ccnd1 60186 1 ig proteintech mouse Search Results


anti cyclin d1  (Cell Signaling Technology Inc)
93
Cell Signaling Technology Inc anti cyclin d1
Anti Cyclin D1, supplied by Cell Signaling Technology Inc, 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/anti cyclin d1/product/Cell Signaling Technology Inc
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cyclind1 26939 1 ap proteintech 34 kda  (Proteintech)
96
Proteintech cyclind1 26939 1 ap proteintech 34 kda
Cyclind1 26939 1 Ap Proteintech 34 Kda, 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
https://www.bioz.com/result/cyclind1 26939 1 ap proteintech 34 kda/product/Proteintech
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cyclind1 26939 1 ap proteintech 34 kda - by Bioz Stars, 2026-02
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cyclin d1  (Proteintech)
96
Proteintech cyclin d1
Western blot analysis was utilized to assess the expression levels of NUCB2, E-cadherin, N-cadherin, VEGF, and <t>cyclin</t> <t>D1</t> in GBM8401 and U87-MG cells across four distinct groups: the control group, the negative control group, the si-NUCB2#1 group, and the si-NUCB2#2 group *** p < 0.001 compared with control group.
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
https://www.bioz.com/result/cyclin d1/product/Proteintech
Average 96 stars, based on 1 article reviews
cyclin d1 - by Bioz Stars, 2026-02
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ccnd1  (Proteintech)
96
Proteintech ccnd1
Xenograft mouse model to support the oncogenic role of CORO6 in ccRCC development. (A–C) CORO6 depletion suppressed ccRCC tumor growth monitored by tumor size (A) , growth curve (B) , and tumor weight (C) . (D) The mRNA levels of c-Myc, AXIN2, and <t>CCND1</t> were remarkably reduced in CORO6-depleted ccRCC tumors. The expression levels of detected genes were normalized to 18s rRNA. (E) Western blotting showed that the protein levels of c-Myc, AXIN2, and CCND1 were remarkably reduced in CORO6-depleted ccRCC tumors. GAPDH was used as the internal control. (F–H) CORO6-promoted ccRCC tumor growth was inhibited by the administration of IWP-O1 monitored by tumor size (F) , growth curve (G) , and tumor weight (H) . ** P < 0.01, *** P < 0.001, and **** P < 0.0001. Compared with CORO6 OE, ### p < 0.001 and #### p < 0.0001.
Ccnd1, 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
https://www.bioz.com/result/ccnd1/product/Proteintech
Average 96 stars, based on 1 article reviews
ccnd1 - by Bioz Stars, 2026-02
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anti cyclin d1  (Proteintech)
96
Proteintech anti cyclin d1
Xenograft mouse model to support the oncogenic role of CORO6 in ccRCC development. (A–C) CORO6 depletion suppressed ccRCC tumor growth monitored by tumor size (A) , growth curve (B) , and tumor weight (C) . (D) The mRNA levels of c-Myc, AXIN2, and <t>CCND1</t> were remarkably reduced in CORO6-depleted ccRCC tumors. The expression levels of detected genes were normalized to 18s rRNA. (E) Western blotting showed that the protein levels of c-Myc, AXIN2, and CCND1 were remarkably reduced in CORO6-depleted ccRCC tumors. GAPDH was used as the internal control. (F–H) CORO6-promoted ccRCC tumor growth was inhibited by the administration of IWP-O1 monitored by tumor size (F) , growth curve (G) , and tumor weight (H) . ** P < 0.01, *** P < 0.001, and **** P < 0.0001. Compared with CORO6 OE, ### p < 0.001 and #### p < 0.0001.
Anti 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
https://www.bioz.com/result/anti cyclin d1/product/Proteintech
Average 96 stars, based on 1 article reviews
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cyclin d1 rabbit polyclonal antibody  (Proteintech)
96
Proteintech cyclin d1 rabbit polyclonal antibody
Chrysin retards H1N1 influenza virus-induced G0/G1 cell cycle arrest in epithelial cells. (A) A549 cells were infected with A/PR/8/34 (H1N1) virus (MOI = 0.5) in the presence or absence of chrysin for 2 hours, then the supernatant was removed and supplemented by fresh medium containing 8 μM chrysin for 10 hours stimulation. Cycle distribution was assessed using flow cytometry. (B) statistical charts of the cell population in G0/G1, S, and G2/M phases. (C) A549 cells were infected with A/PR/8/34 (H1N1) virus (MOI = 0.5) for 2 hours in the presence or absence of 8 μM chrysin, then the supernatant was discarded, and fresh medium containing 8 μM chrysin was added for 10 hours of treatment. Following that, the extracted protein was subjected to western blotting to determine the amounts of P53, P21, <t>Cyclin</t> <t>D1,</t> CDK4, CDK6, Cyclin E1, and CDK2. (D) Statistical analysis of the protein expression levels of P53, P21, Cyclin D1, CDK4, CDK6, Cyclin E1, and CDK2 in A549 cells. Protein loading was normalized based on β-actin and shown as a regular value. Data are expressed as the mean ± SEM. All data are representative of three independent experiments. *P < 0.05, **P < 0.01 by unpaired two-tailed Student’s t-test. ns, no significant difference.
Cyclin D1 Rabbit Polyclonal Antibody, 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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Average 96 stars, based on 1 article reviews
cyclin d1 rabbit polyclonal antibody - by Bioz Stars, 2026-02
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cyclin d1  (Santa Cruz Biotechnology)
95
Santa Cruz Biotechnology cyclin d1
Chrysin retards H1N1 influenza virus-induced G0/G1 cell cycle arrest in epithelial cells. (A) A549 cells were infected with A/PR/8/34 (H1N1) virus (MOI = 0.5) in the presence or absence of chrysin for 2 hours, then the supernatant was removed and supplemented by fresh medium containing 8 μM chrysin for 10 hours stimulation. Cycle distribution was assessed using flow cytometry. (B) statistical charts of the cell population in G0/G1, S, and G2/M phases. (C) A549 cells were infected with A/PR/8/34 (H1N1) virus (MOI = 0.5) for 2 hours in the presence or absence of 8 μM chrysin, then the supernatant was discarded, and fresh medium containing 8 μM chrysin was added for 10 hours of treatment. Following that, the extracted protein was subjected to western blotting to determine the amounts of P53, P21, <t>Cyclin</t> <t>D1,</t> CDK4, CDK6, Cyclin E1, and CDK2. (D) Statistical analysis of the protein expression levels of P53, P21, Cyclin D1, CDK4, CDK6, Cyclin E1, and CDK2 in A549 cells. Protein loading was normalized based on β-actin and shown as a regular value. Data are expressed as the mean ± SEM. All data are representative of three independent experiments. *P < 0.05, **P < 0.01 by unpaired two-tailed Student’s t-test. ns, no significant difference.
Cyclin D1, supplied by Santa Cruz Biotechnology, used in various techniques. Bioz Stars score: 95/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/result/cyclin d1/product/Santa Cruz Biotechnology
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Image Search Results


