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Bio-Rad superscript kit
Superscript Kit, supplied by Bio-Rad, used in various techniques. Bioz Stars score: 92/100, based on 3 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/result/superscript kit/product/Bio-Rad
Average 92 stars, based on 3 article reviews
Price from $9.99 to $1999.99
superscript kit - by Bioz Stars, 2020-08
92/100 stars

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Real-time Polymerase Chain Reaction:

Article Title: Sca-1 Identifies a Distinct Androgen-Independent Murine Prostatic Luminal Cell Lineage with Bipotent Potential
Article Snippet: .. Reverse transcription was performed using the superscript Kit (BioRad, Hercules, CA). qRT-PCR was performed using the SYBR GreenER qPCR mix (BioRad, Hercules, CA) on a StepOne plus Real-Time PCR system (Applied Biosystems, Grand Island, NY). ..

Quantitative RT-PCR:

Article Title: Sca-1 Identifies a Distinct Androgen-Independent Murine Prostatic Luminal Cell Lineage with Bipotent Potential
Article Snippet: .. Reverse transcription was performed using the superscript Kit (BioRad, Hercules, CA). qRT-PCR was performed using the SYBR GreenER qPCR mix (BioRad, Hercules, CA) on a StepOne plus Real-Time PCR system (Applied Biosystems, Grand Island, NY). ..

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  • 86
    Bio-Rad cdna superscript kit
    <t>SREBP</t> expression levels in BMDM of WT and SREBP-1aDF mice Total RNA was isolated from BMDM and equal amounts of RNA were used for the quantitative RT-PCR assay. RNA expression level for SREBP-1a (A), SREBP-1c (B), and SREBP-2 (C) are shown as the quantitative expression levels calculated by comparison to qPCR values obtained with a standard curve of serially diluted linear plasmid <t>cDNA.</t> The data are plotted as femtograms of RNA normalized to ribosomal L32 samples analyzed in parallel. Bars represent the standard deviations. (D) nuclear SREBP-1 protein level. Nuclear protein was prepared from BMDM of WT and SREBP-1aDF mice. Aliquots (30 µg) were analyzed by immunoblotting for SREBP-1. *, p = 0.0031, indicating a statistically significant difference between BMDM from the two lines of mice.
    Cdna Superscript Kit, supplied by Bio-Rad, used in various techniques. Bioz Stars score: 86/100, based on 4 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/cdna superscript kit/product/Bio-Rad
    Average 86 stars, based on 4 article reviews
    Price from $9.99 to $1999.99
    cdna superscript kit - by Bioz Stars, 2020-08
    86/100 stars
      Buy from Supplier

    92
    Bio-Rad superscript iii first strand synthesis kit
    Mechanisms of CSC regulation by HSF1 a Western blots of <t>three</t> matched pairs of HSF1 high CSC-like BPLER vs. HSF1 low non-CSC-like HMLER cells (#2-4) reveal only minor differences in heat shock proteins HSP70 and HSP90. The cell lysates were probed with anti-HSP70 and anti-HSP90 antibodies. β -actin (Actin) was used as loading control. b Real-time <t>PCR</t> analysis of ZEB1 mRNA reveals no significant change with HSF1 over-expression ( left panel ) and knockdown ( right panel ) after 2 days DOX addition. The Zeb1 mRNA was quantified with real-time PCR after HSF1 over-expression in SUM159 and BT20 cells ( black bar, left panel ) or knockdown in BT474, T47D, and MCF7 cells ( black bar, right panel ) compared to control cells without DOX ( white bars ). GAPDH was used to normalize Ct value. The error bars represent standard deviation of the mean. c HSF1 over-expression or knockdown has no effect on heat shock protein (HSP) or EMT marker expression. Western blot analysis of HSF1, HSP 70, 90, E-cadherin(E-cad), and Vimentin(Vim) after HSF1 over-expression (HSF1) in SUM159 and BT20 cells (left panel) and knockdown (KD) in BT474, T47D, and MCF7 cells ( right panel ) cells compared to control cells (without DOX) revealed no significant changes. β -actin (Actin) was used as loading control. d HSF1 high CSC-like BPLER cells are more sensitive to protein translation inhibition compared to HSF1 low non-CSC-like HMLER cells. Three pairs of matched BPLER and HMLER cell lines (#2–4) were treated either with cycloheximide ( top panel ) or anisomycin ( bottom panel ) for 8 h, and cultured in drug-free medium for 4 days and cell viability was measured with celltiter-blue assay on day 4. The bar graphs show percent cell viability as compared to control cells (100 %, not shown here). HMLER: white bar ; BPLER: black bar
    Superscript Iii First Strand Synthesis Kit, supplied by Bio-Rad, used in various techniques. Bioz Stars score: 92/100, based on 2 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/superscript iii first strand synthesis kit/product/Bio-Rad
    Average 92 stars, based on 2 article reviews
    Price from $9.99 to $1999.99
    superscript iii first strand synthesis kit - by Bioz Stars, 2020-08
    92/100 stars
      Buy from Supplier

