l wnt 3a  (ATCC)


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    ATCC l wnt 3a
    L Wnt 3a, supplied by ATCC, used in various techniques. Bioz Stars score: 99/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    crl 2647 mouse  (ATCC)


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    ATCC crl 2647 mouse
    Crl 2647 Mouse, supplied by ATCC, used in various techniques. Bioz Stars score: 86/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    l wnt 3a atcc crl 2647 mouse  (ATCC)


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    ATCC l wnt 3a atcc crl 2647 mouse
    L Wnt 3a Atcc Crl 2647 Mouse, supplied by ATCC, used in various techniques. Bioz Stars score: 86/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    l wnt 3a  (ATCC)


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    ATCC l wnt 3a
    L Wnt 3a, supplied by ATCC, used in various techniques. Bioz Stars score: 99/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    mwnt3a  (ATCC)


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    ATCC mwnt3a
    Mwnt3a, supplied by ATCC, used in various techniques. Bioz Stars score: 99/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    l wnt3a cells  (ATCC)


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    ATCC l wnt3a cells
    PANK1 inhibits the Wnt/β-catenin signaling pathway. (A) The Topflash reporter was used to detect the effect of PANK1 on the transcriptional activity of β-catenin. After transfection, the cells were stimulated by lithium chloride or <t>Wnt3a</t> for 8h before the measurement of the reporter activity. (B) The effect of overexpression of PANK1 on the level of β-catenin protein in PVTT and QGY-7701 cells was measured. After the cells were stimulated by Wnt3a for different periods of time, the β-catenin protein was measured by western blot. (C) The effect of knocked-down expression of PANK1 on the level of β-catenin protein in Huh7 and QGY-7701 cells was measured. After the cells were stimulated by Wnt3a for different periods of time, the β-catenin protein was measured by western blot. (D-E) The effect of overexpression of PANK1 in Huh7 and QGY-7701 cells on the half-life of β-catenin protein level was measured. After the cells were stimulated by CHX (50µg/ml) for different periods of time, the β-catenin protein was measured by western blot. The levels of β-catenin protein were quantified and analyze. (F) The effect of PANK1 overexpression in PVTT and QGY-7701 cells on the mRNA level of Axin2 was measured. After being stimulated by Wnt3a for different periods of time, the cells were collected to measure the mRNA level of Axin2. (G) The effect of knocked-down expression of PANK1 in Huh7 and QGY-7701 cells on the mRNA levels of Axin2 was measured. After the cells were stimulated by Wnt3a for different periods of time, they were collected to measure the mRNA level of Axin2. (H) RNA sequencing was performed on Huh7 cells with the knockdown of PANK1 expression, and on control cells, obtaining a volcano plot. (I) Differential expression of target genes of the Wnt/β-catenin signaling pathway from RNA sequencing, shown as a heat map. (J) As shown in the GEPIA database, PANK1 expression is negatively correlated with expression of Axin and SOX9, the target genes of Wnt/β-catenin signaling pathway. ****, P <0.0001.
    L Wnt3a Cells, supplied by ATCC, used in various techniques. Bioz Stars score: 99/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    1) Product Images from "Pantothenate Kinase 1 Inhibits the Progression of Hepatocellular Carcinoma by Negatively Regulating Wnt/β-catenin Signaling"

    Article Title: Pantothenate Kinase 1 Inhibits the Progression of Hepatocellular Carcinoma by Negatively Regulating Wnt/β-catenin Signaling

