mouse anti human ccnd1 monoclonal antibody Search Results


90
Agilent technologies mouse anti-cyclin d1 antibody
A. Illustration of less aggressive growth (Border) and distinct cell death (Inside) caused by lumbar puncture (LP) resveratrol through HE staining. B. TUNEL labeling and <t>Cyclin</t> <t>D1</t> immunohistochemical staining performed on the tumors treated by lumbar punctured 0.3% DMSO (C) and resveratrol (Res). C, D. The incidences of TUNEL-positive and Cyclin D1-positive cells in the two experimental groups.
Mouse Anti Cyclin D1 Antibody, supplied by Agilent technologies, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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Arigo Biolaboratories mouse anti-cyclin-d1
A. Illustration of less aggressive growth (Border) and distinct cell death (Inside) caused by lumbar puncture (LP) resveratrol through HE staining. B. TUNEL labeling and <t>Cyclin</t> <t>D1</t> immunohistochemical staining performed on the tumors treated by lumbar punctured 0.3% DMSO (C) and resveratrol (Res). C, D. The incidences of TUNEL-positive and Cyclin D1-positive cells in the two experimental groups.
Mouse Anti Cyclin D1, supplied by Arigo Biolaboratories, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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OriGene anti-cyclin d1
A. Illustration of less aggressive growth (Border) and distinct cell death (Inside) caused by lumbar puncture (LP) resveratrol through HE staining. B. TUNEL labeling and <t>Cyclin</t> <t>D1</t> immunohistochemical staining performed on the tumors treated by lumbar punctured 0.3% DMSO (C) and resveratrol (Res). C, D. The incidences of TUNEL-positive and Cyclin D1-positive cells in the two experimental groups.
Anti Cyclin D1, supplied by OriGene, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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Boster Bio anti cyclin d1
A. Illustration of less aggressive growth (Border) and distinct cell death (Inside) caused by lumbar puncture (LP) resveratrol through HE staining. B. TUNEL labeling and <t>Cyclin</t> <t>D1</t> immunohistochemical staining performed on the tumors treated by lumbar punctured 0.3% DMSO (C) and resveratrol (Res). C, D. The incidences of TUNEL-positive and Cyclin D1-positive cells in the two experimental groups.
Anti Cyclin D1, supplied by Boster Bio, used in various techniques. Bioz Stars score: 95/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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Average 95 stars, based on 1 article reviews
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98
Cell Signaling Technology Inc mouse anti cyclin d1
A. Illustration of less aggressive growth (Border) and distinct cell death (Inside) caused by lumbar puncture (LP) resveratrol through HE staining. B. TUNEL labeling and <t>Cyclin</t> <t>D1</t> immunohistochemical staining performed on the tumors treated by lumbar punctured 0.3% DMSO (C) and resveratrol (Res). C, D. The incidences of TUNEL-positive and Cyclin D1-positive cells in the two experimental groups.
Mouse Anti Cyclin D1, supplied by Cell Signaling Technology Inc, used in various techniques. Bioz Stars score: 98/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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Cell Signaling Technology Inc anti cyclin d1 rabbit pab
A. Illustration of less aggressive growth (Border) and distinct cell death (Inside) caused by lumbar puncture (LP) resveratrol through HE staining. B. TUNEL labeling and <t>Cyclin</t> <t>D1</t> immunohistochemical staining performed on the tumors treated by lumbar punctured 0.3% DMSO (C) and resveratrol (Res). C, D. The incidences of TUNEL-positive and Cyclin D1-positive cells in the two experimental groups.
Anti Cyclin D1 Rabbit Pab, supplied by Cell Signaling Technology Inc, used in various techniques. Bioz Stars score: 97/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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Santa Cruz Biotechnology rabbit anti cyclin d1 polyclonal ab
A. Illustration of less aggressive growth (Border) and distinct cell death (Inside) caused by lumbar puncture (LP) resveratrol through HE staining. B. TUNEL labeling and <t>Cyclin</t> <t>D1</t> immunohistochemical staining performed on the tumors treated by lumbar punctured 0.3% DMSO (C) and resveratrol (Res). C, D. The incidences of TUNEL-positive and Cyclin D1-positive cells in the two experimental groups.
Rabbit Anti Cyclin D1 Polyclonal Ab, supplied by Santa Cruz Biotechnology, used in various techniques. Bioz Stars score: 98/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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96
Santa Cruz Biotechnology anti cyclin d1
A. Illustration of less aggressive growth (Border) and distinct cell death (Inside) caused by lumbar puncture (LP) resveratrol through HE staining. B. TUNEL labeling and <t>Cyclin</t> <t>D1</t> immunohistochemical staining performed on the tumors treated by lumbar punctured 0.3% DMSO (C) and resveratrol (Res). C, D. The incidences of TUNEL-positive and Cyclin D1-positive cells in the two experimental groups.
Anti Cyclin D1, supplied by Santa Cruz Biotechnology, used in various techniques. Bioz Stars score: 96/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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96
