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Proteintech ruvbl2

Figure 5. Correlation between candidate genes expression and DSS in MM. (A) Kaplan–Meier survival curves comparing high and low levels of six candidate genes in MM were analyzed using the GSE2658 dataset (n = 559). Cox P < 0.05 was considered to be statistically difference. (B) Diagnostic value of TP53 in GSE13591 for MM. (C) Diagnostic value of <t>RUVBL2</t> in GSE13591 for MM. (D) Diagnostic value of MCM5 in GSE13591 for MM.

Ruvbl2, supplied by Proteintech, used in various techniques. Bioz Stars score: 93/100, based on 27 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/result/ruvbl2/product/Proteintech
Average 93 stars, based on 27 article reviews

ruvbl2 - by Bioz Stars, 2026-04

93/100 stars

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1) Product Images from "Identification of RUVBL2 as a novel biomarker to predict the prognosis and drug sensitivity in multiple myeloma based on ferroptosis genes."

Article Title: Identification of RUVBL2 as a novel biomarker to predict the prognosis and drug sensitivity in multiple myeloma based on ferroptosis genes.

Journal: Hematology (Amsterdam, Netherlands)

doi: 10.1080/16078454.2025.2467499

Figure Legend Snippet: Figure 5. Correlation between candidate genes expression and DSS in MM. (A) Kaplan–Meier survival curves comparing high and low levels of six candidate genes in MM were analyzed using the GSE2658 dataset (n = 559). Cox P < 0.05 was considered to be statistically difference. (B) Diagnostic value of TP53 in GSE13591 for MM. (C) Diagnostic value of RUVBL2 in GSE13591 for MM. (D) Diagnostic value of MCM5 in GSE13591 for MM.

Techniques Used: Expressing, Diagnostic Assay

Figure 6. Expression of RUVBL2 and its clinical significance in MM. (A–C) Relative expression (log2) of RUVBL2 in normal and MM patients in GSE13591, GSE6477 and GSE146649 datasets from the GEO. (D) Relative mRNA expression of RUVBL2 in healthy donors (n = 8) and MM patients (n = 17) were assessed by qRT-PCR. (E) Protein expression of RUVBL2 in healthy donors and MM patients were assessed by Western blotting. (F) Histogram displayed the relative gray values. (G) Kaplan–Meier analysis and log-rank tests were used to assess the correlation between RUVBL2 expression level and survival in MM patients. *P < 0.05, low RUVBL2 vs. high RUVBL2. The data presented as the mean ± SD of three independent experiments.

Figure Legend Snippet: Figure 6. Expression of RUVBL2 and its clinical significance in MM. (A–C) Relative expression (log2) of RUVBL2 in normal and MM patients in GSE13591, GSE6477 and GSE146649 datasets from the GEO. (D) Relative mRNA expression of RUVBL2 in healthy donors (n = 8) and MM patients (n = 17) were assessed by qRT-PCR. (E) Protein expression of RUVBL2 in healthy donors and MM patients were assessed by Western blotting. (F) Histogram displayed the relative gray values. (G) Kaplan–Meier analysis and log-rank tests were used to assess the correlation between RUVBL2 expression level and survival in MM patients. *P < 0.05, low RUVBL2 vs. high RUVBL2. The data presented as the mean ± SD of three independent experiments.

Techniques Used: Expressing, Quantitative RT-PCR, Western Blot

Figure 7. RUVBL2 function in MM cells. (A) Inhibition efficiency of RUVBL2 siRNA was detected by qRT-PCR. (B) RUVBL2 was sup pressed using siRNA (NC siRNA and RUVBL2 siRNA). The protein expression of RUVBL2 was assessed by Western blotting. (C) RUVBL2 was inhibited in MM cells either using siRNA (NC siRNA and RUVBL2 siRNA) or by culturing in the absence or presence of BTZ (10 nM) for 48 h. Cell viability was detected by the CCK-8 assay. (D,E) RUVBL2 was inhibited in MM cells either using siRNA (NC siRNA and RUVBL2 siRNA) or by culturing in the absence or presence of BTZ (10 nM) for 48 h. The apoptosis rates were assessed by flow cytometry. The data presented as the mean ± SD of three independent experiments. *P < 0.05, **p < 0.01, ***p < 0.001.