Western blot analysis was utilized to assess the expression levels of NUCB2, E-cadherin, N-cadherin, VEGF, and cyclin D1 in GBM8401 and U87-MG cells across four distinct groups: the control group, the negative control group, the si-NUCB2#1 group, and the si-NUCB2#2 group *** p < 0.001 compared with control group.

Journal: Cells

Article Title: Role of Nucleobindin-2 in the Clinical Pathogenesis and Treatment Resistance of Glioblastoma

doi: 10.3390/cells12192420

Figure Lengend Snippet: Western blot analysis was utilized to assess the expression levels of NUCB2, E-cadherin, N-cadherin, VEGF, and cyclin D1 in GBM8401 and U87-MG cells across four distinct groups: the control group, the negative control group, the si-NUCB2#1 group, and the si-NUCB2#2 group *** p < 0.001 compared with control group.

Article Snippet: After a 1 h incubation in blocking buffer, the membranes were then exposed to primary antibodies (NUCB2 (PAB27403; 1:500; Abnova; Taipe, Taiwan), β-actin (A5441; 1:20,000; Sigma; USA), cyclin D1 (60186-1-lg; 1:500; Proteintech; Chicago, IL, USA), E-cadherin (20874-1-AP; 1:500; Proteintech; USA), N-cadherin (22018-1-AP; 1:500; Proteintech; USA), vascular endothelial growth factor (VEGF) (AP6290b; 1:500; ABGENT; San Diego, CA, USA), ku70 (sc-17789; 1:500; SANTA CRUZ; Santa Cruz, CA, USA, Europe), ku80 (ARG57867; 1:1000; Arigo; Hsinchu, Taiwan), Rad51 (GTX70230; 1:2000; GeneTex; Irvine, CA, USA), Rad52 (sc-365341; 1:500; SANTA CRUZ; Europe), cleaved caspase-3 (#9664; 1:500; Cell Signaling; Beverly, MA, USA), and poly (ADP-ribose) polymerases (PARP) (#9542; 1:500; Cell Signaling; USA)) for 16 h at 4 °C.

