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  • 95
    Thermo Fisher human single
    Human Single, supplied by Thermo Fisher, used in various techniques. Bioz Stars score: 95/100, based on 160 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    95
    Millipore human rad51
    Impact of recombinase <t>(RAD51)</t> suppression in FLO-1 cells. FLO-1 cells were transduced with control (CS) or RAD51-specific (RS4) shRNAs and selected in puromycin. A: (I) RS4 lentiviruses mediate a strong suppression of RAD51. The expression profile of
    Human Rad51, supplied by Millipore, used in various techniques. Bioz Stars score: 95/100, based on 18 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    94
    Millipore human hdac6
    Selective <t>HDAC6</t> inhibitors down‐regulate PD‐L1 expression in vitro. (A) WM164, WM983A and WM793 human melanoma cell lines were incubated with the HDAC6 inhibitor Tubastatin A (3 μM) for 24 h, followed for
    Human Hdac6, supplied by Millipore, used in various techniques. Bioz Stars score: 94/100, based on 20 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    93
    Millipore human pten
    Selective <t>HDAC6</t> inhibitors down‐regulate PD‐L1 expression in vitro. (A) WM164, WM983A and WM793 human melanoma cell lines were incubated with the HDAC6 inhibitor Tubastatin A (3 μM) for 24 h, followed for
    Human Pten, supplied by Millipore, used in various techniques. Bioz Stars score: 93/100, based on 20 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    94
    Millipore human mecp2
    <t>Mecp2</t> and sexual differentiation of juvenile play behavior
    Human Mecp2, supplied by Millipore, used in various techniques. Bioz Stars score: 94/100, based on 35 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    93
    Millipore human nanog
    <t>Mecp2</t> and sexual differentiation of juvenile play behavior
    Human Nanog, supplied by Millipore, used in various techniques. Bioz Stars score: 93/100, based on 8 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    85
    Millipore human nov
    <t>Mecp2</t> and sexual differentiation of juvenile play behavior
    Human Nov, supplied by Millipore, used in various techniques. Bioz Stars score: 85/100, based on 2 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    94
    Millipore human parg
    <t>Mecp2</t> and sexual differentiation of juvenile play behavior
    Human Parg, supplied by Millipore, used in various techniques. Bioz Stars score: 94/100, based on 6 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    91
    Millipore human pedf
    Effect of E2 on <t>VEGF</t> and <t>PEDF</t> level in Cell Media. RhREC were grown for 24 h in a medium containing 0.0, 0.1, 1.0, or 10.0 nM E2. ELISA was performed and the cell medium was used to quantify VEGF (A) and PEDF (B) in the cell medium. (A)
    Human Pedf, supplied by Millipore, used in various techniques. Bioz Stars score: 91/100, based on 22 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    94
    Millipore human scf
    MC protease expression identified by immunostaining over time. MCs were recovered after 2 d of culture in liquid suspension culture with <t>SCF</t> alone, in direct coculture with HAECs, in <t>HAEC</t> coculture separated by a transwell membrane, with HAEC-conditioned
    Human Scf, supplied by Millipore, used in various techniques. Bioz Stars score: 94/100, based on 89 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    93
    Millipore human src
    αBTX-induced AChR endocytosis is mediated by <t>Src</t> phosphorylation. (A) CHO-K1/A5 cells were cotransfected with dominant-negative Src <t>K297R</t> and GFP, and the internalization of AChR induced by αBTX was assessed in cells positive for Src K297R. Note the absence of punctate structures in cells transfected with dominant-negative Src K297R. (B) CHO-K1/A5 cells were labeled with b-αBTX in the presence or absence of 10 μM PP2 and chased for 6 h. Surface AChR levels were determined by measuring the accessibility of b-αBTX to SA-PE. The histogram shows the quantification of surface-accessible AChR in the presence or absence (αBTX alone) of PP2. Each bar represents the weighted mean of internal AChR as estimated using flow cytometry data from 10,000 cells (see Materials and methods) normalized to cells labeled with b-αBTX on ice. Error bars represent SEM. *, P
    Human Src, supplied by Millipore, used in various techniques. Bioz Stars score: 93/100, based on 30 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    93
    Millipore human upa
    IgG binding from human leptospirosis immune serum to L. interrogans . Bacteria were coated onto microtiter plates (25 × 10 6 leptospires/well) and IgG was bound by incubating bacteria 50% nonimmune human sera (NHS) or confirmed paired leptospirosis patients sera: MAT negative (MAT−) or MAT positive (MAT+). Bacteria were treated with <t>PBS,</t> 40 μ g/mL PLG (PLG), 5 μ g/mL <t>uPA</t> (uPA), or PLG + uPA (Pla). Presence of human IgG deposited on leptospires was determined by ELISA using Fc-specific anti-human IgG antibodies. Bars represent the mean absorbance values at 492 nm ± the standard deviation of three replicates for each experimental group and are representative of two independent experiments.
    Human Upa, supplied by Millipore, used in various techniques. Bioz Stars score: 93/100, based on 234 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    93
    Millipore mif human
    IgG binding from human leptospirosis immune serum to L. interrogans . Bacteria were coated onto microtiter plates (25 × 10 6 leptospires/well) and IgG was bound by incubating bacteria 50% nonimmune human sera (NHS) or confirmed paired leptospirosis patients sera: MAT negative (MAT−) or MAT positive (MAT+). Bacteria were treated with <t>PBS,</t> 40 μ g/mL PLG (PLG), 5 μ g/mL <t>uPA</t> (uPA), or PLG + uPA (Pla). Presence of human IgG deposited on leptospires was determined by ELISA using Fc-specific anti-human IgG antibodies. Bars represent the mean absorbance values at 492 nm ± the standard deviation of three replicates for each experimental group and are representative of two independent experiments.
    Mif Human, supplied by Millipore, used in various techniques. Bioz Stars score: 93/100, based on 3 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    94
    Millipore human akr1c3
    Western immunoblot of <t>AKR1C3</t> (17β-HSD5) protein in a feminizing estrogen-secreting adrenal carcinoma, an aldosterone-producing adrenal adenoma, and H295 cells after treatment (24 hours) with either VIP (100 nM) or forskolin (10 μM). Lane 1: Aldosterone-producing adrenal adenoma (25 μg protein); lane 2: Estrogen-secreting adrenal carcinoma (25 μg protein); lane 3: Untreated control H295 cells (25 μg protein); lane 4: Forskolin (Fsk)-treated H295 cells (25 μg protein); lane 5: VIP-treated H295 cells (25 μg protein).
    Human Akr1c3, supplied by Millipore, used in various techniques. Bioz Stars score: 94/100, based on 17 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    93
    Millipore human apoe3
    Role of Calpain in ApoE-Induced ABCA1 Protein ( A ) Macrophages were treated with 100 μg/ml cycloheximide (CHX) or vehicle medium in the presence or absence of 4 μM Akt inhibitor X (Akt X) for 2 h, followed by 2 h incubation with 10 μg/ml <t>apoE3</t> or medium alone. ( B ) Macrophages were treated with vehicle medium (Veh), 50 μM ALLN, 1 mM leupeptin (Lpeptn), 10 μM aprotinin (Aprotn), 20μM pepstatin (Peptn), or 5 μM lactacystin (Lactyn) for 2 h. ( C ) Macrophages were treated with 50 μM ALLN or vehicle medium in the presence or absence of 4 μM Akt inhibitor X (Akt X) for 2 h, followed by 2 h incubation with 10 μg/ml apoE3 or control medium. ( D ) Macrophages were treated with or without 4 μM Akt inhibitor X (Akt X) for 2 h, followed by 2 h treatment with 10 μg/ml apoE3 or control medium alone. The cells were then treated with 3 μg/ml of calpain-1 or vehicle medium. ABCA1 (A1) protein was detected by immunoblotting, and quantified relative to GAPDH ( A–C ) or CD-MPR ( D ). ( E ) Macrophages were treated with 4 μM Akt X or vehicle medium for 2 h, followed by 2 h treatment with 10 μg/ml apoE3 or control medium. Calpain activity was measured with a calpain activity kit. Data represent mean ± SE of 3–4 independent experiments. ( A ) * P