Figure Legend Snippet: Figure 7. RUVBL2 function in MM cells. (A) Inhibition efficiency of RUVBL2 siRNA was detected by qRT-PCR. (B) RUVBL2 was sup pressed using siRNA (NC siRNA and RUVBL2 siRNA). The protein expression of RUVBL2 was assessed by Western blotting. (C) RUVBL2 was inhibited in MM cells either using siRNA (NC siRNA and RUVBL2 siRNA) or by culturing in the absence or presence of BTZ (10 nM) for 48 h. Cell viability was detected by the CCK-8 assay. (D,E) RUVBL2 was inhibited in MM cells either using siRNA (NC siRNA and RUVBL2 siRNA) or by culturing in the absence or presence of BTZ (10 nM) for 48 h. The apoptosis rates were assessed by flow cytometry. The data presented as the mean ± SD of three independent experiments. *P < 0.05, **p < 0.01, ***p < 0.001.

Techniques Used: Inhibition, Quantitative RT-PCR, Expressing, Western Blot, CCK-8 Assay, Flow Cytometry

Figure 8. Silencing RUVBL2 overcome BTZ resistance in MM patient-derived CD138+ myeloma cells. (A) Protein expression of RUVBL2 in MM patients (P1–P6) was assessed by Western blotting. P1–P3: BTZ-sensitive MM patients and P4–P6: BTZ-resistant MM patients. (B) Histogram displayed the relative gray values. (C) RUVBL2 was suppressed in CD138+ primary cells from borte zomib-resistant MM patients (P4–P6) either using siRNA (NC siRNA and RUVBL2 siRNA) or by culturing in the absence or presence of BTZ (10 nM) for 48 h. Cell viability was detected by the CCK-8 assay. (D,E) RUVBL2 was suppressed in CD138+ primary cells from BTZ-resistant MM patients (P4–P6) using RUVBL2 siRNA and then treated by BTZ (10 nM) for 48 h. The apoptosis rates were assessed by flow cytometry. The data presented as the mean ± SD of three independent experiments. *P < 0.05, **p < 0.01, ***p < 0.001, ****P < 0.0001.

Figure Legend Snippet: Figure 8. Silencing RUVBL2 overcome BTZ resistance in MM patient-derived CD138+ myeloma cells. (A) Protein expression of RUVBL2 in MM patients (P1–P6) was assessed by Western blotting. P1–P3: BTZ-sensitive MM patients and P4–P6: BTZ-resistant MM patients. (B) Histogram displayed the relative gray values. (C) RUVBL2 was suppressed in CD138+ primary cells from borte zomib-resistant MM patients (P4–P6) either using siRNA (NC siRNA and RUVBL2 siRNA) or by culturing in the absence or presence of BTZ (10 nM) for 48 h. Cell viability was detected by the CCK-8 assay. (D,E) RUVBL2 was suppressed in CD138+ primary cells from BTZ-resistant MM patients (P4–P6) using RUVBL2 siRNA and then treated by BTZ (10 nM) for 48 h. The apoptosis rates were assessed by flow cytometry. The data presented as the mean ± SD of three independent experiments. *P < 0.05, **p < 0.01, ***p < 0.001, ****P < 0.0001.

Techniques Used: Derivative Assay, Expressing, Western Blot, CCK-8 Assay, Flow Cytometry

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HMGB2, RUVBL2, and RPAP2 promote IAV polymerase activity. A) Minigenome reporter assay in eHAP WT cells transfected with a non-targeting siRNA (siNT), two siRNA pools targeting both ANP32A and ANP32B (siANP32.1 and siANP32.2), or siRNA pools targeting 31 genes enriched in WT cells or 2 genes enriched in both WT and ANP32-KO cells. Cells were transfected with plasmids to reconstitute PR8 polymerase activity. Firefly luciferase activity was normalized to co-transfected Renilla luciferase levels. Putative replication-specific proviral factors are shown in green, replication-specific antiviral factors in red, and transcription-specific proviral factors in blue. Statistical significance was assessed compared to siNT using an unpaired t test. B-I) Minigenome reporter assay in A549 WT and HMGB2-KO cells (B-E) or WT and RUVBL2-KO cells (F-I) transfected with plasmids to reconstitute PR8 (B and F), Vic75 (C and G), Eng195 (D and H), and Tky05 (E and I) polymerase activity. Firefly luciferase activity was normalized to co-transfected Renilla luciferase levels. Statistical significance was assessed compared to WT using an unpaired t test. J-O) Accumulation of segment 4 (Haemagglutinin (HA)) vRNA (J and M), cRNA (K and N), and mRNA (L and O) in A549 WT and RPAP2-KO cells (J-L) or WT and HMGB2-KO cells (M-O) following infection with PR8 (MOI=3). Data is shown as the fold change over input (0hpi). Statistical significance was assessed at each timepoint following log transformation using multiple unpaired t tests, corrected for multiple comparisons using the FDR. For all panels: Data is shown as mean of n=3 technical repeats, representative of n=3 biological repeats. ns, not significant; *, p<0.05; **, p<0.01; ***, p<0.001; ****, p<0.0001. See also Figure S4 and S5.

