. Experiments were performed in duplicate and 3 separate samples were analyzed for each <t>mouse</t> strain. The synphilin-1 and actin qRT-PCR products are shown. The image shows the products from one of the mice analyzed for the indicated strains. F ) The ratio of the synphilin-1 to actin C T value was calculated for each sample. The graph depicts the average of the ratios between replicate samples for each mouse strain. The error bars indicate standard deviation (n=6).
    Affinity Purified Mouse Anti Actin, supplied by Millipore, used in various techniques. Bioz Stars score: 99/100, based on 3 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/affinity purified mouse anti actin/product/Millipore
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    Price from $9.99 to $1999.99
    affinity purified mouse anti actin - by Bioz Stars, 2020-09
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    Image Search Results


    Anti-dopamine-β-hydroxylase (DBH)-conjugated saporin (DSAP) produces glucocorticoid resistance in the paraventricular nucleus of the hypothalamus (PVH) of high-fat/high-sucrose choice (HFSC)-fed animals. A–G : combined adrenal weights ( A ), thymus weights ( B ), and corticotropin-releasing hormone (CRH) immunoreactivity (ir) in the PVH ( C and D–G ) in mouse IgG-saporin conjugate (MSAP) and DSAP animals given chow or a HFSC diet for 56 days. MGL, mean gray level. H–K : DBH immunoreactivity in the same sections stained for CRH immunoreactivity ( D–G ) in MSAP ( H and J ) and DSAP ( E and G ) animals. Scale bars = 150 μm. dp, PVH dorsal parvicellular part; mpd, PVH dorsal zone of the medial parvicellular part; mpv, PVH ventral zone of the medial parvicellular part; pm, PVH posterior magnocellular part; pv, PVH periventricular part; V3, 3rd ventricle. Values are means ± SE; n = 5 MSAP-chow and DSAP-HFSC and n = 8 DSAP-chow and MSAP-HFSC. ns, Not significant.

    Journal: American Journal of Physiology - Regulatory, Integrative and Comparative Physiology

    Article Title: Obesity, Diabetes and Energy Homeostasis: Catecholaminergic projections into an interconnected forebrain network control the sensitivity of male rats to diet-induced obesity

    doi: 10.1152/ajpregu.00423.2017

    Figure Lengend Snippet: Anti-dopamine-β-hydroxylase (DBH)-conjugated saporin (DSAP) produces glucocorticoid resistance in the paraventricular nucleus of the hypothalamus (PVH) of high-fat/high-sucrose choice (HFSC)-fed animals. A–G : combined adrenal weights ( A ), thymus weights ( B ), and corticotropin-releasing hormone (CRH) immunoreactivity (ir) in the PVH ( C and D–G ) in mouse IgG-saporin conjugate (MSAP) and DSAP animals given chow or a HFSC diet for 56 days. MGL, mean gray level. H–K : DBH immunoreactivity in the same sections stained for CRH immunoreactivity ( D–G ) in MSAP ( H and J ) and DSAP ( E and G ) animals. Scale bars = 150 μm. dp, PVH dorsal parvicellular part; mpd, PVH dorsal zone of the medial parvicellular part; mpv, PVH ventral zone of the medial parvicellular part; pm, PVH posterior magnocellular part; pv, PVH periventricular part; V3, 3rd ventricle. Values are means ± SE; n = 5 MSAP-chow and DSAP-HFSC and n = 8 DSAP-chow and MSAP-HFSC. ns, Not significant.

    Article Snippet: Sections containing the hypothalamus and hindbrains of all MSAP- and DSAP-injected animals were stained using an antibody against DBH (1:10,000 dilution, mouse anti-DBH; catalog no. MAB308, Millipore, Temecula, CA).

    Techniques: Staining

    Effect of MSK1-mediated p65 Ser276 phosphorylation in IL-1β-induced SCF expression. A. Human lung fibroblasts in culture were transiently co-transfected with the pGL3e/SCF firefly luciferase construct and a Renilla luciferase construct (pRL-TK) as an internal control. Cells were pre-incubated for 1 h with a combination of SB202190 (SB; 3.5 µM) and PD98059 (PD; 20 µM) or with H89 (10 µM) and treated with IL-1β (20 U/ml). After 150 min, cells were harvested for luciferase activity measurement. The results are expressed as the level of pGL3e/SCF constructions' promoter-driven firefly luciferase expression after correcting for the transfection efficiency by pRL-TK luciferase measurements and represented as a percentage of control values. B. Fibroblasts were transfected with control and anti-MSK1 siRNA (100 nM), or transfection medium alone (control). After 48 hours, inhibition of MSK1 with siRNA was controlled by Western blotting in the cell lysate, using anti-MSK1, with anti-β-actin antibodies as a deposit control. Cells were treated with IL-1β (20 U/ml). SCF protein levels were assessed in the supernatant 5 hours after treatment by ELISA. C . Fibroblasts were transfected with WT or “kinase-dead” (KD) MSK1 plasmid (1 µg), WT or S276C p65 plasmids or transfection medium alone (control), and treated with IL-1β (20 U/ml). SCF protein levels were assessed by ELISA in the supernatant obtained 5 hours after treatment. Results are expressed as percentages of control values of three independent experiments performed in fibroblasts from three different donors.

