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mouse antibodies against rrm2 (Santa Cruz Biotechnology)

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Santa Cruz Biotechnology mouse antibodies against rrm2
Mouse Antibodies Against Rrm2, supplied by Santa Cruz Biotechnology, used in various techniques. Bioz Stars score: 91/100, based on 8 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/product/mouse+antibodies+against+rrm2/pmc06858455-279-0-31?v=Santa+Cruz+Biotechnology
Average 91 stars, based on 8 article reviews

mouse antibodies against rrm2 - by Bioz Stars, 2026-08

91/100 stars

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RRM2 is upregulated in ccRCC and predicts poor prognosis. (A) The mRNA level of RRM2 in tissues from 10 cases of ccRCC and the corresponding normal renal tissues was examined using RT-qPCR analysis. ** P <0.01. (B) IHC staining was performed in 90 cases of ccRCC tissues and 30 cases of normal renal tissues. The representative images of RRM2 expression in the cell cytoplasm are shown (×400). The scale bar represents 50 µm. (C) The IHC score of RRM2 in the above samples. ** P <0.01. (D) Survival analysis of RCC patients related to RRM2 expression was analyzed by Kaplan–Meier survival curves. Abbreviations: ccRCC, clear-cell renal cell carcinoma; IHC, immunohistochemistry; RRM2, ribonucleotide reductase subunit M2.

Journal: OncoTargets and therapy

Article Title: Ribonucleotide reductase subunit M2 as a novel target for clear-cell renal cell carcinoma

doi: 10.2147/OTT.S196347

Figure Lengend Snippet: RRM2 is upregulated in ccRCC and predicts poor prognosis. (A) The mRNA level of RRM2 in tissues from 10 cases of ccRCC and the corresponding normal renal tissues was examined using RT-qPCR analysis. ** P <0.01. (B) IHC staining was performed in 90 cases of ccRCC tissues and 30 cases of normal renal tissues. The representative images of RRM2 expression in the cell cytoplasm are shown (×400). The scale bar represents 50 µm. (C) The IHC score of RRM2 in the above samples. ** P <0.01. (D) Survival analysis of RCC patients related to RRM2 expression was analyzed by Kaplan–Meier survival curves. Abbreviations: ccRCC, clear-cell renal cell carcinoma; IHC, immunohistochemistry; RRM2, ribonucleotide reductase subunit M2.

Article Snippet: 16 Briefly, the proteins of the cells on the membrane were incubated with a primary mouse monoclonal antibody against human RRM2 (1:1000 dilution; ab57653; Abcam) at 4 °C overnight.

Techniques: Quantitative RT-PCR, Immunohistochemistry, Expressing

Expression of RRM2 in ccRCC and normal tissues

Journal: OncoTargets and therapy

Article Title: Ribonucleotide reductase subunit M2 as a novel target for clear-cell renal cell carcinoma

doi: 10.2147/OTT.S196347

Figure Lengend Snippet: Expression of RRM2 in ccRCC and normal tissues

Techniques: Expressing

Association of RRM2 expression with clinicopathologic characteristics in ccRCC

Journal: OncoTargets and therapy

Article Title: Ribonucleotide reductase subunit M2 as a novel target for clear-cell renal cell carcinoma

doi: 10.2147/OTT.S196347

Figure Lengend Snippet: Association of RRM2 expression with clinicopathologic characteristics in ccRCC

Techniques: Expressing

Univariate and multivariate Cox regression analysis for overall survival in ccRCC

Journal: OncoTargets and therapy

Article Title: Ribonucleotide reductase subunit M2 as a novel target for clear-cell renal cell carcinoma

doi: 10.2147/OTT.S196347

Figure Lengend Snippet: Univariate and multivariate Cox regression analysis for overall survival in ccRCC

Techniques: Expressing

Knockdown of RRM2 inhibits the proliferation and induces G0/G1 arrest in RCC cells through attenuation of the dNTP pool. (A) Western blotting showed that knockdown of RRM2 using siRNAs could effectively decrease the protein expression of RRM2 in 786-O and 769-P cells. (B) The proliferation assay showed that the viability of 786-O and 769-P cells was significantly decreased by the knockdown of RRM2. * P <0.05; *** P <0.001. (C) Flow cytometry showed that the knockdown of RRM2 induced G0/G1 arrest in 786-O and 769-P cells. *** P <0.001. (D) LC-MS/MS analysis showed that the knockdown of RRM2 significantly decreased the dNTP pool, individually dATP and dGTP, in 786-O and 769-P cells. *** P <0.001. Abbreviations: NC, negative control; RRM2, ribonucleotide reductase subunit M2.