Journal: bioRxiv

Article Title: Influenza A virus polymerase co-opts distinct sets of host proteins for RNA transcription or replication

doi: 10.1101/2025.06.06.658254

Figure Lengend Snippet: HMGB2, RUVBL2, and RPAP2 promote IAV polymerase activity. A) Minigenome reporter assay in eHAP WT cells transfected with a non-targeting siRNA (siNT), two siRNA pools targeting both ANP32A and ANP32B (siANP32.1 and siANP32.2), or siRNA pools targeting 31 genes enriched in WT cells or 2 genes enriched in both WT and ANP32-KO cells. Cells were transfected with plasmids to reconstitute PR8 polymerase activity. Firefly luciferase activity was normalized to co-transfected Renilla luciferase levels. Putative replication-specific proviral factors are shown in green, replication-specific antiviral factors in red, and transcription-specific proviral factors in blue. Statistical significance was assessed compared to siNT using an unpaired t test. B-I) Minigenome reporter assay in A549 WT and HMGB2-KO cells (B-E) or WT and RUVBL2-KO cells (F-I) transfected with plasmids to reconstitute PR8 (B and F), Vic75 (C and G), Eng195 (D and H), and Tky05 (E and I) polymerase activity. Firefly luciferase activity was normalized to co-transfected Renilla luciferase levels. Statistical significance was assessed compared to WT using an unpaired t test. J-O) Accumulation of segment 4 (Haemagglutinin (HA)) vRNA (J and M), cRNA (K and N), and mRNA (L and O) in A549 WT and RPAP2-KO cells (J-L) or WT and HMGB2-KO cells (M-O) following infection with PR8 (MOI=3). Data is shown as the fold change over input (0hpi). Statistical significance was assessed at each timepoint following log transformation using multiple unpaired t tests, corrected for multiple comparisons using the FDR. For all panels: Data is shown as mean of n=3 technical repeats, representative of n=3 biological repeats. ns, not significant; *, p<0.05; **, p<0.01; ***, p<0.001; ****, p<0.0001. See also Figure S4 and S5.

Article Snippet: Commercial multi-guide sgRNAs targeting HMGB2, RUVBL2, and RPAP2 (Synthego) and non-targeting sgRNA (Synthego) were used.

Techniques: Activity Assay, Reporter Assay, Transfection, Luciferase, Infection, Transformation Assay

HMGB2 and RUVBL2 are replication-specific cofactors and RPAP2 is a transcription-specific cofactor. A) Schematic showing vRNA, cRNA, and mRNA synthesis in a minigenome setup with a WT, replication-deficient (PA E410A), or transcription-deficient (PA D108A) polymerase. B and C) cRNA:vRNA ratio (B) and mRNA:vRNA ratio (C) produced by a PR8 WT vRNP following transient knockdown of both ANP32A and ANP32B (siANP32.1 and siANP32.2), HMGB2, RUVBL2, or RPAP2. Activity of a replication-deficient vRNP (green striped) and transcription-deficient vRNP (blue striped) in cells transfected with a non-targeting siRNA (siNT) is also shown. cRNA:vRNA ratios were normalized to the ratio produced by the transcription-deficient vRNP in siNT-treated cells (B). mRNA:vRNA ratios were normalized to the ratio produced by the replication-deficient vRNP in siNT-treated cells (C). vRNA template provided was a pPolI-Firefly luciferase plasmid. Statistical significance was assessed compared to replication-deficient/transcription-deficient polymerases using an unpaired t test. D) Schematic showing vRNA, cRNA, and mRNA synthesis under conditions of a cRNP stabilization assay with cycloheximide (CHX) treatment. E-H) cRNP stabilization assay with CHX in A549 WT and HMGB2-KO cells (E and F) or WT and RPAP2-KO cells (G and H). Data is shown as fold change in segment 4 (Haemagglutinin (HA)) cRNA:vRNA ratio (E and G) and mRNA:vRNA ratio (F and H) over input (0hpi). Statistical significance was determined at each timepoint following log transformation using multiple unpaired t tests, corrected for multiple comparisons using the FDR. For (B), (C), and (E-H): Data is shown as mean of n=3 technical repeats, representative of n=3 biological repeats. ns, not significant; *, p<0.05; **, p<0.01; ***, p<0.001. See also Figure S6.