Techniques: Western Blot, Expressing, Control, Negative Control

Xenograft mouse model to support the oncogenic role of CORO6 in ccRCC development. (A–C) CORO6 depletion suppressed ccRCC tumor growth monitored by tumor size (A) , growth curve (B) , and tumor weight (C) . (D) The mRNA levels of c-Myc, AXIN2, and CCND1 were remarkably reduced in CORO6-depleted ccRCC tumors. The expression levels of detected genes were normalized to 18s rRNA. (E) Western blotting showed that the protein levels of c-Myc, AXIN2, and CCND1 were remarkably reduced in CORO6-depleted ccRCC tumors. GAPDH was used as the internal control. (F–H) CORO6-promoted ccRCC tumor growth was inhibited by the administration of IWP-O1 monitored by tumor size (F) , growth curve (G) , and tumor weight (H) . ** P < 0.01, *** P < 0.001, and **** P < 0.0001. Compared with CORO6 OE, ### p < 0.001 and #### p < 0.0001.

Journal: Frontiers in Cell and Developmental Biology

Article Title: CORO6 Promotes Cell Growth and Invasion of Clear Cell Renal Cell Carcinoma via Activation of WNT Signaling

doi: 10.3389/fcell.2021.647301

Figure Lengend Snippet: Xenograft mouse model to support the oncogenic role of CORO6 in ccRCC development. (A–C) CORO6 depletion suppressed ccRCC tumor growth monitored by tumor size (A) , growth curve (B) , and tumor weight (C) . (D) The mRNA levels of c-Myc, AXIN2, and CCND1 were remarkably reduced in CORO6-depleted ccRCC tumors. The expression levels of detected genes were normalized to 18s rRNA. (E) Western blotting showed that the protein levels of c-Myc, AXIN2, and CCND1 were remarkably reduced in CORO6-depleted ccRCC tumors. GAPDH was used as the internal control. (F–H) CORO6-promoted ccRCC tumor growth was inhibited by the administration of IWP-O1 monitored by tumor size (F) , growth curve (G) , and tumor weight (H) . ** P < 0.01, *** P < 0.001, and **** P < 0.0001. Compared with CORO6 OE, ### p < 0.001 and #### p < 0.0001.

Article Snippet: The antibodies used in this study were as follows: c-Myc (10828-1-AP; Proteintech, Rosemont, IL, USA), CORO6 (17243-1-AP; Proteintech), CCND1 (60186-1-lg; Proteintech), GAPDH (60004-lg; Proteintech), and AXIN2 (ab109307; Abcam, Cambridge, UK).

Techniques: Expressing, Western Blot, Control

Chrysin retards H1N1 influenza virus-induced G0/G1 cell cycle arrest in epithelial cells. (A) A549 cells were infected with A/PR/8/34 (H1N1) virus (MOI = 0.5) in the presence or absence of chrysin for 2 hours, then the supernatant was removed and supplemented by fresh medium containing 8 μM chrysin for 10 hours stimulation. Cycle distribution was assessed using flow cytometry. (B) statistical charts of the cell population in G0/G1, S, and G2/M phases. (C) A549 cells were infected with A/PR/8/34 (H1N1) virus (MOI = 0.5) for 2 hours in the presence or absence of 8 μM chrysin, then the supernatant was discarded, and fresh medium containing 8 μM chrysin was added for 10 hours of treatment. Following that, the extracted protein was subjected to western blotting to determine the amounts of P53, P21, Cyclin D1, CDK4, CDK6, Cyclin E1, and CDK2. (D) Statistical analysis of the protein expression levels of P53, P21, Cyclin D1, CDK4, CDK6, Cyclin E1, and CDK2 in A549 cells. Protein loading was normalized based on β-actin and shown as a regular value. Data are expressed as the mean ± SEM. All data are representative of three independent experiments. *P < 0.05, **P < 0.01 by unpaired two-tailed Student’s t-test. ns, no significant difference.

Journal: Frontiers in Immunology

Article Title: Chrysin Ameliorates Influenza Virus Infection in the Upper Airways by Repressing Virus-Induced Cell Cycle Arrest and Mitochondria-Dependent Apoptosis

doi: 10.3389/fimmu.2022.872958

Figure Lengend Snippet: Chrysin retards H1N1 influenza virus-induced G0/G1 cell cycle arrest in epithelial cells. (A) A549 cells were infected with A/PR/8/34 (H1N1) virus (MOI = 0.5) in the presence or absence of chrysin for 2 hours, then the supernatant was removed and supplemented by fresh medium containing 8 μM chrysin for 10 hours stimulation. Cycle distribution was assessed using flow cytometry. (B) statistical charts of the cell population in G0/G1, S, and G2/M phases. (C) A549 cells were infected with A/PR/8/34 (H1N1) virus (MOI = 0.5) for 2 hours in the presence or absence of 8 μM chrysin, then the supernatant was discarded, and fresh medium containing 8 μM chrysin was added for 10 hours of treatment. Following that, the extracted protein was subjected to western blotting to determine the amounts of P53, P21, Cyclin D1, CDK4, CDK6, Cyclin E1, and CDK2. (D) Statistical analysis of the protein expression levels of P53, P21, Cyclin D1, CDK4, CDK6, Cyclin E1, and CDK2 in A549 cells. Protein loading was normalized based on β-actin and shown as a regular value. Data are expressed as the mean ± SEM. All data are representative of three independent experiments. *P < 0.05, **P < 0.01 by unpaired two-tailed Student’s t-test. ns, no significant difference.