    Human Apoe3, supplied by Millipore, used in various techniques. Bioz Stars score: 93/100, based on 13 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    94
    TaKaRa human blood
    Role of Calpain in ApoE-Induced ABCA1 Protein ( A ) Macrophages were treated with 100 μg/ml cycloheximide (CHX) or vehicle medium in the presence or absence of 4 μM Akt inhibitor X (Akt X) for 2 h, followed by 2 h incubation with 10 μg/ml <t>apoE3</t> or medium alone. ( B ) Macrophages were treated with vehicle medium (Veh), 50 μM ALLN, 1 mM leupeptin (Lpeptn), 10 μM aprotinin (Aprotn), 20μM pepstatin (Peptn), or 5 μM lactacystin (Lactyn) for 2 h. ( C ) Macrophages were treated with 50 μM ALLN or vehicle medium in the presence or absence of 4 μM Akt inhibitor X (Akt X) for 2 h, followed by 2 h incubation with 10 μg/ml apoE3 or control medium. ( D ) Macrophages were treated with or without 4 μM Akt inhibitor X (Akt X) for 2 h, followed by 2 h treatment with 10 μg/ml apoE3 or control medium alone. The cells were then treated with 3 μg/ml of calpain-1 or vehicle medium. ABCA1 (A1) protein was detected by immunoblotting, and quantified relative to GAPDH ( A–C ) or CD-MPR ( D ). ( E ) Macrophages were treated with 4 μM Akt X or vehicle medium for 2 h, followed by 2 h treatment with 10 μg/ml apoE3 or control medium. Calpain activity was measured with a calpain activity kit. Data represent mean ± SE of 3–4 independent experiments. ( A ) * P
    Human Blood, supplied by TaKaRa, used in various techniques. Bioz Stars score: 94/100, based on 3 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    90
    Millipore human ldlr
    Role of Calpain in ApoE-Induced ABCA1 Protein ( A ) Macrophages were treated with 100 μg/ml cycloheximide (CHX) or vehicle medium in the presence or absence of 4 μM Akt inhibitor X (Akt X) for 2 h, followed by 2 h incubation with 10 μg/ml <t>apoE3</t> or medium alone. ( B ) Macrophages were treated with vehicle medium (Veh), 50 μM ALLN, 1 mM leupeptin (Lpeptn), 10 μM aprotinin (Aprotn), 20μM pepstatin (Peptn), or 5 μM lactacystin (Lactyn) for 2 h. ( C ) Macrophages were treated with 50 μM ALLN or vehicle medium in the presence or absence of 4 μM Akt inhibitor X (Akt X) for 2 h, followed by 2 h incubation with 10 μg/ml apoE3 or control medium. ( D ) Macrophages were treated with or without 4 μM Akt inhibitor X (Akt X) for 2 h, followed by 2 h treatment with 10 μg/ml apoE3 or control medium alone. The cells were then treated with 3 μg/ml of calpain-1 or vehicle medium. ABCA1 (A1) protein was detected by immunoblotting, and quantified relative to GAPDH ( A–C ) or CD-MPR ( D ). ( E ) Macrophages were treated with 4 μM Akt X or vehicle medium for 2 h, followed by 2 h treatment with 10 μg/ml apoE3 or control medium. Calpain activity was measured with a calpain activity kit. Data represent mean ± SE of 3–4 independent experiments. ( A ) * P
    Human Ldlr, supplied by Millipore, used in various techniques. Bioz Stars score: 90/100, based on 15 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    94
    Millipore human stat3
    Mean ± SEM relative mRNA abundance of (A) all forms of the leptin receptor Ob-R and (B) the long-form leptin receptor Ob-Rb, and relative protein expression of (C) the long-form leptin receptor and (D) phosphorylated <t>STAT3</t> relative to total STAT3, in the lungs of sheep fetuses infused iv with either saline or leptin (0.5 or 1.0 LEP) for 5 days. †, significantly different from saline group, unpaired Student's t test, P
    Human Stat3, supplied by Millipore, used in various techniques. Bioz Stars score: 94/100, based on 26 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    94
    Millipore human wnt3a
    Growth of Math1 mutant intestinal organoids required exogenous Wnt. ( A ) Crypt organoids from adult control mice form efficiently during the first 3 d of culture. Note the presence of Paneth cells (indicated by asterisks) in the crypts from control mice. Progressive degeneration of Math1-deficient crypts occurred between days 2 and 3 in culture. Addition of <t>Wnt3a</t> supported the growth of Math1 mutant crypts into organoids. ( B and C ) Quantification of the total number of organoids ( B ) and the organoid structural complexity ( C ) of crypts from each mouse genotype during the first 3 d of culture in presence or absence of exogenous Wnt3a.
    Human Wnt3a, supplied by Millipore, used in various techniques. Bioz Stars score: 94/100, based on 4 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    94
    Millipore human nqo1
    SULT1B1 stimulates AA-I reactivity with DNA in the presence of <t>NQO1.</t> AA-I or 3-nitrobenzanthrone (100 μM) were incubated with DNA, PAPS, NADPH, 500nM of SULT1 enzymes and/or NQO1. Twenty micrograms of DNA was used for the adduct analysis. ( A) Fragment of a 30% polyacrylamide gel following 32 P-labeling. dG-AL-II or dA-AL-II (upper and lower band, respectively). Lanes 1–5, 2, 3, 4, 5, 6h incubations of AA-I, NQO1 and DNA, respectively; Lanes 6–10, AA-I, NQO1 and SULT1B1. ( B) Time dependence for AL-I-DNA adducts formation. ( C) The same experiment using 3-nitrobenzanthrone. Filled circles DNA adducts in the presence of NQO1, open circles represent DNA adducts in the presence of SULT1A2 and NQO1, filled triangles represent DNA adducts in the presence of SULT1B1 and NQO1. Results shown as mean values for at least two independent experiments.
    Human Nqo1, supplied by Millipore, used in various techniques. Bioz Stars score: 94/100, based on 9 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    97
    Millipore human sox2
    Mitogen deprivation reduced glioblastoma stem-like cell survival. a-h) GSCs were deprived from mitogens for 1 to 3 days. GSCs growing in mitogen-supplemented medium were used as a control (C). a) The number of secondary neurospheres per field of view (NS/FOV) was counted after 3 days of deprivation in GSCs #1-4. b) <t>Sox2</t> levels (green) were analyzed by confocal in GSCs #1-4. Nuclei were counterstained with DAPI (blue). Scale bar: 15 μm. c-d) Expression of Sox2 and Nestin as well as GADPH as a control, was evaluated by RT-PCR, while GFAP expression was analyzed by confocal analysis. Differentiation of GSC#4 was induced as described in methods. e) PI incorporation was measured by flow cytometry (10.000 events) in GSCs #1–14 and the percentage of cell death was estimated. Graph represents mean+s.d. of three independent experiments. Student’s t-test: *** P
    Human Sox2, supplied by Millipore, used in various techniques. Bioz Stars score: 97/100, based on 11 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    92
    Millipore human hdac3
    Knock down of <t>HDAC3</t> by shRNA does not affect global histone acetylation of HeLa S3 cells. (A) Western blotting showing knock down of HDAC3 in HeLa S3 cells. (B) Spectra of histone H3.1, H3.2 and H4 from control cells and HDAC3 knock down cells.
    Human Hdac3, supplied by Millipore, used in various techniques. Bioz Stars score: 92/100, based on 6 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    93
    Millipore human p52
    Knock down of <t>HDAC3</t> by shRNA does not affect global histone acetylation of HeLa S3 cells. (A) Western blotting showing knock down of HDAC3 in HeLa S3 cells. (B) Spectra of histone H3.1, H3.2 and H4 from control cells and HDAC3 knock down cells.
    Human P52, supplied by Millipore, used in various techniques. Bioz Stars score: 93/100, based on 8 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Image Search Results