    99
    Bio-Rad superscript cdna synthesis kit
    Mechanisms of CSC regulation by HSF1 a Western blots of <t>three</t> matched pairs of HSF1 high CSC-like BPLER vs. HSF1 low non-CSC-like HMLER cells (#2-4) reveal only minor differences in heat shock proteins HSP70 and HSP90. The cell lysates were probed with anti-HSP70 and anti-HSP90 antibodies. β -actin (Actin) was used as loading control. b Real-time <t>PCR</t> analysis of ZEB1 mRNA reveals no significant change with HSF1 over-expression ( left panel ) and knockdown ( right panel ) after 2 days DOX addition. The Zeb1 mRNA was quantified with real-time PCR after HSF1 over-expression in SUM159 and BT20 cells ( black bar, left panel ) or knockdown in BT474, T47D, and MCF7 cells ( black bar, right panel ) compared to control cells without DOX ( white bars ). GAPDH was used to normalize Ct value. The error bars represent standard deviation of the mean. c HSF1 over-expression or knockdown has no effect on heat shock protein (HSP) or EMT marker expression. Western blot analysis of HSF1, HSP 70, 90, E-cadherin(E-cad), and Vimentin(Vim) after HSF1 over-expression (HSF1) in SUM159 and BT20 cells (left panel) and knockdown (KD) in BT474, T47D, and MCF7 cells ( right panel ) cells compared to control cells (without DOX) revealed no significant changes. β -actin (Actin) was used as loading control. d HSF1 high CSC-like BPLER cells are more sensitive to protein translation inhibition compared to HSF1 low non-CSC-like HMLER cells. Three pairs of matched BPLER and HMLER cell lines (#2–4) were treated either with cycloheximide ( top panel ) or anisomycin ( bottom panel ) for 8 h, and cultured in drug-free medium for 4 days and cell viability was measured with celltiter-blue assay on day 4. The bar graphs show percent cell viability as compared to control cells (100 %, not shown here). HMLER: white bar ; BPLER: black bar
    Superscript Cdna Synthesis Kit, supplied by Bio-Rad, used in various techniques. Bioz Stars score: 99/100, based on 2 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/superscript cdna synthesis kit/product/Bio-Rad
    Average 99 stars, based on 2 article reviews
    Price from $9.99 to $1999.99
    superscript cdna synthesis kit - by Bioz Stars, 2020-08
    99/100 stars
      Buy from Supplier