Journal: OncoTargets and therapy

Article Title: Ribonucleotide reductase subunit M2 as a novel target for clear-cell renal cell carcinoma

doi: 10.2147/OTT.S196347

Figure Lengend Snippet: Knockdown of RRM2 inhibits the proliferation and induces G0/G1 arrest in RCC cells through attenuation of the dNTP pool. (A) Western blotting showed that knockdown of RRM2 using siRNAs could effectively decrease the protein expression of RRM2 in 786-O and 769-P cells. (B) The proliferation assay showed that the viability of 786-O and 769-P cells was significantly decreased by the knockdown of RRM2. * P <0.05; *** P <0.001. (C) Flow cytometry showed that the knockdown of RRM2 induced G0/G1 arrest in 786-O and 769-P cells. *** P <0.001. (D) LC-MS/MS analysis showed that the knockdown of RRM2 significantly decreased the dNTP pool, individually dATP and dGTP, in 786-O and 769-P cells. *** P <0.001. Abbreviations: NC, negative control; RRM2, ribonucleotide reductase subunit M2.

Techniques: Knockdown, Western Blot, Expressing, Proliferation Assay, Flow Cytometry, Liquid Chromatography with Mass Spectroscopy, Negative Control

RRM2 inhibitor reduces the viability of RCC cells by inducing the G0/G1 arrest. (A) 786-O and 769-P cells were treated with 0.5, 1, or 2 μM Triapine for 24, 48, and 72 hours respectively. The cell viability was assessed by CCK-8 assay. (B) 786-O and 769-P cells were treated with 0.5, 1, or 2 μM Triapine respectively, for 48 hours. The cell cycle distribution was detected by PI staining and shown in the bar graph as percentages of cells. Error bars represent the mean ± SD of three independent experiments. *** P <0.001. (C) 786-O and 769-P cells were treated with 0.5, 1, or 2 μM Triapine, respectively, for 72 hours. Apoptotic cells were detected by PI/Annexin V dual staining and shown in the bar graph as percentages of cells. Error bars represent mean ± SD of three independent experiments. Abbreviations: n.s., not significant; PI, propidium iodide; RCC, renal cell carcinoma; RRM2, ribonucleotide reductase subunit M2.

Journal: OncoTargets and therapy

Article Title: Ribonucleotide reductase subunit M2 as a novel target for clear-cell renal cell carcinoma

doi: 10.2147/OTT.S196347

Figure Lengend Snippet: RRM2 inhibitor reduces the viability of RCC cells by inducing the G0/G1 arrest. (A) 786-O and 769-P cells were treated with 0.5, 1, or 2 μM Triapine for 24, 48, and 72 hours respectively. The cell viability was assessed by CCK-8 assay. (B) 786-O and 769-P cells were treated with 0.5, 1, or 2 μM Triapine respectively, for 48 hours. The cell cycle distribution was detected by PI staining and shown in the bar graph as percentages of cells. Error bars represent the mean ± SD of three independent experiments. *** P <0.001. (C) 786-O and 769-P cells were treated with 0.5, 1, or 2 μM Triapine, respectively, for 72 hours. Apoptotic cells were detected by PI/Annexin V dual staining and shown in the bar graph as percentages of cells. Error bars represent mean ± SD of three independent experiments. Abbreviations: n.s., not significant; PI, propidium iodide; RCC, renal cell carcinoma; RRM2, ribonucleotide reductase subunit M2.

Techniques: CCK-8 Assay, Staining

Overexpression of RRM2 decreased TSP-1 expression in KB-M2-D and KB-HURs cells . (A) Western blot analysis confirmed that only RRM2 was overexpressed in KB-M2-D and KB-HURs; the expression of RRM1 and p53R2 was not significantly modulated in both KB-M2-D and KB-HURs; and the expression of TSP-1 was significantly decreased in KB-M2-D and KB-HURs cells by 60%~70% (TSP1-CM: TSP-1 in concentrated condition medium, TSP1-T: TSP-1 in total protein). (B) Representative quantitative densitometric analysis of RRM2 and TSP-1 expression. Signal intensities were normalized to that of β-actin serving as loading control; data was presented as fold of KB. (C) q-RT-PCR analysis confirmed that RRM2 mRNA was dramatically overexpressed in KB-M2D and KB-HURs compared with parental KB (** p < 0.01). Values of q-RT-PCR were the mean ± SD of three independent experiments and presented as ratio to the level of parental KB cells. (D) q-RT-PCR analysis showed TSP-1 mRNA was significantly decreased in KB-M2D and KB-HURs compared with parental KB (** p < 0.01).