Proteintech cyclin d1
Figure 3. Knockdown of MUC1 expression alters the β‑catenin signaling pathway by blocking β‑catenin translocation to the nucleus. (A) Cell lysates from NC and MR1-D4 clones were subjected to immunoprecipitation (IP) with anti-MUC1-CT antibody or normal IgG and then immunoblotted (IB) with anti‑β‑catenin antibody. Whole cell lysate (WCL) was not subjected to immunoprecipitation. (B) Cytoplasmic extracts from SMMC-7721, NC, MR1-C6 and MR1-D4 cells were analyzed by western blotting for the expression of β‑catenin. Cytoplasmic IκBα was used as a protein loading control. (C) Nuclear extracts from SMMC‑7721, NC, MR1-C6 and MR1-D4 cells were detected by western blotting to assess the levels of nuclear β‑catenin. Lamin B1 served as the nuclear loading control. (D) NC, MR1-C6 and MR1-D4 cells were transiently transfected with TOPflash and FOPflash plasmids. Relative luciferase activity was cal culated as the ratio of TOPflash/FOPflash luciferase activity, and each value was normalized to the luciferase activity of the internal control pRL-TK reporter plasmid. (E) mRNA levels of <t>cyclin</t> <t>D1</t> and c-Myc in NC, MR1-C6 and MR1-D4 cells were detected by qRT-PCR and normalized to β‑actin. Bars represent the relative mRNA level when compared to the NC cells. (F) Cell lysates were analyzed by western blotting for the expression of cyclin D1 and c-Myc. β‑actin was used as a loading control. Data are expressed as the means ± SDs of 3 independent experiments. *P<0.05 compared with NC.
Cyclin D1, supplied by Proteintech, used in various techniques. Bioz Stars score: 96/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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96
Santa Cruz Biotechnology cyclin d1
Figure 3. Knockdown of MUC1 expression alters the β‑catenin signaling pathway by blocking β‑catenin translocation to the nucleus. (A) Cell lysates from NC and MR1-D4 clones were subjected to immunoprecipitation (IP) with anti-MUC1-CT antibody or normal IgG and then immunoblotted (IB) with anti‑β‑catenin antibody. Whole cell lysate (WCL) was not subjected to immunoprecipitation. (B) Cytoplasmic extracts from SMMC-7721, NC, MR1-C6 and MR1-D4 cells were analyzed by western blotting for the expression of β‑catenin. Cytoplasmic IκBα was used as a protein loading control. (C) Nuclear extracts from SMMC‑7721, NC, MR1-C6 and MR1-D4 cells were detected by western blotting to assess the levels of nuclear β‑catenin. Lamin B1 served as the nuclear loading control. (D) NC, MR1-C6 and MR1-D4 cells were transiently transfected with TOPflash and FOPflash plasmids. Relative luciferase activity was cal culated as the ratio of TOPflash/FOPflash luciferase activity, and each value was normalized to the luciferase activity of the internal control pRL-TK reporter plasmid. (E) mRNA levels of <t>cyclin</t> <t>D1</t> and c-Myc in NC, MR1-C6 and MR1-D4 cells were detected by qRT-PCR and normalized to β‑actin. Bars represent the relative mRNA level when compared to the NC cells. (F) Cell lysates were analyzed by western blotting for the expression of cyclin D1 and c-Myc. β‑actin was used as a loading control. Data are expressed as the means ± SDs of 3 independent experiments. *P<0.05 compared with NC.
Cyclin D1, supplied by Santa Cruz Biotechnology, used in various techniques. Bioz Stars score: 96/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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Average 96 stars, based on 1 article reviews
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90
Novocastra mouse monoclonal cyclin d1 antibody
Figure 3. Knockdown of MUC1 expression alters the β‑catenin signaling pathway by blocking β‑catenin translocation to the nucleus. (A) Cell lysates from NC and MR1-D4 clones were subjected to immunoprecipitation (IP) with anti-MUC1-CT antibody or normal IgG and then immunoblotted (IB) with anti‑β‑catenin antibody. Whole cell lysate (WCL) was not subjected to immunoprecipitation. (B) Cytoplasmic extracts from SMMC-7721, NC, MR1-C6 and MR1-D4 cells were analyzed by western blotting for the expression of β‑catenin. Cytoplasmic IκBα was used as a protein loading control. (C) Nuclear extracts from SMMC‑7721, NC, MR1-C6 and MR1-D4 cells were detected by western blotting to assess the levels of nuclear β‑catenin. Lamin B1 served as the nuclear loading control. (D) NC, MR1-C6 and MR1-D4 cells were transiently transfected with TOPflash and FOPflash plasmids. Relative luciferase activity was cal culated as the ratio of TOPflash/FOPflash luciferase activity, and each value was normalized to the luciferase activity of the internal control pRL-TK reporter plasmid. (E) mRNA levels of <t>cyclin</t> <t>D1</t> and c-Myc in NC, MR1-C6 and MR1-D4 cells were detected by qRT-PCR and normalized to β‑actin. Bars represent the relative mRNA level when compared to the NC cells. (F) Cell lysates were analyzed by western blotting for the expression of cyclin D1 and c-Myc. β‑actin was used as a loading control. Data are expressed as the means ± SDs of 3 independent experiments. *P<0.05 compared with NC.
Mouse Monoclonal Cyclin D1 Antibody, supplied by Novocastra, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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Image Search Results