    92
    Bio-Rad superscript kit
    Mechanisms of CSC regulation by HSF1 a Western blots of <t>three</t> matched pairs of HSF1 high CSC-like BPLER vs. HSF1 low non-CSC-like HMLER cells (#2-4) reveal only minor differences in heat shock proteins HSP70 and HSP90. The cell lysates were probed with anti-HSP70 and anti-HSP90 antibodies. β -actin (Actin) was used as loading control. b Real-time <t>PCR</t> analysis of ZEB1 mRNA reveals no significant change with HSF1 over-expression ( left panel ) and knockdown ( right panel ) after 2 days DOX addition. The Zeb1 mRNA was quantified with real-time PCR after HSF1 over-expression in SUM159 and BT20 cells ( black bar, left panel ) or knockdown in BT474, T47D, and MCF7 cells ( black bar, right panel ) compared to control cells without DOX ( white bars ). GAPDH was used to normalize Ct value. The error bars represent standard deviation of the mean. c HSF1 over-expression or knockdown has no effect on heat shock protein (HSP) or EMT marker expression. Western blot analysis of HSF1, HSP 70, 90, E-cadherin(E-cad), and Vimentin(Vim) after HSF1 over-expression (HSF1) in SUM159 and BT20 cells (left panel) and knockdown (KD) in BT474, T47D, and MCF7 cells ( right panel ) cells compared to control cells (without DOX) revealed no significant changes. β -actin (Actin) was used as loading control. d HSF1 high CSC-like BPLER cells are more sensitive to protein translation inhibition compared to HSF1 low non-CSC-like HMLER cells. Three pairs of matched BPLER and HMLER cell lines (#2–4) were treated either with cycloheximide ( top panel ) or anisomycin ( bottom panel ) for 8 h, and cultured in drug-free medium for 4 days and cell viability was measured with celltiter-blue assay on day 4. The bar graphs show percent cell viability as compared to control cells (100 %, not shown here). HMLER: white bar ; BPLER: black bar
    Superscript Kit, supplied by Bio-Rad, used in various techniques. Bioz Stars score: 92/100, based on 3 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/superscript kit/product/Bio-Rad
    Average 92 stars, based on 3 article reviews
    Price from $9.99 to $1999.99
    superscript kit - by Bioz Stars, 2020-08
    92/100 stars
      Buy from Supplier

    Image Search Results


    SREBP expression levels in BMDM of WT and SREBP-1aDF mice Total RNA was isolated from BMDM and equal amounts of RNA were used for the quantitative RT-PCR assay. RNA expression level for SREBP-1a (A), SREBP-1c (B), and SREBP-2 (C) are shown as the quantitative expression levels calculated by comparison to qPCR values obtained with a standard curve of serially diluted linear plasmid cDNA. The data are plotted as femtograms of RNA normalized to ribosomal L32 samples analyzed in parallel. Bars represent the standard deviations. (D) nuclear SREBP-1 protein level. Nuclear protein was prepared from BMDM of WT and SREBP-1aDF mice. Aliquots (30 µg) were analyzed by immunoblotting for SREBP-1. *, p = 0.0031, indicating a statistically significant difference between BMDM from the two lines of mice.

    Journal: Cell metabolism

    Article Title: Linking Lipid Metabolism to the Innate Immune Response in Macrophages through Sterol Regulatory Element Binding Protein -1a

    doi: 10.1016/j.cmet.2011.04.001

    Figure Lengend Snippet: SREBP expression levels in BMDM of WT and SREBP-1aDF mice Total RNA was isolated from BMDM and equal amounts of RNA were used for the quantitative RT-PCR assay. RNA expression level for SREBP-1a (A), SREBP-1c (B), and SREBP-2 (C) are shown as the quantitative expression levels calculated by comparison to qPCR values obtained with a standard curve of serially diluted linear plasmid cDNA. The data are plotted as femtograms of RNA normalized to ribosomal L32 samples analyzed in parallel. Bars represent the standard deviations. (D) nuclear SREBP-1 protein level. Nuclear protein was prepared from BMDM of WT and SREBP-1aDF mice. Aliquots (30 µg) were analyzed by immunoblotting for SREBP-1. *, p = 0.0031, indicating a statistically significant difference between BMDM from the two lines of mice.

    Article Snippet: Total RNA was isolated from macrophages of WT and SREBP-1aDF mice using the Trizol method (Invitrogen). cDNA was synthesized by cDNA superscript kit (Bio-Rad) and used for qPCR with Real-Time PCR Detection (Bio-Rad). mRNA levels were normalized for expression of ribosomal protein L32 mRNA as control and calculated by the comparative threshold cycle method.