Journal: Molecular Cancer

Article Title: Overexpression of RRM2 decreases thrombspondin-1 and increases VEGF production in human cancer cells in vitro and in vivo : implication of RRM2 in angiogenesis

doi: 10.1186/1476-4598-8-11

Figure Lengend Snippet: Overexpression of RRM2 decreased TSP-1 expression in KB-M2-D and KB-HURs cells . (A) Western blot analysis confirmed that only RRM2 was overexpressed in KB-M2-D and KB-HURs; the expression of RRM1 and p53R2 was not significantly modulated in both KB-M2-D and KB-HURs; and the expression of TSP-1 was significantly decreased in KB-M2-D and KB-HURs cells by 60%~70% (TSP1-CM: TSP-1 in concentrated condition medium, TSP1-T: TSP-1 in total protein). (B) Representative quantitative densitometric analysis of RRM2 and TSP-1 expression. Signal intensities were normalized to that of β-actin serving as loading control; data was presented as fold of KB. (C) q-RT-PCR analysis confirmed that RRM2 mRNA was dramatically overexpressed in KB-M2D and KB-HURs compared with parental KB (** p < 0.01). Values of q-RT-PCR were the mean ± SD of three independent experiments and presented as ratio to the level of parental KB cells. (D) q-RT-PCR analysis showed TSP-1 mRNA was significantly decreased in KB-M2D and KB-HURs compared with parental KB (** p < 0.01).

Article Snippet: The mouse monoclonal antibodies against Beta-Actin, RRM2, were obtained from Santa Cruz Biotechnology (Santa Cruz, CA).

Techniques: Over Expression, Expressing, Western Blot, Control, Reverse Transcription Polymerase Chain Reaction

Overexpression of RRM2 increased VEGF expression in KB-M2-D and KB-HURs cells . (A) VEGF in condition mediums of KB-M2-D and Kb-HURs were increased by 2.4-fold and 2.1-fold respectively. Levels of VEGF in the condition medium were measured with ELISA. Data, presented as ng of VEGF protein/ml of medium and per mg of total protein, was the mean ± SD of 2–3 preparation. (B) q-RT-PCR analysis showed that VEGF mRNA was increased in KB-M2D and KB-HURs by 3~4 fold compared with parental KB and KB-V cells. (C) Compared with KB-V, KB-M2-D secreted more VEGF under both normoxia and hypoxia. (D) q-RT-PCR analysis showed KB-M2D expressed more VEGF mRNA than KB-V under both normoxia and hypoxia, * p < 0.05, ** p < 0.01 compared with KB-V.

Journal: Molecular Cancer

Article Title: Overexpression of RRM2 decreases thrombspondin-1 and increases VEGF production in human cancer cells in vitro and in vivo : implication of RRM2 in angiogenesis

doi: 10.1186/1476-4598-8-11

Figure Lengend Snippet: Overexpression of RRM2 increased VEGF expression in KB-M2-D and KB-HURs cells . (A) VEGF in condition mediums of KB-M2-D and Kb-HURs were increased by 2.4-fold and 2.1-fold respectively. Levels of VEGF in the condition medium were measured with ELISA. Data, presented as ng of VEGF protein/ml of medium and per mg of total protein, was the mean ± SD of 2–3 preparation. (B) q-RT-PCR analysis showed that VEGF mRNA was increased in KB-M2D and KB-HURs by 3~4 fold compared with parental KB and KB-V cells. (C) Compared with KB-V, KB-M2-D secreted more VEGF under both normoxia and hypoxia. (D) q-RT-PCR analysis showed KB-M2D expressed more VEGF mRNA than KB-V under both normoxia and hypoxia, * p < 0.05, ** p < 0.01 compared with KB-V.

Article Snippet: The mouse monoclonal antibodies against Beta-Actin, RRM2, were obtained from Santa Cruz Biotechnology (Santa Cruz, CA).