Journal: bioRxiv

Article Title: Influenza A virus polymerase co-opts distinct sets of host proteins for RNA transcription or replication

doi: 10.1101/2025.06.06.658254

Figure Lengend Snippet: HMGB2 and RUVBL2 are replication-specific cofactors and RPAP2 is a transcription-specific cofactor. A) Schematic showing vRNA, cRNA, and mRNA synthesis in a minigenome setup with a WT, replication-deficient (PA E410A), or transcription-deficient (PA D108A) polymerase. B and C) cRNA:vRNA ratio (B) and mRNA:vRNA ratio (C) produced by a PR8 WT vRNP following transient knockdown of both ANP32A and ANP32B (siANP32.1 and siANP32.2), HMGB2, RUVBL2, or RPAP2. Activity of a replication-deficient vRNP (green striped) and transcription-deficient vRNP (blue striped) in cells transfected with a non-targeting siRNA (siNT) is also shown. cRNA:vRNA ratios were normalized to the ratio produced by the transcription-deficient vRNP in siNT-treated cells (B). mRNA:vRNA ratios were normalized to the ratio produced by the replication-deficient vRNP in siNT-treated cells (C). vRNA template provided was a pPolI-Firefly luciferase plasmid. Statistical significance was assessed compared to replication-deficient/transcription-deficient polymerases using an unpaired t test. D) Schematic showing vRNA, cRNA, and mRNA synthesis under conditions of a cRNP stabilization assay with cycloheximide (CHX) treatment. E-H) cRNP stabilization assay with CHX in A549 WT and HMGB2-KO cells (E and F) or WT and RPAP2-KO cells (G and H). Data is shown as fold change in segment 4 (Haemagglutinin (HA)) cRNA:vRNA ratio (E and G) and mRNA:vRNA ratio (F and H) over input (0hpi). Statistical significance was determined at each timepoint following log transformation using multiple unpaired t tests, corrected for multiple comparisons using the FDR. For (B), (C), and (E-H): Data is shown as mean of n=3 technical repeats, representative of n=3 biological repeats. ns, not significant; *, p<0.05; **, p<0.01; ***, p<0.001. See also Figure S6.

Article Snippet: Commercial multi-guide sgRNAs targeting HMGB2, RUVBL2, and RPAP2 (Synthego) and non-targeting sgRNA (Synthego) were used.

Techniques: Produced, Knockdown, Activity Assay, Transfection, Luciferase, Plasmid Preparation, Transformation Assay

Journal: bioRxiv

Article Title: Influenza A virus polymerase co-opts distinct sets of host proteins for RNA transcription or replication

doi: 10.1101/2025.06.06.658254

Article Snippet: Primary antibodies used were rabbit IZ-vinculin (EPR8185; Abcam), rabbit IZ-PB2 (GTX125926; Genetex), rabbit IZ-HMGB2 (EPR6301; Abcam), rabbit IZ-RUVBL2 (10195-1-AP; ThermoFisher Scientific), mouse IZ-tubulin (AB7291; Abcam), mouse IZ-FLAG (F1804, Sigma).

Techniques: Activity Assay, Reporter Assay, Transfection, Luciferase, Infection, Transformation Assay

Journal: bioRxiv

Article Title: Influenza A virus polymerase co-opts distinct sets of host proteins for RNA transcription or replication

doi: 10.1101/2025.06.06.658254

Techniques: Produced, Knockdown, Activity Assay, Transfection, Luciferase, Plasmid Preparation, Transformation Assay

Journal: Cell reports

Article Title: The Hao-Fountain syndrome protein USP7 regulates neuronal connectivity in the brain via a novel p53-independent ubiquitin signaling pathway

doi: 10.1016/j.celrep.2025.115231

Figure Lengend Snippet:

Article Snippet: Mouse anti-Ruvbl2 , Santa Cruz , Cat# sc-374135, RRID:AB_10915735.