    Journal: International Journal of Biological Sciences

    doi: 10.7150/ijbs.67842

    PANK1 inhibits the Wnt/β-catenin signaling pathway. (A) The Topflash reporter was used to detect the effect of PANK1 on the transcriptional activity of β-catenin. After transfection, the cells were stimulated by lithium chloride or Wnt3a for 8h before the measurement of the reporter activity. (B) The effect of overexpression of PANK1 on the level of β-catenin protein in PVTT and QGY-7701 cells was measured. After the cells were stimulated by Wnt3a for different periods of time, the β-catenin protein was measured by western blot. (C) The effect of knocked-down expression of PANK1 on the level of β-catenin protein in Huh7 and QGY-7701 cells was measured. After the cells were stimulated by Wnt3a for different periods of time, the β-catenin protein was measured by western blot. (D-E) The effect of overexpression of PANK1 in Huh7 and QGY-7701 cells on the half-life of β-catenin protein level was measured. After the cells were stimulated by CHX (50µg/ml) for different periods of time, the β-catenin protein was measured by western blot. The levels of β-catenin protein were quantified and analyze. (F) The effect of PANK1 overexpression in PVTT and QGY-7701 cells on the mRNA level of Axin2 was measured. After being stimulated by Wnt3a for different periods of time, the cells were collected to measure the mRNA level of Axin2. (G) The effect of knocked-down expression of PANK1 in Huh7 and QGY-7701 cells on the mRNA levels of Axin2 was measured. After the cells were stimulated by Wnt3a for different periods of time, they were collected to measure the mRNA level of Axin2. (H) RNA sequencing was performed on Huh7 cells with the knockdown of PANK1 expression, and on control cells, obtaining a volcano plot. (I) Differential expression of target genes of the Wnt/β-catenin signaling pathway from RNA sequencing, shown as a heat map. (J) As shown in the GEPIA database, PANK1 expression is negatively correlated with expression of Axin and SOX9, the target genes of Wnt/β-catenin signaling pathway. ****, P <0.0001.
    Figure Legend Snippet: PANK1 inhibits the Wnt/β-catenin signaling pathway. (A) The Topflash reporter was used to detect the effect of PANK1 on the transcriptional activity of β-catenin. After transfection, the cells were stimulated by lithium chloride or Wnt3a for 8h before the measurement of the reporter activity. (B) The effect of overexpression of PANK1 on the level of β-catenin protein in PVTT and QGY-7701 cells was measured. After the cells were stimulated by Wnt3a for different periods of time, the β-catenin protein was measured by western blot. (C) The effect of knocked-down expression of PANK1 on the level of β-catenin protein in Huh7 and QGY-7701 cells was measured. After the cells were stimulated by Wnt3a for different periods of time, the β-catenin protein was measured by western blot. (D-E) The effect of overexpression of PANK1 in Huh7 and QGY-7701 cells on the half-life of β-catenin protein level was measured. After the cells were stimulated by CHX (50µg/ml) for different periods of time, the β-catenin protein was measured by western blot. The levels of β-catenin protein were quantified and analyze. (F) The effect of PANK1 overexpression in PVTT and QGY-7701 cells on the mRNA level of Axin2 was measured. After being stimulated by Wnt3a for different periods of time, the cells were collected to measure the mRNA level of Axin2. (G) The effect of knocked-down expression of PANK1 in Huh7 and QGY-7701 cells on the mRNA levels of Axin2 was measured. After the cells were stimulated by Wnt3a for different periods of time, they were collected to measure the mRNA level of Axin2. (H) RNA sequencing was performed on Huh7 cells with the knockdown of PANK1 expression, and on control cells, obtaining a volcano plot. (I) Differential expression of target genes of the Wnt/β-catenin signaling pathway from RNA sequencing, shown as a heat map. (J) As shown in the GEPIA database, PANK1 expression is negatively correlated with expression of Axin and SOX9, the target genes of Wnt/β-catenin signaling pathway. ****, P <0.0001.

    Techniques Used: Activity Assay, Transfection, Over Expression, Western Blot, Expressing, RNA Sequencing Assay