    Impact of recombinase (RAD51) suppression in FLO-1 cells. FLO-1 cells were transduced with control (CS) or RAD51-specific (RS4) shRNAs and selected in puromycin. A: (I) RS4 lentiviruses mediate a strong suppression of RAD51. The expression profile of

    Journal: Cancer genomics & proteomics

    Article Title: Targeting PI3K and RAD51 in Barrett’s Adenocarcinoma: Impact on DNA Damage Checkpoints, Expression Profile and Tumor Growth

    doi:

    Figure Lengend Snippet: Impact of recombinase (RAD51) suppression in FLO-1 cells. FLO-1 cells were transduced with control (CS) or RAD51-specific (RS4) shRNAs and selected in puromycin. A: (I) RS4 lentiviruses mediate a strong suppression of RAD51. The expression profile of

    Article Snippet: Wortmannin and lentivirus particles producing either non-targeted control (CS) shRNAs or those targeting human RAD51 (RS4) were purchased from Sigma-Aldrich.

    Techniques: Transduction, Expressing

    Impact of RAD51 suppression on antitumor activity of wortmannin (WM): To investigate the combined effect of RAD51-suppression and wortmannin, both the wortmannin dose and RAD51 suppression were reduced so that separately these treatments did not have

    Journal: Cancer genomics & proteomics

    Article Title: Targeting PI3K and RAD51 in Barrett’s Adenocarcinoma: Impact on DNA Damage Checkpoints, Expression Profile and Tumor Growth

    doi:

    Figure Lengend Snippet: Impact of RAD51 suppression on antitumor activity of wortmannin (WM): To investigate the combined effect of RAD51-suppression and wortmannin, both the wortmannin dose and RAD51 suppression were reduced so that separately these treatments did not have

    Article Snippet: Wortmannin and lentivirus particles producing either non-targeted control (CS) shRNAs or those targeting human RAD51 (RS4) were purchased from Sigma-Aldrich.

    Techniques: Activity Assay

    Impact of RAD51 suppression on the efficacy of wortmannin (WM) in FLO-1 cells. FLO-1 cells, untransduced (FC) or transduced with control (CS) or RAD51-specific (RS4) shRNAs were treated with WM and evaluated for its impact on growth, telomere maintenance,

    Journal: Cancer genomics & proteomics

    Article Title: Targeting PI3K and RAD51 in Barrett’s Adenocarcinoma: Impact on DNA Damage Checkpoints, Expression Profile and Tumor Growth

    doi:

    Figure Lengend Snippet: Impact of RAD51 suppression on the efficacy of wortmannin (WM) in FLO-1 cells. FLO-1 cells, untransduced (FC) or transduced with control (CS) or RAD51-specific (RS4) shRNAs were treated with WM and evaluated for its impact on growth, telomere maintenance,

    Article Snippet: Wortmannin and lentivirus particles producing either non-targeted control (CS) shRNAs or those targeting human RAD51 (RS4) were purchased from Sigma-Aldrich.

    Techniques: Transduction

    Selective HDAC6 inhibitors down‐regulate PD‐L1 expression in vitro. (A) WM164, WM983A and WM793 human melanoma cell lines were incubated with the HDAC6 inhibitor Tubastatin A (3 μM) for 24 h, followed for

    Journal: Molecular Oncology

    Article Title: Essential Role of HDAC6 in the Regulation of PD-L1 in melanoma

    doi: 10.1016/j.molonc.2015.12.012

    Figure Lengend Snippet: Selective HDAC6 inhibitors down‐regulate PD‐L1 expression in vitro. (A) WM164, WM983A and WM793 human melanoma cell lines were incubated with the HDAC6 inhibitor Tubastatin A (3 μM) for 24 h, followed for

    Article Snippet: shRNA lentiviral transduction particles for murine HDAC6 (NM010413, TRCN0000008415), for human HDAC6 (NM00604, TRC0000004839) and non‐target shRNA (SHC002V) were obtained from Sigma Aldrich (St. Louis, MO).

    Techniques: Expressing, In Vitro, Incubation

    Constitutive active STAT3 rescue PD‐L1 expression in the absence of HDAC6. NT, HDAC6KD and STAT3KD WM164 melanoma cells were transfected with either STAT3C‐flag plasmid (B) or empty vector (A) and then stimulated with IL‐6 (30 ng/mL)

    Journal: Molecular Oncology

    Article Title: Essential Role of HDAC6 in the Regulation of PD-L1 in melanoma

    doi: 10.1016/j.molonc.2015.12.012

    Figure Lengend Snippet: Constitutive active STAT3 rescue PD‐L1 expression in the absence of HDAC6. NT, HDAC6KD and STAT3KD WM164 melanoma cells were transfected with either STAT3C‐flag plasmid (B) or empty vector (A) and then stimulated with IL‐6 (30 ng/mL)

    Article Snippet: shRNA lentiviral transduction particles for murine HDAC6 (NM010413, TRCN0000008415), for human HDAC6 (NM00604, TRC0000004839) and non‐target shRNA (SHC002V) were obtained from Sigma Aldrich (St. Louis, MO).

    Techniques: Expressing, Transfection, Plasmid Preparation

    Manipulation of HDAC6 modulates the expression of membrane co‐stimulatory molecules and other regulatory proteins. NT and HDAC6KD WM164 human melanoma cells were stimulated with IFNγ (100 ng/ml) or left untreated. Next, the presence

    Journal: Molecular Oncology

    Article Title: Essential Role of HDAC6 in the Regulation of PD-L1 in melanoma

    doi: 10.1016/j.molonc.2015.12.012

    Figure Lengend Snippet: Manipulation of HDAC6 modulates the expression of membrane co‐stimulatory molecules and other regulatory proteins. NT and HDAC6KD WM164 human melanoma cells were stimulated with IFNγ (100 ng/ml) or left untreated. Next, the presence

    Article Snippet: shRNA lentiviral transduction particles for murine HDAC6 (NM010413, TRCN0000008415), for human HDAC6 (NM00604, TRC0000004839) and non‐target shRNA (SHC002V) were obtained from Sigma Aldrich (St. Louis, MO).

    Techniques: Expressing

    Selective HDAC6 inhibitors down‐regulate PD‐L1 expression in vivo. In vivo tumor growth of C57BL/6 mice injected subcutaneously with B16‐F10‐luc WT cells. Mice were treated by intraperitoneal injection

    Journal: Molecular Oncology

    Article Title: Essential Role of HDAC6 in the Regulation of PD-L1 in melanoma

    doi: 10.1016/j.molonc.2015.12.012

    Figure Lengend Snippet: Selective HDAC6 inhibitors down‐regulate PD‐L1 expression in vivo. In vivo tumor growth of C57BL/6 mice injected subcutaneously with B16‐F10‐luc WT cells. Mice were treated by intraperitoneal injection

    Article Snippet: shRNA lentiviral transduction particles for murine HDAC6 (NM010413, TRCN0000008415), for human HDAC6 (NM00604, TRC0000004839) and non‐target shRNA (SHC002V) were obtained from Sigma Aldrich (St. Louis, MO).

    Techniques: Expressing, In Vivo, Mouse Assay, Injection

    HDAC6 and STAT3 are recruited to the PD‐L1 promoter. (A) Schematic diagram of the PD‐L1 promoter showing the potential STAT3 binding sites and primers used in the ChiP assays. ChiP analysis of WM164 wild type melanoma cell line stimulated

    Journal: Molecular Oncology

    Article Title: Essential Role of HDAC6 in the Regulation of PD-L1 in melanoma

    doi: 10.1016/j.molonc.2015.12.012

    Figure Lengend Snippet: HDAC6 and STAT3 are recruited to the PD‐L1 promoter. (A) Schematic diagram of the PD‐L1 promoter showing the potential STAT3 binding sites and primers used in the ChiP assays. ChiP analysis of WM164 wild type melanoma cell line stimulated

    Article Snippet: shRNA lentiviral transduction particles for murine HDAC6 (NM010413, TRCN0000008415), for human HDAC6 (NM00604, TRC0000004839) and non‐target shRNA (SHC002V) were obtained from Sigma Aldrich (St. Louis, MO).