    Techniques: Expressing, Mouse Assay, Isolation, Quantitative RT-PCR, RNA Expression, Real-time Polymerase Chain Reaction, Plasmid Preparation

    Mechanisms of CSC regulation by HSF1 a Western blots of three matched pairs of HSF1 high CSC-like BPLER vs. HSF1 low non-CSC-like HMLER cells (#2-4) reveal only minor differences in heat shock proteins HSP70 and HSP90. The cell lysates were probed with anti-HSP70 and anti-HSP90 antibodies. β -actin (Actin) was used as loading control. b Real-time PCR analysis of ZEB1 mRNA reveals no significant change with HSF1 over-expression ( left panel ) and knockdown ( right panel ) after 2 days DOX addition. The Zeb1 mRNA was quantified with real-time PCR after HSF1 over-expression in SUM159 and BT20 cells ( black bar, left panel ) or knockdown in BT474, T47D, and MCF7 cells ( black bar, right panel ) compared to control cells without DOX ( white bars ). GAPDH was used to normalize Ct value. The error bars represent standard deviation of the mean. c HSF1 over-expression or knockdown has no effect on heat shock protein (HSP) or EMT marker expression. Western blot analysis of HSF1, HSP 70, 90, E-cadherin(E-cad), and Vimentin(Vim) after HSF1 over-expression (HSF1) in SUM159 and BT20 cells (left panel) and knockdown (KD) in BT474, T47D, and MCF7 cells ( right panel ) cells compared to control cells (without DOX) revealed no significant changes. β -actin (Actin) was used as loading control. d HSF1 high CSC-like BPLER cells are more sensitive to protein translation inhibition compared to HSF1 low non-CSC-like HMLER cells. Three pairs of matched BPLER and HMLER cell lines (#2–4) were treated either with cycloheximide ( top panel ) or anisomycin ( bottom panel ) for 8 h, and cultured in drug-free medium for 4 days and cell viability was measured with celltiter-blue assay on day 4. The bar graphs show percent cell viability as compared to control cells (100 %, not shown here). HMLER: white bar ; BPLER: black bar

    Journal: Breast Cancer Research and Treatment

    Article Title: Heat shock factor 1 induces cancer stem cell phenotype in breast cancer cell lines

    doi: 10.1007/s10549-015-3521-1

    Figure Lengend Snippet: Mechanisms of CSC regulation by HSF1 a Western blots of three matched pairs of HSF1 high CSC-like BPLER vs. HSF1 low non-CSC-like HMLER cells (#2-4) reveal only minor differences in heat shock proteins HSP70 and HSP90. The cell lysates were probed with anti-HSP70 and anti-HSP90 antibodies. β -actin (Actin) was used as loading control. b Real-time PCR analysis of ZEB1 mRNA reveals no significant change with HSF1 over-expression ( left panel ) and knockdown ( right panel ) after 2 days DOX addition. The Zeb1 mRNA was quantified with real-time PCR after HSF1 over-expression in SUM159 and BT20 cells ( black bar, left panel ) or knockdown in BT474, T47D, and MCF7 cells ( black bar, right panel ) compared to control cells without DOX ( white bars ). GAPDH was used to normalize Ct value. The error bars represent standard deviation of the mean. c HSF1 over-expression or knockdown has no effect on heat shock protein (HSP) or EMT marker expression. Western blot analysis of HSF1, HSP 70, 90, E-cadherin(E-cad), and Vimentin(Vim) after HSF1 over-expression (HSF1) in SUM159 and BT20 cells (left panel) and knockdown (KD) in BT474, T47D, and MCF7 cells ( right panel ) cells compared to control cells (without DOX) revealed no significant changes. β -actin (Actin) was used as loading control. d HSF1 high CSC-like BPLER cells are more sensitive to protein translation inhibition compared to HSF1 low non-CSC-like HMLER cells. Three pairs of matched BPLER and HMLER cell lines (#2–4) were treated either with cycloheximide ( top panel ) or anisomycin ( bottom panel ) for 8 h, and cultured in drug-free medium for 4 days and cell viability was measured with celltiter-blue assay on day 4. The bar graphs show percent cell viability as compared to control cells (100 %, not shown here). HMLER: white bar ; BPLER: black bar

    Article Snippet: Real-time RT-PCR Quantitative real-time RT-PCR was performed using SuperScript® III First-Strand Synthesis kit and SsoFast ™ EvaGreen® Supermix according to the manufacturers’ instructions and analyzed with BioRad CFX Manager Software.

    Techniques: Western Blot, Real-time Polymerase Chain Reaction, Over Expression, Standard Deviation, Marker, Expressing, Inhibition, Cell Culture, CtB Assay