    PANK1 phosphorylates the N-terminal serine and threonine residues of β-catenin. (A) The effect of knockdown or overexpression of PANK1 in Huh7 and QGY-7701 cells on the phosphorylation level of β-catenin was measured. After the cells were stimulated by Wnt3a for different periods of time, the phosphorylation level of β-catenin was measured by western blot. (B) Ubiquitin assay was performed to measure the effect of PANK1 expression on the ubiquitination level of β-catenin. After being treated with MG132 for 10h, the PVTT cells with overexpressed PANK1, Huh7 cells, with down-regulated expression of PANK1, and their respective control cells were lysed for supernatant collection. The antibody against β-catenin was used for CO-IP. Then, a western blot assay was performed, and the antibody against ubiquitin was used for measurement. (C) The interaction between exogenously expressed CK1α (Myc-CK1α) and PANK1 (Flag-PANK1) was measured in 293T cells. The Myc-CK1α and Flag-PANK1 plasmids were transiently transfected into 293T cells. 48h later, CO-IP was performed with an antibody against Myc or the Flag tag. (D) The interaction between endogenous CK1α and PANK1 in Huh7 and QGY-7701 cells was measured. (E) The Wnt3a stimulation-dependent interaction between CK1α and PANK1 in QGY-7701 cells was measured. After treatment with Wnt3a for different periods of time, the QGY-7701 cells with the overexpression PANK1 were lysed and centrifuged for supernatant collection. The antibody against Flag was used for CO-IP. (F) The phosphorylation of β-catenin by PANK was measured through the in vitro kinase reaction. See “Materials and Methods” for the details on the reaction.
    Figure Legend Snippet: PANK1 phosphorylates the N-terminal serine and threonine residues of β-catenin. (A) The effect of knockdown or overexpression of PANK1 in Huh7 and QGY-7701 cells on the phosphorylation level of β-catenin was measured. After the cells were stimulated by Wnt3a for different periods of time, the phosphorylation level of β-catenin was measured by western blot. (B) Ubiquitin assay was performed to measure the effect of PANK1 expression on the ubiquitination level of β-catenin. After being treated with MG132 for 10h, the PVTT cells with overexpressed PANK1, Huh7 cells, with down-regulated expression of PANK1, and their respective control cells were lysed for supernatant collection. The antibody against β-catenin was used for CO-IP. Then, a western blot assay was performed, and the antibody against ubiquitin was used for measurement. (C) The interaction between exogenously expressed CK1α (Myc-CK1α) and PANK1 (Flag-PANK1) was measured in 293T cells. The Myc-CK1α and Flag-PANK1 plasmids were transiently transfected into 293T cells. 48h later, CO-IP was performed with an antibody against Myc or the Flag tag. (D) The interaction between endogenous CK1α and PANK1 in Huh7 and QGY-7701 cells was measured. (E) The Wnt3a stimulation-dependent interaction between CK1α and PANK1 in QGY-7701 cells was measured. After treatment with Wnt3a for different periods of time, the QGY-7701 cells with the overexpression PANK1 were lysed and centrifuged for supernatant collection. The antibody against Flag was used for CO-IP. (F) The phosphorylation of β-catenin by PANK was measured through the in vitro kinase reaction. See “Materials and Methods” for the details on the reaction.

    Techniques Used: Over Expression, Western Blot, Ubiquitin Assay, Expressing, Co-Immunoprecipitation Assay, Transfection, FLAG-tag, In Vitro

    lwnt3a cell line  (ATCC)


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    ATCC lwnt3a cell line
    Lwnt3a Cell Line, supplied by ATCC, used in various techniques. Bioz Stars score: 99/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    l wnt3a  (ATCC)


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    ATCC l wnt3a
    Mouse <t>L-Wnt3a</t> cells were cultured according to ATCC recommendations. Cells were then transfected with TOPflash or vector control and treated with Vehicle (DMSO), 5 μM IWP-2, or 10 μM IWP-2. Three days later a luciferase assay was performed and data was normalized to vector control. Data is representative of three separate experiments. *p≤0.05 in comparison to vehicle.
    L Wnt3a, supplied by ATCC, used in various techniques. Bioz Stars score: 99/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    1) Product Images from "Porcupine Is Not Required for the Production of the Majority of Wnts from Primary Human Astrocytes and CD8+ T Cells"

    Article Title: Porcupine Is Not Required for the Production of the Majority of Wnts from Primary Human Astrocytes and CD8+ T Cells

    Journal: PLoS ONE

    doi: 10.1371/journal.pone.0092159

    Mouse L-Wnt3a cells were cultured according to ATCC recommendations. Cells were then transfected with TOPflash or vector control and treated with Vehicle (DMSO), 5 μM IWP-2, or 10 μM IWP-2. Three days later a luciferase assay was performed and data was normalized to vector control. Data is representative of three separate experiments. *p≤0.05 in comparison to vehicle.
    Figure Legend Snippet: Mouse L-Wnt3a cells were cultured according to ATCC recommendations. Cells were then transfected with TOPflash or vector control and treated with Vehicle (DMSO), 5 μM IWP-2, or 10 μM IWP-2. Three days later a luciferase assay was performed and data was normalized to vector control. Data is representative of three separate experiments. *p≤0.05 in comparison to vehicle.