    Techniques: Binding Assay, Chromatin Immunoprecipitation

    HDAC6 modulates the expression of PD‐L1 in melanoma cells. (A) NT and STAT3KD WM164, WM983A and WM793 melanoma cells were treated with IL‐6 (30 ng/mL) or left untreated. The presence of STAT3, PD‐L1 and GAPDH was evaluated

    Journal: Molecular Oncology

    Article Title: Essential Role of HDAC6 in the Regulation of PD-L1 in melanoma

    doi: 10.1016/j.molonc.2015.12.012

    Figure Lengend Snippet: HDAC6 modulates the expression of PD‐L1 in melanoma cells. (A) NT and STAT3KD WM164, WM983A and WM793 melanoma cells were treated with IL‐6 (30 ng/mL) or left untreated. The presence of STAT3, PD‐L1 and GAPDH was evaluated

    Article Snippet: shRNA lentiviral transduction particles for murine HDAC6 (NM010413, TRCN0000008415), for human HDAC6 (NM00604, TRC0000004839) and non‐target shRNA (SHC002V) were obtained from Sigma Aldrich (St. Louis, MO).

    Techniques: Expressing

    The absence of HDAC6 impairs the STAT3 activation in melanoma cells. (A) NT and HDAC6KD WM164, WM983A and WM793 melanoma cells were treated with IL‐6 (30 ng/mL) or left untreated. Then, the presence of HDAC6, acetylated tubulin, STAT3,

    Journal: Molecular Oncology

    Article Title: Essential Role of HDAC6 in the Regulation of PD-L1 in melanoma

    doi: 10.1016/j.molonc.2015.12.012

    Figure Lengend Snippet: The absence of HDAC6 impairs the STAT3 activation in melanoma cells. (A) NT and HDAC6KD WM164, WM983A and WM793 melanoma cells were treated with IL‐6 (30 ng/mL) or left untreated. Then, the presence of HDAC6, acetylated tubulin, STAT3,

    Article Snippet: shRNA lentiviral transduction particles for murine HDAC6 (NM010413, TRCN0000008415), for human HDAC6 (NM00604, TRC0000004839) and non‐target shRNA (SHC002V) were obtained from Sigma Aldrich (St. Louis, MO).

    Techniques: Activation Assay

    Mecp2 and sexual differentiation of juvenile play behavior

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

    Article Title: Mecp2 organizes juvenile social behavior in a sex-specific manner

    doi: 10.1523/JNEUROSCI.1345-08.2008

    Figure Lengend Snippet: Mecp2 and sexual differentiation of juvenile play behavior

    Article Snippet: Membranes were then incubated overnight at 4 °C with agitation in TBS containing 0.05% Tween-20 (TBS-T) and 2% nonfat dry milk with an antibody that recognizes the C-terminus of human MeCP2 (amino acids 465–478), a sequence conserved in rat and mouse (rabbit polyclonal, M9317; 1 : 2000 dilution, Sigma, St Louis, MO, USA).

    Techniques:

    Adult anxiety-like behaviors were not modified by neonatal amygdala Mecp2 disruption

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

    Article Title: Mecp2 organizes juvenile social behavior in a sex-specific manner

    doi: 10.1523/JNEUROSCI.1345-08.2008

    Figure Lengend Snippet: Adult anxiety-like behaviors were not modified by neonatal amygdala Mecp2 disruption

    Article Snippet: Membranes were then incubated overnight at 4 °C with agitation in TBS containing 0.05% Tween-20 (TBS-T) and 2% nonfat dry milk with an antibody that recognizes the C-terminus of human MeCP2 (amino acids 465–478), a sequence conserved in rat and mouse (rabbit polyclonal, M9317; 1 : 2000 dilution, Sigma, St Louis, MO, USA).

    Techniques: Modification

    Mecp2 disruption with siRNA

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

    Article Title: Mecp2 organizes juvenile social behavior in a sex-specific manner

    doi: 10.1523/JNEUROSCI.1345-08.2008

    Figure Lengend Snippet: Mecp2 disruption with siRNA

    Article Snippet: Membranes were then incubated overnight at 4 °C with agitation in TBS containing 0.05% Tween-20 (TBS-T) and 2% nonfat dry milk with an antibody that recognizes the C-terminus of human MeCP2 (amino acids 465–478), a sequence conserved in rat and mouse (rabbit polyclonal, M9317; 1 : 2000 dilution, Sigma, St Louis, MO, USA).

    Techniques:

    Mecp2 disruption and juvenile sociability

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

    Article Title: Mecp2 organizes juvenile social behavior in a sex-specific manner

    doi: 10.1523/JNEUROSCI.1345-08.2008

    Figure Lengend Snippet: Mecp2 disruption and juvenile sociability

    Article Snippet: Membranes were then incubated overnight at 4 °C with agitation in TBS containing 0.05% Tween-20 (TBS-T) and 2% nonfat dry milk with an antibody that recognizes the C-terminus of human MeCP2 (amino acids 465–478), a sequence conserved in rat and mouse (rabbit polyclonal, M9317; 1 : 2000 dilution, Sigma, St Louis, MO, USA).

    Techniques:

    Effect of E2 on VEGF and PEDF level in Cell Media. RhREC were grown for 24 h in a medium containing 0.0, 0.1, 1.0, or 10.0 nM E2. ELISA was performed and the cell medium was used to quantify VEGF (A) and PEDF (B) in the cell medium. (A)

    Journal: Journal of Ocular Pharmacology and Therapeutics

    Article Title: Effects of Tamoxifen Versus Raloxifene on Retinal Capillary Endothelial Cell Proliferation

    doi: 10.1089/jop.2010.0171

    Figure Lengend Snippet: Effect of E2 on VEGF and PEDF level in Cell Media. RhREC were grown for 24 h in a medium containing 0.0, 0.1, 1.0, or 10.0 nM E2. ELISA was performed and the cell medium was used to quantify VEGF (A) and PEDF (B) in the cell medium. (A)

    Article Snippet: To quantify rhesus monkey VEGF and PEDF in the medium, ELISAs for human VEGF (Invitrogen) and human PEDF (Millipore) were employed according to manufacturer's instructions.

    Techniques: Enzyme-linked Immunosorbent Assay

    MC protease expression identified by immunostaining over time. MCs were recovered after 2 d of culture in liquid suspension culture with SCF alone, in direct coculture with HAECs, in HAEC coculture separated by a transwell membrane, with HAEC-conditioned

    Journal:

    Article Title: Human airway epithelial cell determinants of survival and functional phenotype for primary human mast cells

    doi: 10.1073/pnas.0503948102

    Figure Lengend Snippet: MC protease expression identified by immunostaining over time. MCs were recovered after 2 d of culture in liquid suspension culture with SCF alone, in direct coculture with HAECs, in HAEC coculture separated by a transwell membrane, with HAEC-conditioned

    Article Snippet: Analysis of SCF protein expression from HAEC supernatants was performed by using a sandwich ELISA specific for human SCF (Chemicon).

    Techniques: Expressing, Immunostaining

    Effect of coculture of MCs with HAECs on IgE-dependent histamine release and eicosanoid generation as measured by ELISA. MCs were maintained in monoculture with SCF or in coculture with HAECs for 4 d. Results depict percentage histamine release, cys-LT

    Journal:

    Article Title: Human airway epithelial cell determinants of survival and functional phenotype for primary human mast cells

    doi: 10.1073/pnas.0503948102

    Figure Lengend Snippet: Effect of coculture of MCs with HAECs on IgE-dependent histamine release and eicosanoid generation as measured by ELISA. MCs were maintained in monoculture with SCF or in coculture with HAECs for 4 d. Results depict percentage histamine release, cys-LT

    Article Snippet: Analysis of SCF protein expression from HAEC supernatants was performed by using a sandwich ELISA specific for human SCF (Chemicon).