Techniques: Western Blot, Immunoprecipitation, Immunofluorescence, Virus, Recombinant, Protease Inhibitor, Magnetic Beads, Mass Spectrometry, Software

Journal: Hematology (Amsterdam, Netherlands)

Article Title: Identification of RUVBL2 as a novel biomarker to predict the prognosis and drug sensitivity in multiple myeloma based on ferroptosis genes.

doi: 10.1080/16078454.2025.2467499

Figure Lengend Snippet: Figure 5. Correlation between candidate genes expression and DSS in MM. (A) Kaplan–Meier survival curves comparing high and low levels of six candidate genes in MM were analyzed using the GSE2658 dataset (n = 559). Cox P < 0.05 was considered to be statistically difference. (B) Diagnostic value of TP53 in GSE13591 for MM. (C) Diagnostic value of RUVBL2 in GSE13591 for MM. (D) Diagnostic value of MCM5 in GSE13591 for MM.

Article Snippet: RUVBL2 and β-actin antibodies were bought from Proteintech (Wuhan, China).

Techniques: Expressing, Diagnostic Assay

Journal: Hematology (Amsterdam, Netherlands)

Article Title: Identification of RUVBL2 as a novel biomarker to predict the prognosis and drug sensitivity in multiple myeloma based on ferroptosis genes.

doi: 10.1080/16078454.2025.2467499

Figure Lengend Snippet: Figure 6. Expression of RUVBL2 and its clinical significance in MM. (A–C) Relative expression (log2) of RUVBL2 in normal and MM patients in GSE13591, GSE6477 and GSE146649 datasets from the GEO. (D) Relative mRNA expression of RUVBL2 in healthy donors (n = 8) and MM patients (n = 17) were assessed by qRT-PCR. (E) Protein expression of RUVBL2 in healthy donors and MM patients were assessed by Western blotting. (F) Histogram displayed the relative gray values. (G) Kaplan–Meier analysis and log-rank tests were used to assess the correlation between RUVBL2 expression level and survival in MM patients. *P < 0.05, low RUVBL2 vs. high RUVBL2. The data presented as the mean ± SD of three independent experiments.

Article Snippet: RUVBL2 and β-actin antibodies were bought from Proteintech (Wuhan, China).

Techniques: Expressing, Quantitative RT-PCR, Western Blot

Journal: Hematology (Amsterdam, Netherlands)

Article Title: Identification of RUVBL2 as a novel biomarker to predict the prognosis and drug sensitivity in multiple myeloma based on ferroptosis genes.

doi: 10.1080/16078454.2025.2467499

Figure Lengend Snippet: Figure 7. RUVBL2 function in MM cells. (A) Inhibition efficiency of RUVBL2 siRNA was detected by qRT-PCR. (B) RUVBL2 was sup pressed using siRNA (NC siRNA and RUVBL2 siRNA). The protein expression of RUVBL2 was assessed by Western blotting. (C) RUVBL2 was inhibited in MM cells either using siRNA (NC siRNA and RUVBL2 siRNA) or by culturing in the absence or presence of BTZ (10 nM) for 48 h. Cell viability was detected by the CCK-8 assay. (D,E) RUVBL2 was inhibited in MM cells either using siRNA (NC siRNA and RUVBL2 siRNA) or by culturing in the absence or presence of BTZ (10 nM) for 48 h. The apoptosis rates were assessed by flow cytometry. The data presented as the mean ± SD of three independent experiments. *P < 0.05, **p < 0.01, ***p < 0.001.

Article Snippet: RUVBL2 and β-actin antibodies were bought from Proteintech (Wuhan, China).

Techniques: Inhibition, Quantitative RT-PCR, Expressing, Western Blot, CCK-8 Assay, Flow Cytometry

Journal: Hematology (Amsterdam, Netherlands)

Article Title: Identification of RUVBL2 as a novel biomarker to predict the prognosis and drug sensitivity in multiple myeloma based on ferroptosis genes.

doi: 10.1080/16078454.2025.2467499

Figure Lengend Snippet: Figure 8. Silencing RUVBL2 overcome BTZ resistance in MM patient-derived CD138+ myeloma cells. (A) Protein expression of RUVBL2 in MM patients (P1–P6) was assessed by Western blotting. P1–P3: BTZ-sensitive MM patients and P4–P6: BTZ-resistant MM patients. (B) Histogram displayed the relative gray values. (C) RUVBL2 was suppressed in CD138+ primary cells from borte zomib-resistant MM patients (P4–P6) either using siRNA (NC siRNA and RUVBL2 siRNA) or by culturing in the absence or presence of BTZ (10 nM) for 48 h. Cell viability was detected by the CCK-8 assay. (D,E) RUVBL2 was suppressed in CD138+ primary cells from BTZ-resistant MM patients (P4–P6) using RUVBL2 siRNA and then treated by BTZ (10 nM) for 48 h. The apoptosis rates were assessed by flow cytometry. The data presented as the mean ± SD of three independent experiments. *P < 0.05, **p < 0.01, ***p < 0.001, ****P < 0.0001.