    Techniques Used: Cell Culture, Transfection, Plasmid Preparation, Luciferase

    mouse l1 cells expressing wnt3a  (ATCC)


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    ATCC mouse l1 cells expressing wnt3a
    Luciferase activity in CHO cells transfected with WT-LRP5 or mutant LRP5 in the presence of <t>Wnt3a-CM</t> (white bars) or L1 control medium (grey bars) . The activities of the signaling pathway are presented in relative luciferase units (RLU) determined by the ratio between the luciferase and β-galactosidase activities and given as a fold change relative to corresponding samples treated with 10% FBS-DMEM. * p < 0.05, ** p < 0.01 as compared with WT-LRP5. Results are expressed as mean ± SD.
    Mouse L1 Cells Expressing Wnt3a, supplied by ATCC, used in various techniques. Bioz Stars score: 99/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    1) Product Images from "Mutations in LRP5 cause primary osteoporosis without features of OI by reducing Wnt signaling activity"

    Article Title: Mutations in LRP5 cause primary osteoporosis without features of OI by reducing Wnt signaling activity

    Journal: BMC Medical Genetics

    doi: 10.1186/1471-2350-13-26

    Luciferase activity in CHO cells transfected with WT-LRP5 or mutant LRP5 in the presence of Wnt3a-CM (white bars) or L1 control medium (grey bars) . The activities of the signaling pathway are presented in relative luciferase units (RLU) determined by the ratio between the luciferase and β-galactosidase activities and given as a fold change relative to corresponding samples treated with 10% FBS-DMEM. * p < 0.05, ** p < 0.01 as compared with WT-LRP5. Results are expressed as mean ± SD.
    Figure Legend Snippet: Luciferase activity in CHO cells transfected with WT-LRP5 or mutant LRP5 in the presence of Wnt3a-CM (white bars) or L1 control medium (grey bars) . The activities of the signaling pathway are presented in relative luciferase units (RLU) determined by the ratio between the luciferase and β-galactosidase activities and given as a fold change relative to corresponding samples treated with 10% FBS-DMEM. * p < 0.05, ** p < 0.01 as compared with WT-LRP5. Results are expressed as mean ± SD.

    Techniques Used: Luciferase, Activity Assay, Transfection, Mutagenesis

    A) Tph1 gene expression and B) 5- Htr1b gene expression in CHO cells transfected with wild type LRP5 (WT-LRP5) or mutant LRP5 and treated with Wnt3a-CM or L1-CM . Expression of the Tph1 and 5- Htr1b genes is shown as a fold change relative to the untreated control (pcDNA3.1+) and normalized to β-actin . The effects of the LRP5 mutants on the expression of these genes were examined by comparing the results for the mutants with those for WT-LRP5 using Student's t test. The statistical significance of each pair is denoted below the mutant columns; ** p < 0.01 as compared to WT-LRP5. Results are expressed as mean ± SD.
    Figure Legend Snippet: A) Tph1 gene expression and B) 5- Htr1b gene expression in CHO cells transfected with wild type LRP5 (WT-LRP5) or mutant LRP5 and treated with Wnt3a-CM or L1-CM . Expression of the Tph1 and 5- Htr1b genes is shown as a fold change relative to the untreated control (pcDNA3.1+) and normalized to β-actin . The effects of the LRP5 mutants on the expression of these genes were examined by comparing the results for the mutants with those for WT-LRP5 using Student's t test. The statistical significance of each pair is denoted below the mutant columns; ** p < 0.01 as compared to WT-LRP5. Results are expressed as mean ± SD.