    Techniques: Enzyme-linked Immunosorbent Assay

    SCF protein expression by HAECs. Release of soluble SCF protein into HAEC culture media was detected by SCF-ELISA. ( A ) All data are mean ± SEM ( n = 4). Detection of membrane-bound SCF expression by immunohistochemical staining of HAECs by using

    Journal:

    Article Title: Human airway epithelial cell determinants of survival and functional phenotype for primary human mast cells

    doi: 10.1073/pnas.0503948102

    Figure Lengend Snippet: SCF protein expression by HAECs. Release of soluble SCF protein into HAEC culture media was detected by SCF-ELISA. ( A ) All data are mean ± SEM ( n = 4). Detection of membrane-bound SCF expression by immunohistochemical staining of HAECs by using

    Article Snippet: Analysis of SCF protein expression from HAEC supernatants was performed by using a sandwich ELISA specific for human SCF (Chemicon).

    Techniques: Expressing, Enzyme-linked Immunosorbent Assay, Immunohistochemistry, Staining

    Expression of SCF mRNA by HAECs. Soluble (572 bp) and membrane-bound (488 bp) SCF expression by HAECs was identified by RT-PCR analysis. SCF cDNA was amplified by 35 cycles of PCR. Lanes 1 and 2, HAEC donor 1; lanes 3 and 4, primary human MC; lanes 5

    Journal:

    Article Title: Human airway epithelial cell determinants of survival and functional phenotype for primary human mast cells

    doi: 10.1073/pnas.0503948102

    Figure Lengend Snippet: Expression of SCF mRNA by HAECs. Soluble (572 bp) and membrane-bound (488 bp) SCF expression by HAECs was identified by RT-PCR analysis. SCF cDNA was amplified by 35 cycles of PCR. Lanes 1 and 2, HAEC donor 1; lanes 3 and 4, primary human MC; lanes 5

    Article Snippet: Analysis of SCF protein expression from HAEC supernatants was performed by using a sandwich ELISA specific for human SCF (Chemicon).

    Techniques: Expressing, Reverse Transcription Polymerase Chain Reaction, Amplification, Polymerase Chain Reaction

    αBTX-induced AChR endocytosis is mediated by Src phosphorylation. (A) CHO-K1/A5 cells were cotransfected with dominant-negative Src K297R and GFP, and the internalization of AChR induced by αBTX was assessed in cells positive for Src K297R. Note the absence of punctate structures in cells transfected with dominant-negative Src K297R. (B) CHO-K1/A5 cells were labeled with b-αBTX in the presence or absence of 10 μM PP2 and chased for 6 h. Surface AChR levels were determined by measuring the accessibility of b-αBTX to SA-PE. The histogram shows the quantification of surface-accessible AChR in the presence or absence (αBTX alone) of PP2. Each bar represents the weighted mean of internal AChR as estimated using flow cytometry data from 10,000 cells (see Materials and methods) normalized to cells labeled with b-αBTX on ice. Error bars represent SEM. *, P

    Journal: The Journal of Cell Biology

    Article Title: Nicotinic acetylcholine receptor is internalized via a Rac-dependent, dynamin-independent endocytic pathway

    doi: 10.1083/jcb.200709086

    Figure Lengend Snippet: αBTX-induced AChR endocytosis is mediated by Src phosphorylation. (A) CHO-K1/A5 cells were cotransfected with dominant-negative Src K297R and GFP, and the internalization of AChR induced by αBTX was assessed in cells positive for Src K297R. Note the absence of punctate structures in cells transfected with dominant-negative Src K297R. (B) CHO-K1/A5 cells were labeled with b-αBTX in the presence or absence of 10 μM PP2 and chased for 6 h. Surface AChR levels were determined by measuring the accessibility of b-αBTX to SA-PE. The histogram shows the quantification of surface-accessible AChR in the presence or absence (αBTX alone) of PP2. Each bar represents the weighted mean of internal AChR as estimated using flow cytometry data from 10,000 cells (see Materials and methods) normalized to cells labeled with b-αBTX on ice. Error bars represent SEM. *, P

    Article Snippet: Wild-type and kinase-dead (K297R) isoforms of human Src obtained from Millipore were cloned into a mammalian expression vector, pCDNA3.1(B-)MycHis+, using available restriction sites.

    Techniques: Dominant Negative Mutation, Transfection, Labeling, Flow Cytometry, Cytometry

    IgG binding from human leptospirosis immune serum to L. interrogans . Bacteria were coated onto microtiter plates (25 × 10 6 leptospires/well) and IgG was bound by incubating bacteria 50% nonimmune human sera (NHS) or confirmed paired leptospirosis patients sera: MAT negative (MAT−) or MAT positive (MAT+). Bacteria were treated with PBS, 40 μ g/mL PLG (PLG), 5 μ g/mL uPA (uPA), or PLG + uPA (Pla). Presence of human IgG deposited on leptospires was determined by ELISA using Fc-specific anti-human IgG antibodies. Bars represent the mean absorbance values at 492 nm ± the standard deviation of three replicates for each experimental group and are representative of two independent experiments.

    Journal: Journal of Biomedicine and Biotechnology

    Article Title: Plasminogen Binding Proteins and Plasmin Generation on the Surface of Leptospira spp.: The Contribution to the Bacteria-Host Interactions

    doi: 10.1155/2012/758513

    Figure Lengend Snippet: IgG binding from human leptospirosis immune serum to L. interrogans . Bacteria were coated onto microtiter plates (25 × 10 6 leptospires/well) and IgG was bound by incubating bacteria 50% nonimmune human sera (NHS) or confirmed paired leptospirosis patients sera: MAT negative (MAT−) or MAT positive (MAT+). Bacteria were treated with PBS, 40 μ g/mL PLG (PLG), 5 μ g/mL uPA (uPA), or PLG + uPA (Pla). Presence of human IgG deposited on leptospires was determined by ELISA using Fc-specific anti-human IgG antibodies. Bars represent the mean absorbance values at 492 nm ± the standard deviation of three replicates for each experimental group and are representative of two independent experiments.

    Article Snippet: Wells were washed three times with PBS-T, and then 4 ng/well of human uPA (Sigma) were added.

    Techniques: Binding Assay, Proximity Ligation Assay, Enzyme-linked Immunosorbent Assay, Standard Deviation

    Cleavage of the plasmin-specific chromogenic substrate by plasmin-bound leptospires. Live low-passage virulent and high-passage nonvirulent L. interrogans serovar Copenhageni cells received the following treatments: PBS only (PBS), uPA alone (uPA), 5 μ g PLG alone (PLG), PLG in crescent quantities (0.5, 2 and 5 μ g) together with uPA, and 30% human plasma together with uPA (30% plasma). Bars represent mean absorbance as a measure of relative substrate degradation ± the standard deviation of three replicates for each experimental group and are representative of three independent experiments. *Virulent leptospires experiments: statistically significant ( P

    Journal: Journal of Biomedicine and Biotechnology

    Article Title: Plasminogen Binding Proteins and Plasmin Generation on the Surface of Leptospira spp.: The Contribution to the Bacteria-Host Interactions

    doi: 10.1155/2012/758513

    Figure Lengend Snippet: Cleavage of the plasmin-specific chromogenic substrate by plasmin-bound leptospires. Live low-passage virulent and high-passage nonvirulent L. interrogans serovar Copenhageni cells received the following treatments: PBS only (PBS), uPA alone (uPA), 5 μ g PLG alone (PLG), PLG in crescent quantities (0.5, 2 and 5 μ g) together with uPA, and 30% human plasma together with uPA (30% plasma). Bars represent mean absorbance as a measure of relative substrate degradation ± the standard deviation of three replicates for each experimental group and are representative of three independent experiments. *Virulent leptospires experiments: statistically significant ( P

    Article Snippet: Wells were washed three times with PBS-T, and then 4 ng/well of human uPA (Sigma) were added.

    Techniques: Standard Deviation

    Human IgG and C3b binding to L. interrogans. Bacteria were coated onto microtiter plates (25 × 10 6 leptospires/well) and IgG (a) or C3b (b)were bound by incubating bacteria with 100% NHS. Bacteria were treated with PBS, 40 μ g/mL PLG (PLG), 5 μ g/mL uPA (uPA), or PLG + uPA (Pla). Presence of human IgG or C3b deposited on leptospires was determined by ELISA. Bars represent the mean absorbance values at 492 nm ± the standard deviation of three replicates for each experimental group and are representative of two independent experiments.