Article Snippet: RUVBL2 and β-actin antibodies were bought from Proteintech (Wuhan, China).

Techniques: Derivative Assay, Expressing, Western Blot, CCK-8 Assay, Flow Cytometry

(A) Tracing of oxygen consumption rate (OCR) basal and injection with 10 nM oleic acid (OA) or OA + 40 nM Etomoxir (Eto). (B) The sperm, after 1 hour of incubation with or without seminal vesicle secretions (SV) from nontreated (Ctrl) or flutamide-treated mice(Flu), were used for IVF, and the cleavaged oocytes were observed. The absolute number of oocytes collected from the oviduct and the cleavage rate are shown. (C) Western blot analysis for phosphotyrosine (P-Tyr) in capacitated spermatozoa (Ctrl; 1-hour incubation in HTF medium) and treated with SV from healthy mice or 10 nM oleic acid (OA). (D) Quantitative analysis of GLUT4 relative to α-tubulin obtained from Western blot. (E) Flow cytometric analysis of the sperm after 1 hour incubation in control medium (HTF) and medium containing SV or 10 nM OA, using fluorescein isothiocyanate-conjugated peanut agglutinin (PNA-FITC; to distinguish between acrosome-reacted and non-reacted cells) and propidium iodide (PI; to distinguish between dead and viable cells). (F) The percentage of viable sperm with an acrosome reaction (PI-, PNA-FITC+) was evaluated by flow cytometry in the 4th quadrant (4Q; red square). Data are mean ± SEM. At least three independent replicates. Percentage data were subjected to arcsine transformation before statistical analysis. (B) Dunnett’s test was used to analyze the cleavage rate. Different letters represent significantly different groups. (D,F) Differences between groups were assessed by one-way analysis of variance (ANOVA). When ANOVA was significant, differences among values were analyzed by Tukey’s Honest Significant Difference test for multiple comparisons.

Journal: bioRxiv

Article Title: Testosterone-Induced Metabolic Changes in Seminal Vesicle Epithelial cells Alter Plasma Components to Enhance Sperm Fertility

doi: 10.1101/2024.01.16.575926

Figure Lengend Snippet: (A) Tracing of oxygen consumption rate (OCR) basal and injection with 10 nM oleic acid (OA) or OA + 40 nM Etomoxir (Eto). (B) The sperm, after 1 hour of incubation with or without seminal vesicle secretions (SV) from nontreated (Ctrl) or flutamide-treated mice(Flu), were used for IVF, and the cleavaged oocytes were observed. The absolute number of oocytes collected from the oviduct and the cleavage rate are shown. (C) Western blot analysis for phosphotyrosine (P-Tyr) in capacitated spermatozoa (Ctrl; 1-hour incubation in HTF medium) and treated with SV from healthy mice or 10 nM oleic acid (OA). (D) Quantitative analysis of GLUT4 relative to α-tubulin obtained from Western blot. (E) Flow cytometric analysis of the sperm after 1 hour incubation in control medium (HTF) and medium containing SV or 10 nM OA, using fluorescein isothiocyanate-conjugated peanut agglutinin (PNA-FITC; to distinguish between acrosome-reacted and non-reacted cells) and propidium iodide (PI; to distinguish between dead and viable cells). (F) The percentage of viable sperm with an acrosome reaction (PI-, PNA-FITC+) was evaluated by flow cytometry in the 4th quadrant (4Q; red square). Data are mean ± SEM. At least three independent replicates. Percentage data were subjected to arcsine transformation before statistical analysis. (B) Dunnett’s test was used to analyze the cleavage rate. Different letters represent significantly different groups. (D,F) Differences between groups were assessed by one-way analysis of variance (ANOVA). When ANOVA was significant, differences among values were analyzed by Tukey’s Honest Significant Difference test for multiple comparisons.

Article Snippet: The membranes were incubated overnight at 4°C with primary antibodies: anti-phosphotyrosine antibody (1:10,000; 8959; Cell Signaling), anti-GLUT4 antibody (1:100; ab33780; Abcam), anti-ACLY antibody (1:10,000; ab40793; Abcam) or anti-α/β-Tubulin antibody (1:1,000; 2148S; Cell Signaling).

Techniques: Injection, Incubation, Western Blot, Control, Flow Cytometry, Transformation Assay

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