    Techniques Used: Expressing, Transfection, Mutagenesis

    l wnt3a cells  (ATCC)


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    ATCC l wnt3a cells
    Luciferase activity in CHO cells transfected with WT-LRP5 or mutant LRP5 in the presence of <t>Wnt3a-CM</t> (white bars) or L1 control medium (grey bars) . The activities of the signaling pathway are presented in relative luciferase units (RLU) determined by the ratio between the luciferase and β-galactosidase activities and given as a fold change relative to corresponding samples treated with 10% FBS-DMEM. * p < 0.05, ** p < 0.01 as compared with WT-LRP5. Results are expressed as mean ± SD.
    L Wnt3a Cells, supplied by ATCC, used in various techniques. Bioz Stars score: 99/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    1) Product Images from "Mutations in LRP5 cause primary osteoporosis without features of OI by reducing Wnt signaling activity"

    Article Title: Mutations in LRP5 cause primary osteoporosis without features of OI by reducing Wnt signaling activity

    Journal: BMC Medical Genetics

    doi: 10.1186/1471-2350-13-26

    Luciferase activity in CHO cells transfected with WT-LRP5 or mutant LRP5 in the presence of Wnt3a-CM (white bars) or L1 control medium (grey bars) . The activities of the signaling pathway are presented in relative luciferase units (RLU) determined by the ratio between the luciferase and β-galactosidase activities and given as a fold change relative to corresponding samples treated with 10% FBS-DMEM. * p < 0.05, ** p < 0.01 as compared with WT-LRP5. Results are expressed as mean ± SD.
    Figure Legend Snippet: Luciferase activity in CHO cells transfected with WT-LRP5 or mutant LRP5 in the presence of Wnt3a-CM (white bars) or L1 control medium (grey bars) . The activities of the signaling pathway are presented in relative luciferase units (RLU) determined by the ratio between the luciferase and β-galactosidase activities and given as a fold change relative to corresponding samples treated with 10% FBS-DMEM. * p < 0.05, ** p < 0.01 as compared with WT-LRP5. Results are expressed as mean ± SD.

    Techniques Used: Luciferase, Activity Assay, Transfection, Mutagenesis

    A) Tph1 gene expression and B) 5- Htr1b gene expression in CHO cells transfected with wild type LRP5 (WT-LRP5) or mutant LRP5 and treated with Wnt3a-CM or L1-CM . Expression of the Tph1 and 5- Htr1b genes is shown as a fold change relative to the untreated control (pcDNA3.1+) and normalized to β-actin . The effects of the LRP5 mutants on the expression of these genes were examined by comparing the results for the mutants with those for WT-LRP5 using Student's t test. The statistical significance of each pair is denoted below the mutant columns; ** p < 0.01 as compared to WT-LRP5. Results are expressed as mean ± SD.
    Figure Legend Snippet: A) Tph1 gene expression and B) 5- Htr1b gene expression in CHO cells transfected with wild type LRP5 (WT-LRP5) or mutant LRP5 and treated with Wnt3a-CM or L1-CM . Expression of the Tph1 and 5- Htr1b genes is shown as a fold change relative to the untreated control (pcDNA3.1+) and normalized to β-actin . The effects of the LRP5 mutants on the expression of these genes were examined by comparing the results for the mutants with those for WT-LRP5 using Student's t test. The statistical significance of each pair is denoted below the mutant columns; ** p < 0.01 as compared to WT-LRP5. Results are expressed as mean ± SD.

    Techniques Used: Expressing, Transfection, Mutagenesis

    l wnt 3a cells  (ATCC)