Techniques: Over Expression, Expressing, Enzyme-linked Immunosorbent Assay, Reverse Transcription Polymerase Chain Reaction

Knockdown of RRM2 increased TSP-1 and decreased VEGF expression in KB cells . (A) q-RT-PCR analysis showed that RRM2 mRNA was decreased by ~80%, and TSP-1 mRNA was increased by ~5 folds in KB cells at 48 h post-transfection with RRM2 siRNA. (B) Western blot analysis showed that TSP-1 protein was significantly increased by ~2.6-fold (KB-W: KB cell, Sc-siR: scramble siRNA transfected KB, R2-siR: RRM2 siRNA transfected KB). (C) q-RT-PCR analysis confirmed RRM2 mRNA was significantly decreased in KB cells at 48 h post-transfection under both normoxia and hypoxia. (D) q-RT-PCR analysis showed VEGF mRNA in KB cells was decreased after RRM2 knockdown under both normoxia and hypoxia. (E) VEGF in condition medium of KB was significantly decreased after RRM2 knockdown under both normoxia and hypoxia. Data was presented as the mean ± SD of 2–3 independent experiments, * p < 0.05, ** p < 0.01, compared with scramble siRNA transfected.

Journal: Molecular Cancer

Article Title: Overexpression of RRM2 decreases thrombspondin-1 and increases VEGF production in human cancer cells in vitro and in vivo : implication of RRM2 in angiogenesis

doi: 10.1186/1476-4598-8-11

Figure Lengend Snippet: Knockdown of RRM2 increased TSP-1 and decreased VEGF expression in KB cells . (A) q-RT-PCR analysis showed that RRM2 mRNA was decreased by ~80%, and TSP-1 mRNA was increased by ~5 folds in KB cells at 48 h post-transfection with RRM2 siRNA. (B) Western blot analysis showed that TSP-1 protein was significantly increased by ~2.6-fold (KB-W: KB cell, Sc-siR: scramble siRNA transfected KB, R2-siR: RRM2 siRNA transfected KB). (C) q-RT-PCR analysis confirmed RRM2 mRNA was significantly decreased in KB cells at 48 h post-transfection under both normoxia and hypoxia. (D) q-RT-PCR analysis showed VEGF mRNA in KB cells was decreased after RRM2 knockdown under both normoxia and hypoxia. (E) VEGF in condition medium of KB was significantly decreased after RRM2 knockdown under both normoxia and hypoxia. Data was presented as the mean ± SD of 2–3 independent experiments, * p < 0.05, ** p < 0.01, compared with scramble siRNA transfected.

Article Snippet: The mouse monoclonal antibodies against Beta-Actin, RRM2, were obtained from Santa Cruz Biotechnology (Santa Cruz, CA).

Techniques: Knockdown, Expressing, Reverse Transcription Polymerase Chain Reaction, Transfection, Western Blot

Knockdown of RRM2 increased TSP-1 and decreased VEGF expression in LNCaP Cells . (A) q-RT-PCR analysis confirmed that RRM2 mRNA decreased by ~80%, and TSP-1 mRNA increased by ~8 folds in LNCaP cells at 48 h post-transfection with RRM2 siRNA. (B) Western blot analysis showed that TSP-1 protein was significantly increased by ~3.4-fold (Ln-Wt: LNCaP cell, Sc-siR: scramble siRNA transfected LNCaP, R2-siR: RRM2 siRNA transfected LNCaP). (C) q-RT-PCR analysis confirmed that RRM2 mRNA was significantly decreased in LNCaP at 48 h post-transfection under both normoxia and hypoxia. (D) q-RT-PCR analysis showed VEGF mRNA in LNCaP cells was decreased after RRM2 knockdown under both normoxia and hypoxia. (E) VEGF in condition medium of LNCaP was significantly decreased after RRM2 knockdown under both normoxia and hypoxia. Data was presented as the mean ± SD of 2–3 independent experiments, * p < 0.05, ** p < 0.01, compared with scramble siRNA transefected.

Journal: Molecular Cancer

Article Title: Overexpression of RRM2 decreases thrombspondin-1 and increases VEGF production in human cancer cells in vitro and in vivo : implication of RRM2 in angiogenesis

doi: 10.1186/1476-4598-8-11

Figure Lengend Snippet: Knockdown of RRM2 increased TSP-1 and decreased VEGF expression in LNCaP Cells . (A) q-RT-PCR analysis confirmed that RRM2 mRNA decreased by ~80%, and TSP-1 mRNA increased by ~8 folds in LNCaP cells at 48 h post-transfection with RRM2 siRNA. (B) Western blot analysis showed that TSP-1 protein was significantly increased by ~3.4-fold (Ln-Wt: LNCaP cell, Sc-siR: scramble siRNA transfected LNCaP, R2-siR: RRM2 siRNA transfected LNCaP). (C) q-RT-PCR analysis confirmed that RRM2 mRNA was significantly decreased in LNCaP at 48 h post-transfection under both normoxia and hypoxia. (D) q-RT-PCR analysis showed VEGF mRNA in LNCaP cells was decreased after RRM2 knockdown under both normoxia and hypoxia. (E) VEGF in condition medium of LNCaP was significantly decreased after RRM2 knockdown under both normoxia and hypoxia. Data was presented as the mean ± SD of 2–3 independent experiments, * p < 0.05, ** p < 0.01, compared with scramble siRNA transefected.