A. Illustration of less aggressive growth (Border) and distinct cell death (Inside) caused by lumbar puncture (LP) resveratrol through HE staining. B. TUNEL labeling and Cyclin D1 immunohistochemical staining performed on the tumors treated by lumbar punctured 0.3% DMSO (C) and resveratrol (Res). C, D. The incidences of TUNEL-positive and Cyclin D1-positive cells in the two experimental groups.

Journal: Oncotarget

Article Title: Lumbar puncture-administered resveratrol inhibits STAT3 activation, enhancing autophagy and apoptosis in orthotopic rat glioblastomas

doi: 10.18632/oncotarget.12414

Figure Lengend Snippet: A. Illustration of less aggressive growth (Border) and distinct cell death (Inside) caused by lumbar puncture (LP) resveratrol through HE staining. B. TUNEL labeling and Cyclin D1 immunohistochemical staining performed on the tumors treated by lumbar punctured 0.3% DMSO (C) and resveratrol (Res). C, D. The incidences of TUNEL-positive and Cyclin D1-positive cells in the two experimental groups.

Article Snippet: In parallel, immunohistochemical staining was performed adjacent sections using a mouse anti-Cyclin D1 antibody (1:80; DAKO, Glostrup, Denmark) to evaluate tumor proliferation [ ].