Article Snippet: Then on-specific binding was blocked with 5% skimmed milk (BioFroxx, 1172GR500), and it was incubated with primary antibodies against P53 Polyclonal antibody, P21 Rabbit Polyclonal antibody (Proteintech, 10355-1-AP), Cyclin D1 Rabbit Polyclonal antibody (Proteintech, 60186-1-lg), CDK4 Polyclonal antibody (Proteintech, 11026-1-AP), CDK6 Polyclonal antibody (Proteintech, 14052-1-AP), Cyclin E1 Rabbit Polyclonal antibody (Proteintech, 11554-1-AP), CDK2 Polyclonal antibody (Proteintech, 10122-1-AP), Bax antibody (Cell signaling technology, 2772), Bcl-xl rabbit polyclonal antibody (Proteintech, 26967-1-AP), Caspase 3 antibody (Cell signaling technology, 9662), Caspase 9 polyclonal antibody (Proteintech, 10380-1-AP), H1N1 NP Monoclonal Antibody (Thermo Fisher, GT1236), H1N1 HA Polyclonal Antibody (Thermo Fisher, PA5-34929), β-actin antibody (Abcam, ab8226) overnight at 4°C.

Techniques: Virus, Infection, Flow Cytometry, Western Blot, Expressing, Two Tailed Test

A schematic diagram of the role of chrysin in suppressing influenza virus infection by blocking G0/G1 cell cycle arrest and the mitochondrial apoptosis pathway. Chrysin restrains influenza virus infection by disrupting ROS-mediated dual signaling pathways, including the suppression of p53 and p21, which promotes the activation of CDK4, Cyclin D1, and Cyclin E1, culminating in the prevention of cell cycle arrest at the G0/G1 phase. Alternatively, chrysin can reduce ROS-mediated Bax while increasing Bcl-xl, which in turn blocks mitochondrial apoptosis by inhibiting cleaved-caspase 9 and cleaved-caspase 3.

Journal: Frontiers in Immunology

Article Title: Chrysin Ameliorates Influenza Virus Infection in the Upper Airways by Repressing Virus-Induced Cell Cycle Arrest and Mitochondria-Dependent Apoptosis

doi: 10.3389/fimmu.2022.872958

Figure Lengend Snippet: A schematic diagram of the role of chrysin in suppressing influenza virus infection by blocking G0/G1 cell cycle arrest and the mitochondrial apoptosis pathway. Chrysin restrains influenza virus infection by disrupting ROS-mediated dual signaling pathways, including the suppression of p53 and p21, which promotes the activation of CDK4, Cyclin D1, and Cyclin E1, culminating in the prevention of cell cycle arrest at the G0/G1 phase. Alternatively, chrysin can reduce ROS-mediated Bax while increasing Bcl-xl, which in turn blocks mitochondrial apoptosis by inhibiting cleaved-caspase 9 and cleaved-caspase 3.

Article Snippet: Then on-specific binding was blocked with 5% skimmed milk (BioFroxx, 1172GR500), and it was incubated with primary antibodies against P53 Polyclonal antibody, P21 Rabbit Polyclonal antibody (Proteintech, 10355-1-AP), Cyclin D1 Rabbit Polyclonal antibody (Proteintech, 60186-1-lg), CDK4 Polyclonal antibody (Proteintech, 11026-1-AP), CDK6 Polyclonal antibody (Proteintech, 14052-1-AP), Cyclin E1 Rabbit Polyclonal antibody (Proteintech, 11554-1-AP), CDK2 Polyclonal antibody (Proteintech, 10122-1-AP), Bax antibody (Cell signaling technology, 2772), Bcl-xl rabbit polyclonal antibody (Proteintech, 26967-1-AP), Caspase 3 antibody (Cell signaling technology, 9662), Caspase 9 polyclonal antibody (Proteintech, 10380-1-AP), H1N1 NP Monoclonal Antibody (Thermo Fisher, GT1236), H1N1 HA Polyclonal Antibody (Thermo Fisher, PA5-34929), β-actin antibody (Abcam, ab8226) overnight at 4°C.

Techniques: Virus, Infection, Blocking Assay, Protein-Protein interactions, Activation Assay