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    ATCC l wnt 3a cells
    L Wnt 3a Cells, supplied by ATCC, used in various techniques. Bioz Stars score: 99/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    ATCC l wnt3a cells
    PANK1 inhibits the Wnt/β-catenin signaling pathway. (A) The Topflash reporter was used to detect the effect of PANK1 on the transcriptional activity of β-catenin. After transfection, the cells were stimulated by lithium chloride or <t>Wnt3a</t> for 8h before the measurement of the reporter activity. (B) The effect of overexpression of PANK1 on the level of β-catenin protein in PVTT and QGY-7701 cells was measured. After the cells were stimulated by Wnt3a for different periods of time, the β-catenin protein was measured by western blot. (C) The effect of knocked-down expression of PANK1 on the level of β-catenin protein in Huh7 and QGY-7701 cells was measured. After the cells were stimulated by Wnt3a for different periods of time, the β-catenin protein was measured by western blot. (D-E) The effect of overexpression of PANK1 in Huh7 and QGY-7701 cells on the half-life of β-catenin protein level was measured. After the cells were stimulated by CHX (50µg/ml) for different periods of time, the β-catenin protein was measured by western blot. The levels of β-catenin protein were quantified and analyze. (F) The effect of PANK1 overexpression in PVTT and QGY-7701 cells on the mRNA level of Axin2 was measured. After being stimulated by Wnt3a for different periods of time, the cells were collected to measure the mRNA level of Axin2. (G) The effect of knocked-down expression of PANK1 in Huh7 and QGY-7701 cells on the mRNA levels of Axin2 was measured. After the cells were stimulated by Wnt3a for different periods of time, they were collected to measure the mRNA level of Axin2. (H) RNA sequencing was performed on Huh7 cells with the knockdown of PANK1 expression, and on control cells, obtaining a volcano plot. (I) Differential expression of target genes of the Wnt/β-catenin signaling pathway from RNA sequencing, shown as a heat map. (J) As shown in the GEPIA database, PANK1 expression is negatively correlated with expression of Axin and SOX9, the target genes of Wnt/β-catenin signaling pathway. ****, P <0.0001.
    L Wnt3a Cells, supplied by ATCC, used in various techniques. Bioz Stars score: 99/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    ATCC lwnt3a cell line
    PANK1 inhibits the Wnt/β-catenin signaling pathway. (A) The Topflash reporter was used to detect the effect of PANK1 on the transcriptional activity of β-catenin. After transfection, the cells were stimulated by lithium chloride or <t>Wnt3a</t> for 8h before the measurement of the reporter activity. (B) The effect of overexpression of PANK1 on the level of β-catenin protein in PVTT and QGY-7701 cells was measured. After the cells were stimulated by Wnt3a for different periods of time, the β-catenin protein was measured by western blot. (C) The effect of knocked-down expression of PANK1 on the level of β-catenin protein in Huh7 and QGY-7701 cells was measured. After the cells were stimulated by Wnt3a for different periods of time, the β-catenin protein was measured by western blot. (D-E) The effect of overexpression of PANK1 in Huh7 and QGY-7701 cells on the half-life of β-catenin protein level was measured. After the cells were stimulated by CHX (50µg/ml) for different periods of time, the β-catenin protein was measured by western blot. The levels of β-catenin protein were quantified and analyze. (F) The effect of PANK1 overexpression in PVTT and QGY-7701 cells on the mRNA level of Axin2 was measured. After being stimulated by Wnt3a for different periods of time, the cells were collected to measure the mRNA level of Axin2. (G) The effect of knocked-down expression of PANK1 in Huh7 and QGY-7701 cells on the mRNA levels of Axin2 was measured. After the cells were stimulated by Wnt3a for different periods of time, they were collected to measure the mRNA level of Axin2. (H) RNA sequencing was performed on Huh7 cells with the knockdown of PANK1 expression, and on control cells, obtaining a volcano plot. (I) Differential expression of target genes of the Wnt/β-catenin signaling pathway from RNA sequencing, shown as a heat map. (J) As shown in the GEPIA database, PANK1 expression is negatively correlated with expression of Axin and SOX9, the target genes of Wnt/β-catenin signaling pathway. ****, P <0.0001.
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    ATCC l wnt3a
    Mouse <t>L-Wnt3a</t> cells were cultured according to ATCC recommendations. Cells were then transfected with TOPflash or vector control and treated with Vehicle (DMSO), 5 μM IWP-2, or 10 μM IWP-2. Three days later a luciferase assay was performed and data was normalized to vector control. Data is representative of three separate experiments. *p≤0.05 in comparison to vehicle.
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    ATCC mouse l1 cells expressing wnt3a
    Luciferase activity in CHO cells transfected with WT-LRP5 or mutant LRP5 in the presence of <t>Wnt3a-CM</t> (white bars) or L1 control medium (grey bars) . The activities of the signaling pathway are presented in relative luciferase units (RLU) determined by the ratio between the luciferase and β-galactosidase activities and given as a fold change relative to corresponding samples treated with 10% FBS-DMEM. * p < 0.05, ** p < 0.01 as compared with WT-LRP5. Results are expressed as mean ± SD.
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    ATCC l wnt 3a cells
    Luciferase activity in CHO cells transfected with WT-LRP5 or mutant LRP5 in the presence of <t>Wnt3a-CM</t> (white bars) or L1 control medium (grey bars) . The activities of the signaling pathway are presented in relative luciferase units (RLU) determined by the ratio between the luciferase and β-galactosidase activities and given as a fold change relative to corresponding samples treated with 10% FBS-DMEM. * p < 0.05, ** p < 0.01 as compared with WT-LRP5. Results are expressed as mean ± SD.
    L Wnt 3a Cells, supplied by ATCC, used in various techniques. Bioz Stars score: 99/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Image Search Results