Article Snippet: The mouse monoclonal antibodies against Beta-Actin, RRM2, were obtained from Santa Cruz Biotechnology (Santa Cruz, CA).

Techniques: Knockdown, Expressing, Reverse Transcription Polymerase Chain Reaction, Transfection, Western Blot

Overexpression of RRM2 promoted the growth of KB-M2-D in vivo . (A) Typical RT-CES traces described that KB and KB-M2-D proliferated in an equal rate. CI was recorded every half hour. Each trace for each cell was an average of 4 replicates. (B) Tumor growth curves showed that RRM2 significantly promoted KB-M2-D in vivo growth. (C) Overexpression of RRM2 increased tumor xenografts size of KB-M2-D at the end of experiment. (D) q-RT-PCR analysis confirmed that RRM2, VEGF and TSP-1 mRNA was significantly different in KB-V and KB-M2 xenografts. * p < 0.05; ** p < 0.01, compared with Kb-V. Data expressed was the mean ± SD of 12 mice of two independent experiments.

Journal: Molecular Cancer

Article Title: Overexpression of RRM2 decreases thrombspondin-1 and increases VEGF production in human cancer cells in vitro and in vivo : implication of RRM2 in angiogenesis

doi: 10.1186/1476-4598-8-11

Figure Lengend Snippet: Overexpression of RRM2 promoted the growth of KB-M2-D in vivo . (A) Typical RT-CES traces described that KB and KB-M2-D proliferated in an equal rate. CI was recorded every half hour. Each trace for each cell was an average of 4 replicates. (B) Tumor growth curves showed that RRM2 significantly promoted KB-M2-D in vivo growth. (C) Overexpression of RRM2 increased tumor xenografts size of KB-M2-D at the end of experiment. (D) q-RT-PCR analysis confirmed that RRM2, VEGF and TSP-1 mRNA was significantly different in KB-V and KB-M2 xenografts. * p < 0.05; ** p < 0.01, compared with Kb-V. Data expressed was the mean ± SD of 12 mice of two independent experiments.

Article Snippet: The mouse monoclonal antibodies against Beta-Actin, RRM2, were obtained from Santa Cruz Biotechnology (Santa Cruz, CA).

Techniques: Over Expression, In Vivo, Reverse Transcription Polymerase Chain Reaction

CD31 immunohistochemistry assay displayed that overexpression of RRM2 resulted in more vascularized tumor xenografts . Representative immunohistochemical assay of vascularization of tumor xenografts generated in vivo by (A) KB-V and (B) KB-M2-D cells (×100). (C) Semi-quantitative analysis showed that CD31 staining was significantly increased in KB-M2D tumor xenografts compared with that of KB-V, * p < 0.05. Values expressed were the mean ± SD of 8 mice of two independent experiments.

Journal: Molecular Cancer

Article Title: Overexpression of RRM2 decreases thrombspondin-1 and increases VEGF production in human cancer cells in vitro and in vivo : implication of RRM2 in angiogenesis

doi: 10.1186/1476-4598-8-11

Figure Lengend Snippet: CD31 immunohistochemistry assay displayed that overexpression of RRM2 resulted in more vascularized tumor xenografts . Representative immunohistochemical assay of vascularization of tumor xenografts generated in vivo by (A) KB-V and (B) KB-M2-D cells (×100). (C) Semi-quantitative analysis showed that CD31 staining was significantly increased in KB-M2D tumor xenografts compared with that of KB-V, * p < 0.05. Values expressed were the mean ± SD of 8 mice of two independent experiments.

Article Snippet: The mouse monoclonal antibodies against Beta-Actin, RRM2, were obtained from Santa Cruz Biotechnology (Santa Cruz, CA).

Techniques: Immunohistochemistry, Over Expression, Immunohistochemical staining, Generated, In Vivo, Staining

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