    Journal: Journal of Biomedicine and Biotechnology

    Article Title: Plasminogen Binding Proteins and Plasmin Generation on the Surface of Leptospira spp.: The Contribution to the Bacteria-Host Interactions

    doi: 10.1155/2012/758513

    Figure Lengend Snippet: Human IgG and C3b binding to L. interrogans. Bacteria were coated onto microtiter plates (25 × 10 6 leptospires/well) and IgG (a) or C3b (b)were bound by incubating bacteria with 100% NHS. Bacteria were treated with PBS, 40 μ g/mL PLG (PLG), 5 μ g/mL uPA (uPA), or PLG + uPA (Pla). Presence of human IgG or C3b deposited on leptospires was determined by ELISA. Bars represent the mean absorbance values at 492 nm ± the standard deviation of three replicates for each experimental group and are representative of two independent experiments.

    Article Snippet: Wells were washed three times with PBS-T, and then 4 ng/well of human uPA (Sigma) were added.

    Techniques: Binding Assay, Proximity Ligation Assay, Enzyme-linked Immunosorbent Assay, Standard Deviation

    Inhibition of PLG binding to L. interrogans by ACA. Low-passage virulent L. interrogans serovar Copenhageni cells were treated with the following: PLG together with uPA (PLG + uPA), PLG together with uPA with the addition of crescent concentrations of ACA (0.01 to 1,000 mM ACA), PLG alone (PLG), uPA alone (uPA), ACA alone (ACA), and no additions (PBS). The cleavage of the plasmin-specific substrate D-Val-Leu-Lys 4-nitroanilide dihydrochloridein by the treated spirochetes was measured by absorbance readings at 405 nm. Bars represent mean absorbance ± the standard deviation of three replicates for each experimental group and are representative of three independent experiments. Statistically significant substrate degradation inhibition results in comparison to the positive control (PLG + uPA) are shown: P

    Journal: Journal of Biomedicine and Biotechnology

    Article Title: Plasminogen Binding Proteins and Plasmin Generation on the Surface of Leptospira spp.: The Contribution to the Bacteria-Host Interactions

    doi: 10.1155/2012/758513

    Figure Lengend Snippet: Inhibition of PLG binding to L. interrogans by ACA. Low-passage virulent L. interrogans serovar Copenhageni cells were treated with the following: PLG together with uPA (PLG + uPA), PLG together with uPA with the addition of crescent concentrations of ACA (0.01 to 1,000 mM ACA), PLG alone (PLG), uPA alone (uPA), ACA alone (ACA), and no additions (PBS). The cleavage of the plasmin-specific substrate D-Val-Leu-Lys 4-nitroanilide dihydrochloridein by the treated spirochetes was measured by absorbance readings at 405 nm. Bars represent mean absorbance ± the standard deviation of three replicates for each experimental group and are representative of three independent experiments. Statistically significant substrate degradation inhibition results in comparison to the positive control (PLG + uPA) are shown: P

    Article Snippet: Wells were washed three times with PBS-T, and then 4 ng/well of human uPA (Sigma) were added.

    Techniques: Inhibition, Binding Assay, Standard Deviation, Positive Control

    Western immunoblot of AKR1C3 (17β-HSD5) protein in a feminizing estrogen-secreting adrenal carcinoma, an aldosterone-producing adrenal adenoma, and H295 cells after treatment (24 hours) with either VIP (100 nM) or forskolin (10 μM). Lane 1: Aldosterone-producing adrenal adenoma (25 μg protein); lane 2: Estrogen-secreting adrenal carcinoma (25 μg protein); lane 3: Untreated control H295 cells (25 μg protein); lane 4: Forskolin (Fsk)-treated H295 cells (25 μg protein); lane 5: VIP-treated H295 cells (25 μg protein).

    Journal: Molecular and cellular endocrinology

    Article Title: Estrogen biosynthesis in human H295 adrenocortical carcinoma cells

    doi: 10.1016/j.mce.2008.10.032

    Figure Lengend Snippet: Western immunoblot of AKR1C3 (17β-HSD5) protein in a feminizing estrogen-secreting adrenal carcinoma, an aldosterone-producing adrenal adenoma, and H295 cells after treatment (24 hours) with either VIP (100 nM) or forskolin (10 μM). Lane 1: Aldosterone-producing adrenal adenoma (25 μg protein); lane 2: Estrogen-secreting adrenal carcinoma (25 μg protein); lane 3: Untreated control H295 cells (25 μg protein); lane 4: Forskolin (Fsk)-treated H295 cells (25 μg protein); lane 5: VIP-treated H295 cells (25 μg protein).

    Article Snippet: This was followed by an overnight incubation at 4°C with the mouse monoclonal antibody (Novartis #677, ) against human aromatase at 1:3000 dilution in 5% dried semi-skimmed milk/PBST, or a mouse monoclonal antibody (1:1000 dilution) against human AKR1C3 (17β-HSD5) , before incubation (1h) with a donkey anti-mouse IgG conjugated to horseradish peroxidase (Sigma) at 1:20000 dilution.

    Techniques: Western Blot

    Immunolocalization of AKR1C3 and CYP19 in an adrenal containing an estrogen-secreting adrenal adenocarcinoma. A. Immunohistochemistry for AKR1C3 showing normal adrenal cortex with higher expression centrally in the lipid-poorer cells of the zona reticularis (ZR) than in the lipid-rich cells of the zona fasciculata (ZF); the adrenal capsule is located at the extreme right of the image (original magnification x20). B. Immunohistochemistry for AKR1C3 showing normal adrenal cortex with higher expression in the lipid-poorer cells of the zona reticularis (centre) than in the lipid-rich cells of the zona fasciculata (right); adrenal capsule to the far right of the image (original magnification x40). C. Immunohistochemistry for AKR1C3 showing expression in the carcinoma cells (left), tumor capsule (centrally) and some of the normal adrenocortical cells (right) (original magnification x20). D. Immunohistochemistry for aromatase, showing expression in many of the carcinoma cells (left) and the normal adrenal cortex to be negative (right) (original magnification x20).

    Journal: Molecular and cellular endocrinology

    Article Title: Estrogen biosynthesis in human H295 adrenocortical carcinoma cells

    doi: 10.1016/j.mce.2008.10.032

    Figure Lengend Snippet: Immunolocalization of AKR1C3 and CYP19 in an adrenal containing an estrogen-secreting adrenal adenocarcinoma. A. Immunohistochemistry for AKR1C3 showing normal adrenal cortex with higher expression centrally in the lipid-poorer cells of the zona reticularis (ZR) than in the lipid-rich cells of the zona fasciculata (ZF); the adrenal capsule is located at the extreme right of the image (original magnification x20). B. Immunohistochemistry for AKR1C3 showing normal adrenal cortex with higher expression in the lipid-poorer cells of the zona reticularis (centre) than in the lipid-rich cells of the zona fasciculata (right); adrenal capsule to the far right of the image (original magnification x40). C. Immunohistochemistry for AKR1C3 showing expression in the carcinoma cells (left), tumor capsule (centrally) and some of the normal adrenocortical cells (right) (original magnification x20). D. Immunohistochemistry for aromatase, showing expression in many of the carcinoma cells (left) and the normal adrenal cortex to be negative (right) (original magnification x20).

    Article Snippet: This was followed by an overnight incubation at 4°C with the mouse monoclonal antibody (Novartis #677, ) against human aromatase at 1:3000 dilution in 5% dried semi-skimmed milk/PBST, or a mouse monoclonal antibody (1:1000 dilution) against human AKR1C3 (17β-HSD5) , before incubation (1h) with a donkey anti-mouse IgG conjugated to horseradish peroxidase (Sigma) at 1:20000 dilution.