    Journal: PLoS ONE

    Article Title: Ser276 Phosphorylation of NF-kB p65 by MSK1 Controls SCF Expression in Inflammation

    doi: 10.1371/journal.pone.0004393

    Figure Lengend Snippet: Effect of MSK1-mediated p65 Ser276 phosphorylation in IL-1β-induced SCF expression. A. Human lung fibroblasts in culture were transiently co-transfected with the pGL3e/SCF firefly luciferase construct and a Renilla luciferase construct (pRL-TK) as an internal control. Cells were pre-incubated for 1 h with a combination of SB202190 (SB; 3.5 µM) and PD98059 (PD; 20 µM) or with H89 (10 µM) and treated with IL-1β (20 U/ml). After 150 min, cells were harvested for luciferase activity measurement. The results are expressed as the level of pGL3e/SCF constructions' promoter-driven firefly luciferase expression after correcting for the transfection efficiency by pRL-TK luciferase measurements and represented as a percentage of control values. B. Fibroblasts were transfected with control and anti-MSK1 siRNA (100 nM), or transfection medium alone (control). After 48 hours, inhibition of MSK1 with siRNA was controlled by Western blotting in the cell lysate, using anti-MSK1, with anti-β-actin antibodies as a deposit control. Cells were treated with IL-1β (20 U/ml). SCF protein levels were assessed in the supernatant 5 hours after treatment by ELISA. C . Fibroblasts were transfected with WT or “kinase-dead” (KD) MSK1 plasmid (1 µg), WT or S276C p65 plasmids or transfection medium alone (control), and treated with IL-1β (20 U/ml). SCF protein levels were assessed by ELISA in the supernatant obtained 5 hours after treatment. Results are expressed as percentages of control values of three independent experiments performed in fibroblasts from three different donors.

    Article Snippet: Immunoblotting used the following antibodies: rabbit anti-human IκB-α polyclonal antibody (1/1000, Calbiochem, La Jolla, CA), mouse anti-human phospho- IκB-α monoclonal antibody, (1/1000, Ab-1, Oncogene Research Product, Boston, MA), rabbit anti-human phospho-Ser276 p65 antibody (1/1000, 3037, Cell Signaling Technology, Danvers MA), rabbit anti-human phospho-Ser536 p65 antibody (1/1000, 3031, Cell Signaling Technology), rabbit anti-human p65 polyclonal antibody (1/200, sc-109, Santa Cruz Biotechnology, Santa Cruz, CA), rabbit anti-human CBP polyclonal antibody (1/200, sc-369, Santa Cruz Biotechnology), mouse anti-human β-actin monoclonal antibody (1/5000, Ab-1, Oncogene Research Product), goat anti-human MSK1 (1/200, sc-9392, Santa Cruz Biotechnology.

    Techniques: Expressing, Transfection, Luciferase, Construct, Incubation, Activity Assay, Inhibition, Western Blot, Enzyme-linked Immunosorbent Assay, Plasmid Preparation

    Synphilin-1 protein levels are increased in C3H mice. Cerebral cortical tissues were harvested from BL6 and C3H mice. Protein lysates were extracted from animals at ages 10 weeks ( A and B ) and 8 months ( C and D ). Equal amounts (18 ug) of high-salt protein extracts were loaded onto 10% polyacrylamide gels and analyzed by western blot analysis with the affinity purified polyclonal antibody, UPN79 to assess synphilin-1, as well as an actin antibody to confirm equal protein loading. Four samples were loaded, ea ch from separate mice of the indicated strains. The graphs in B and D show the average ratios of the levels of UPN79 to actin normalized to the values in BL6 animals at the respective aforementioned ages. E ) Total RNA was extracted from cerebral cortical tissues that were harvested from the same BL6 and C3H mice analyzed in C . Synphilin-1 and actin mRNA transcripts were quantified using two-step qRT-PCR. Experiments were performed in duplicate and 3 separate samples were analyzed for each mouse strain. The synphilin-1 and actin qRT-PCR products are shown. The image shows the products from one of the mice analyzed for the indicated strains. F ) The ratio of the synphilin-1 to actin C T value was calculated for each sample. The graph depicts the average of the ratios between replicate samples for each mouse strain. The error bars indicate standard deviation (n=6).

    Journal: Journal of neurochemistry

    Article Title: IDENTIFICATION AND CHARACTERIZATION OF A NOVEL ENDOGENOUS MURINE PARKIN MUTATION

    doi: 10.1111/j.1471-4159.2010.06605.x

    Figure Lengend Snippet: Synphilin-1 protein levels are increased in C3H mice. Cerebral cortical tissues were harvested from BL6 and C3H mice. Protein lysates were extracted from animals at ages 10 weeks ( A and B ) and 8 months ( C and D ). Equal amounts (18 ug) of high-salt protein extracts were loaded onto 10% polyacrylamide gels and analyzed by western blot analysis with the affinity purified polyclonal antibody, UPN79 to assess synphilin-1, as well as an actin antibody to confirm equal protein loading. Four samples were loaded, ea ch from separate mice of the indicated strains. The graphs in B and D show the average ratios of the levels of UPN79 to actin normalized to the values in BL6 animals at the respective aforementioned ages. E ) Total RNA was extracted from cerebral cortical tissues that were harvested from the same BL6 and C3H mice analyzed in C . Synphilin-1 and actin mRNA transcripts were quantified using two-step qRT-PCR. Experiments were performed in duplicate and 3 separate samples were analyzed for each mouse strain. The synphilin-1 and actin qRT-PCR products are shown. The image shows the products from one of the mice analyzed for the indicated strains. F ) The ratio of the synphilin-1 to actin C T value was calculated for each sample. The graph depicts the average of the ratios between replicate samples for each mouse strain. The error bars indicate standard deviation (n=6).

    Article Snippet: Affinity purified mouse anti-actin (clone C4) monoclonal antibody reacts with all forms of vertebrate actin (Millipore, Billerica, MA).

    Techniques: Mouse Assay, Western Blot, Affinity Purification, Quantitative RT-PCR, Standard Deviation