Techniques: Staining, TUNEL Assay, Labeling, Immunohistochemical staining

Figure 3. Knockdown of MUC1 expression alters the β‑catenin signaling pathway by blocking β‑catenin translocation to the nucleus. (A) Cell lysates from NC and MR1-D4 clones were subjected to immunoprecipitation (IP) with anti-MUC1-CT antibody or normal IgG and then immunoblotted (IB) with anti‑β‑catenin antibody. Whole cell lysate (WCL) was not subjected to immunoprecipitation. (B) Cytoplasmic extracts from SMMC-7721, NC, MR1-C6 and MR1-D4 cells were analyzed by western blotting for the expression of β‑catenin. Cytoplasmic IκBα was used as a protein loading control. (C) Nuclear extracts from SMMC‑7721, NC, MR1-C6 and MR1-D4 cells were detected by western blotting to assess the levels of nuclear β‑catenin. Lamin B1 served as the nuclear loading control. (D) NC, MR1-C6 and MR1-D4 cells were transiently transfected with TOPflash and FOPflash plasmids. Relative luciferase activity was cal culated as the ratio of TOPflash/FOPflash luciferase activity, and each value was normalized to the luciferase activity of the internal control pRL-TK reporter plasmid. (E) mRNA levels of cyclin D1 and c-Myc in NC, MR1-C6 and MR1-D4 cells were detected by qRT-PCR and normalized to β‑actin. Bars represent the relative mRNA level when compared to the NC cells. (F) Cell lysates were analyzed by western blotting for the expression of cyclin D1 and c-Myc. β‑actin was used as a loading control. Data are expressed as the means ± SDs of 3 independent experiments. *P<0.05 compared with NC.

Journal: Oncology reports

Article Title: Impact of Mucin1 knockdown on the phenotypic characteristics of the human hepatocellular carcinoma cell line SMMC-7721.

doi: 10.3892/or.2014.3136

Figure Lengend Snippet: Figure 3. Knockdown of MUC1 expression alters the β‑catenin signaling pathway by blocking β‑catenin translocation to the nucleus. (A) Cell lysates from NC and MR1-D4 clones were subjected to immunoprecipitation (IP) with anti-MUC1-CT antibody or normal IgG and then immunoblotted (IB) with anti‑β‑catenin antibody. Whole cell lysate (WCL) was not subjected to immunoprecipitation. (B) Cytoplasmic extracts from SMMC-7721, NC, MR1-C6 and MR1-D4 cells were analyzed by western blotting for the expression of β‑catenin. Cytoplasmic IκBα was used as a protein loading control. (C) Nuclear extracts from SMMC‑7721, NC, MR1-C6 and MR1-D4 cells were detected by western blotting to assess the levels of nuclear β‑catenin. Lamin B1 served as the nuclear loading control. (D) NC, MR1-C6 and MR1-D4 cells were transiently transfected with TOPflash and FOPflash plasmids. Relative luciferase activity was cal culated as the ratio of TOPflash/FOPflash luciferase activity, and each value was normalized to the luciferase activity of the internal control pRL-TK reporter plasmid. (E) mRNA levels of cyclin D1 and c-Myc in NC, MR1-C6 and MR1-D4 cells were detected by qRT-PCR and normalized to β‑actin. Bars represent the relative mRNA level when compared to the NC cells. (F) Cell lysates were analyzed by western blotting for the expression of cyclin D1 and c-Myc. β‑actin was used as a loading control. Data are expressed as the means ± SDs of 3 independent experiments. *P<0.05 compared with NC.

Article Snippet: The primary antibodies used were antibodies against MUC1 (GP1.4) (1:2,000; NeoMarkers), c-Myc (1:1,000), cyclin D1 (1:1,000), β-actin (1:2,000), IκBα (1:2,000) and Lamin B1 (1:2,000; all from Epitomics, Burlingame, CA, USA), β-catenin (1:1,000; BD Biosciences), E-cadherin (Proteintech), caspase-3 (Santa Cruz Biotechnology).

Techniques: Knockdown, Expressing, Blocking Assay, Translocation Assay, Clone Assay, Immunoprecipitation, Western Blot, Control, Transfection, Luciferase, Activity Assay, Plasmid Preparation, Quantitative RT-PCR