    Techniques: Immunohistochemistry, Expressing

    Role of Calpain in ApoE-Induced ABCA1 Protein ( A ) Macrophages were treated with 100 μg/ml cycloheximide (CHX) or vehicle medium in the presence or absence of 4 μM Akt inhibitor X (Akt X) for 2 h, followed by 2 h incubation with 10 μg/ml apoE3 or medium alone. ( B ) Macrophages were treated with vehicle medium (Veh), 50 μM ALLN, 1 mM leupeptin (Lpeptn), 10 μM aprotinin (Aprotn), 20μM pepstatin (Peptn), or 5 μM lactacystin (Lactyn) for 2 h. ( C ) Macrophages were treated with 50 μM ALLN or vehicle medium in the presence or absence of 4 μM Akt inhibitor X (Akt X) for 2 h, followed by 2 h incubation with 10 μg/ml apoE3 or control medium. ( D ) Macrophages were treated with or without 4 μM Akt inhibitor X (Akt X) for 2 h, followed by 2 h treatment with 10 μg/ml apoE3 or control medium alone. The cells were then treated with 3 μg/ml of calpain-1 or vehicle medium. ABCA1 (A1) protein was detected by immunoblotting, and quantified relative to GAPDH ( A–C ) or CD-MPR ( D ). ( E ) Macrophages were treated with 4 μM Akt X or vehicle medium for 2 h, followed by 2 h treatment with 10 μg/ml apoE3 or control medium. Calpain activity was measured with a calpain activity kit. Data represent mean ± SE of 3–4 independent experiments. ( A ) * P

    Journal: Biochemical and biophysical research communications

    Article Title: Akt Isoform-Dependent Regulation of ATP-Binding Cassette A1 Expression by Apolipoprotein E

    doi: 10.1016/j.bbrc.2016.06.031

    Figure Lengend Snippet: Role of Calpain in ApoE-Induced ABCA1 Protein ( A ) Macrophages were treated with 100 μg/ml cycloheximide (CHX) or vehicle medium in the presence or absence of 4 μM Akt inhibitor X (Akt X) for 2 h, followed by 2 h incubation with 10 μg/ml apoE3 or medium alone. ( B ) Macrophages were treated with vehicle medium (Veh), 50 μM ALLN, 1 mM leupeptin (Lpeptn), 10 μM aprotinin (Aprotn), 20μM pepstatin (Peptn), or 5 μM lactacystin (Lactyn) for 2 h. ( C ) Macrophages were treated with 50 μM ALLN or vehicle medium in the presence or absence of 4 μM Akt inhibitor X (Akt X) for 2 h, followed by 2 h incubation with 10 μg/ml apoE3 or control medium. ( D ) Macrophages were treated with or without 4 μM Akt inhibitor X (Akt X) for 2 h, followed by 2 h treatment with 10 μg/ml apoE3 or control medium alone. The cells were then treated with 3 μg/ml of calpain-1 or vehicle medium. ABCA1 (A1) protein was detected by immunoblotting, and quantified relative to GAPDH ( A–C ) or CD-MPR ( D ). ( E ) Macrophages were treated with 4 μM Akt X or vehicle medium for 2 h, followed by 2 h treatment with 10 μg/ml apoE3 or control medium. Calpain activity was measured with a calpain activity kit. Data represent mean ± SE of 3–4 independent experiments. ( A ) * P

    Article Snippet: Human apoE3 (SRP4696), Calpain-1 (C6108) and cycloheximide (C7698) were purchased from Sigma-Aldrich (St. Louis, MO).

    Techniques: Incubation, Activity Assay

    Effect of ApoE3 on Akt Isoform Phosphorylation, and effect of Akt Isoform Knockdown on ABCA1 Protein ( A–B ) Macrophages were treated with apoE3 or medium alone as a control (Ctrl) for 2 h. ( C–F ) Macrophages were transfected with Akt1, Akt2 or Akt3 siRNA (respectively designated as siAkt1, siAkt2 and siAkt3), or scrambled siRNAs (scrmb), and treated with apoE3 or culture medium alone (Ctrl) for 2 h. Phosphorylated Akt (pAkt), total Akt and ABCA1 were detected by immunoblotting, and quantified relative to total Akt ( B ) and GAPDH (GPD) ( D and F ), respectively. The data represent mean ± SE of 4–5 independent experiments. * P

    Journal: Biochemical and biophysical research communications

    Article Title: Akt Isoform-Dependent Regulation of ATP-Binding Cassette A1 Expression by Apolipoprotein E

    doi: 10.1016/j.bbrc.2016.06.031

    Figure Lengend Snippet: Effect of ApoE3 on Akt Isoform Phosphorylation, and effect of Akt Isoform Knockdown on ABCA1 Protein ( A–B ) Macrophages were treated with apoE3 or medium alone as a control (Ctrl) for 2 h. ( C–F ) Macrophages were transfected with Akt1, Akt2 or Akt3 siRNA (respectively designated as siAkt1, siAkt2 and siAkt3), or scrambled siRNAs (scrmb), and treated with apoE3 or culture medium alone (Ctrl) for 2 h. Phosphorylated Akt (pAkt), total Akt and ABCA1 were detected by immunoblotting, and quantified relative to total Akt ( B ) and GAPDH (GPD) ( D and F ), respectively. The data represent mean ± SE of 4–5 independent experiments. * P

    Article Snippet: Human apoE3 (SRP4696), Calpain-1 (C6108) and cycloheximide (C7698) were purchased from Sigma-Aldrich (St. Louis, MO).

    Techniques: Transfection

    Effect of Akt Isoform Overexpression on ABCA1 Protein Macrophages were transfected with Akt1 or Akt2 expression vectors (respectively designated as Akt1Tg and Akt2Tg) or empty vectors ( A–B ). The plasmid-transfected cells were treated with apoE3 or control medium (Ctrl) for 2 h ( C–D ). Akt1/2 and ABCA1 were detected by immunoblotting, quantified relative to GAPDH. Data represent the mean ± SEM of 3–4 independent experiments. * P

    Journal: Biochemical and biophysical research communications

    Article Title: Akt Isoform-Dependent Regulation of ATP-Binding Cassette A1 Expression by Apolipoprotein E

    doi: 10.1016/j.bbrc.2016.06.031

    Figure Lengend Snippet: Effect of Akt Isoform Overexpression on ABCA1 Protein Macrophages were transfected with Akt1 or Akt2 expression vectors (respectively designated as Akt1Tg and Akt2Tg) or empty vectors ( A–B ). The plasmid-transfected cells were treated with apoE3 or control medium (Ctrl) for 2 h ( C–D ). Akt1/2 and ABCA1 were detected by immunoblotting, quantified relative to GAPDH. Data represent the mean ± SEM of 3–4 independent experiments. * P

    Article Snippet: Human apoE3 (SRP4696), Calpain-1 (C6108) and cycloheximide (C7698) were purchased from Sigma-Aldrich (St. Louis, MO).

    Techniques: Over Expression, Transfection, Expressing, Plasmid Preparation

    Mean ± SEM relative mRNA abundance of (A) all forms of the leptin receptor Ob-R and (B) the long-form leptin receptor Ob-Rb, and relative protein expression of (C) the long-form leptin receptor and (D) phosphorylated STAT3 relative to total STAT3, in the lungs of sheep fetuses infused iv with either saline or leptin (0.5 or 1.0 LEP) for 5 days. †, significantly different from saline group, unpaired Student's t test, P

    Journal: Endocrinology

    Article Title: Leptin Matures Aspects of Lung Structure and Function in the Ovine Fetus

    doi: 10.1210/en.2015-1729

    Figure Lengend Snippet: Mean ± SEM relative mRNA abundance of (A) all forms of the leptin receptor Ob-R and (B) the long-form leptin receptor Ob-Rb, and relative protein expression of (C) the long-form leptin receptor and (D) phosphorylated STAT3 relative to total STAT3, in the lungs of sheep fetuses infused iv with either saline or leptin (0.5 or 1.0 LEP) for 5 days. †, significantly different from saline group, unpaired Student's t test, P

    Article Snippet: Equal amounts of sample protein were separated using 7.5% Mini-PROTEAN precast gels followed by incubation overnight at 4°C with rabbit polyclonal primary antibodies ( ) to 1) the ovine long-form leptin receptor (Ob-Rb) (2-μg/mL orb6312; Biorbyt); 2) the mouse phosphorylated STAT3 containing Ser727 (0.5-μg/mL sc-8001-R; Insight Biotechnology Ltd); or 3) the human STAT3 (1:500, 07-2173; Millipore) ( ).

    Techniques: Expressing

    Growth of Math1 mutant intestinal organoids required exogenous Wnt. ( A ) Crypt organoids from adult control mice form efficiently during the first 3 d of culture. Note the presence of Paneth cells (indicated by asterisks) in the crypts from control mice. Progressive degeneration of Math1-deficient crypts occurred between days 2 and 3 in culture. Addition of Wnt3a supported the growth of Math1 mutant crypts into organoids. ( B and C ) Quantification of the total number of organoids ( B ) and the organoid structural complexity ( C ) of crypts from each mouse genotype during the first 3 d of culture in presence or absence of exogenous Wnt3a.

    Journal: Proceedings of the National Academy of Sciences of the United States of America

    Article Title: Functional intestinal stem cells after Paneth cell ablation induced by the loss of transcription factor Math1 (Atoh1)

    doi: 10.1073/pnas.1201652109

    Figure Lengend Snippet: Growth of Math1 mutant intestinal organoids required exogenous Wnt. ( A ) Crypt organoids from adult control mice form efficiently during the first 3 d of culture. Note the presence of Paneth cells (indicated by asterisks) in the crypts from control mice. Progressive degeneration of Math1-deficient crypts occurred between days 2 and 3 in culture. Addition of Wnt3a supported the growth of Math1 mutant crypts into organoids. ( B and C ) Quantification of the total number of organoids ( B ) and the organoid structural complexity ( C ) of crypts from each mouse genotype during the first 3 d of culture in presence or absence of exogenous Wnt3a.

    Article Snippet: In some experiments, media were supplemented with 100 ng/mL human Wnt3a (Millipore).

    Techniques: Mutagenesis, Mouse Assay

    SULT1B1 stimulates AA-I reactivity with DNA in the presence of NQO1. AA-I or 3-nitrobenzanthrone (100 μM) were incubated with DNA, PAPS, NADPH, 500nM of SULT1 enzymes and/or NQO1. Twenty micrograms of DNA was used for the adduct analysis. ( A) Fragment of a 30% polyacrylamide gel following 32 P-labeling. dG-AL-II or dA-AL-II (upper and lower band, respectively). Lanes 1–5, 2, 3, 4, 5, 6h incubations of AA-I, NQO1 and DNA, respectively; Lanes 6–10, AA-I, NQO1 and SULT1B1. ( B) Time dependence for AL-I-DNA adducts formation. ( C) The same experiment using 3-nitrobenzanthrone. Filled circles DNA adducts in the presence of NQO1, open circles represent DNA adducts in the presence of SULT1A2 and NQO1, filled triangles represent DNA adducts in the presence of SULT1B1 and NQO1. Results shown as mean values for at least two independent experiments.

    Journal: Carcinogenesis

    Article Title: Bioactivation of the human carcinogen aristolochic acid

    doi: 10.1093/carcin/bgu095

    Figure Lengend Snippet: SULT1B1 stimulates AA-I reactivity with DNA in the presence of NQO1. AA-I or 3-nitrobenzanthrone (100 μM) were incubated with DNA, PAPS, NADPH, 500nM of SULT1 enzymes and/or NQO1. Twenty micrograms of DNA was used for the adduct analysis. ( A) Fragment of a 30% polyacrylamide gel following 32 P-labeling. dG-AL-II or dA-AL-II (upper and lower band, respectively). Lanes 1–5, 2, 3, 4, 5, 6h incubations of AA-I, NQO1 and DNA, respectively; Lanes 6–10, AA-I, NQO1 and SULT1B1. ( B) Time dependence for AL-I-DNA adducts formation. ( C) The same experiment using 3-nitrobenzanthrone. Filled circles DNA adducts in the presence of NQO1, open circles represent DNA adducts in the presence of SULT1A2 and NQO1, filled triangles represent DNA adducts in the presence of SULT1B1 and NQO1. Results shown as mean values for at least two independent experiments.

    Article Snippet: Human NQO1 was purchased from Sigma–Aldrich.

    Techniques: Incubation, Papanicolaou Stain, Labeling

    Mitogen deprivation reduced glioblastoma stem-like cell survival. a-h) GSCs were deprived from mitogens for 1 to 3 days. GSCs growing in mitogen-supplemented medium were used as a control (C). a) The number of secondary neurospheres per field of view (NS/FOV) was counted after 3 days of deprivation in GSCs #1-4. b) Sox2 levels (green) were analyzed by confocal in GSCs #1-4. Nuclei were counterstained with DAPI (blue). Scale bar: 15 μm. c-d) Expression of Sox2 and Nestin as well as GADPH as a control, was evaluated by RT-PCR, while GFAP expression was analyzed by confocal analysis. Differentiation of GSC#4 was induced as described in methods. e) PI incorporation was measured by flow cytometry (10.000 events) in GSCs #1–14 and the percentage of cell death was estimated. Graph represents mean+s.d. of three independent experiments. Student’s t-test: *** P

    Journal: PLoS ONE

    Article Title: Endothelial Secreted Factors Suppress Mitogen Deprivation-Induced Autophagy and Apoptosis in Glioblastoma Stem-Like Cells

    doi: 10.1371/journal.pone.0093505

    Figure Lengend Snippet: Mitogen deprivation reduced glioblastoma stem-like cell survival. a-h) GSCs were deprived from mitogens for 1 to 3 days. GSCs growing in mitogen-supplemented medium were used as a control (C). a) The number of secondary neurospheres per field of view (NS/FOV) was counted after 3 days of deprivation in GSCs #1-4. b) Sox2 levels (green) were analyzed by confocal in GSCs #1-4. Nuclei were counterstained with DAPI (blue). Scale bar: 15 μm. c-d) Expression of Sox2 and Nestin as well as GADPH as a control, was evaluated by RT-PCR, while GFAP expression was analyzed by confocal analysis. Differentiation of GSC#4 was induced as described in methods. e) PI incorporation was measured by flow cytometry (10.000 events) in GSCs #1–14 and the percentage of cell death was estimated. Graph represents mean+s.d. of three independent experiments. Student’s t-test: *** P

    Article Snippet: Equal amounts of RNA were reverse transcribed using the Maxima Reverse Transcriptase (Thermo Scientific) and the resulting cDNA was used to amplify Nestin and Sox2 transcripts by PCR using gene-specific primers for human Sox2 (Fwd: 5′-CAAAAATGGCCATGCAGGTT-3′ ; Rev: 5′-AGTTGGGATCGAACAAAAGCTATT-3′ ) and human Nestin (Fwd: 5′-TTCTCTTGTCCCGCAGACTT-3′ ; Rev: 5′ AACAGCGACGGAGGTCTCTA-3′) in the presence of RedTaq Mix (Sigma), as described previously .

    Techniques: Expressing, Reverse Transcription Polymerase Chain Reaction, Flow Cytometry, Cytometry

    Knock down of HDAC3 by shRNA does not affect global histone acetylation of HeLa S3 cells. (A) Western blotting showing knock down of HDAC3 in HeLa S3 cells. (B) Spectra of histone H3.1, H3.2 and H4 from control cells and HDAC3 knock down cells.

    Journal: Journal of chromatography. B, Analytical technologies in the biomedical and life sciences

    Article Title: Global Histone Profiling by LC-FTMS after Inhibition and Knockdown of Deacetylases in Human Cells

    doi: 10.1016/j.jchromb.2009.09.042

    Figure Lengend Snippet: Knock down of HDAC3 by shRNA does not affect global histone acetylation of HeLa S3 cells. (A) Western blotting showing knock down of HDAC3 in HeLa S3 cells. (B) Spectra of histone H3.1, H3.2 and H4 from control cells and HDAC3 knock down cells.

    Article Snippet: shRNAs for human HDAC3 constructed in pLKO.1-Puro vectors were purchased from Sigma (Mission shRNA) and contained 5 constructs with different target sequences, all of which were packaged for viral production and infection, and tested for target knockdown. shRNA with scrambled sequence was used for a negative control.

    Techniques: shRNA, Western Blot