    PANK1 inhibits the Wnt/β-catenin signaling pathway. (A) The Topflash reporter was used to detect the effect of PANK1 on the transcriptional activity of β-catenin. After transfection, the cells were stimulated by lithium chloride or Wnt3a for 8h before the measurement of the reporter activity. (B) The effect of overexpression of PANK1 on the level of β-catenin protein in PVTT and QGY-7701 cells was measured. After the cells were stimulated by Wnt3a for different periods of time, the β-catenin protein was measured by western blot. (C) The effect of knocked-down expression of PANK1 on the level of β-catenin protein in Huh7 and QGY-7701 cells was measured. After the cells were stimulated by Wnt3a for different periods of time, the β-catenin protein was measured by western blot. (D-E) The effect of overexpression of PANK1 in Huh7 and QGY-7701 cells on the half-life of β-catenin protein level was measured. After the cells were stimulated by CHX (50µg/ml) for different periods of time, the β-catenin protein was measured by western blot. The levels of β-catenin protein were quantified and analyze. (F) The effect of PANK1 overexpression in PVTT and QGY-7701 cells on the mRNA level of Axin2 was measured. After being stimulated by Wnt3a for different periods of time, the cells were collected to measure the mRNA level of Axin2. (G) The effect of knocked-down expression of PANK1 in Huh7 and QGY-7701 cells on the mRNA levels of Axin2 was measured. After the cells were stimulated by Wnt3a for different periods of time, they were collected to measure the mRNA level of Axin2. (H) RNA sequencing was performed on Huh7 cells with the knockdown of PANK1 expression, and on control cells, obtaining a volcano plot. (I) Differential expression of target genes of the Wnt/β-catenin signaling pathway from RNA sequencing, shown as a heat map. (J) As shown in the GEPIA database, PANK1 expression is negatively correlated with expression of Axin and SOX9, the target genes of Wnt/β-catenin signaling pathway. ****, P <0.0001.

    Journal: International Journal of Biological Sciences

    Article Title: Pantothenate Kinase 1 Inhibits the Progression of Hepatocellular Carcinoma by Negatively Regulating Wnt/β-catenin Signaling

    doi: 10.7150/ijbs.67842

    Figure Lengend Snippet: PANK1 inhibits the Wnt/β-catenin signaling pathway. (A) The Topflash reporter was used to detect the effect of PANK1 on the transcriptional activity of β-catenin. After transfection, the cells were stimulated by lithium chloride or Wnt3a for 8h before the measurement of the reporter activity. (B) The effect of overexpression of PANK1 on the level of β-catenin protein in PVTT and QGY-7701 cells was measured. After the cells were stimulated by Wnt3a for different periods of time, the β-catenin protein was measured by western blot. (C) The effect of knocked-down expression of PANK1 on the level of β-catenin protein in Huh7 and QGY-7701 cells was measured. After the cells were stimulated by Wnt3a for different periods of time, the β-catenin protein was measured by western blot. (D-E) The effect of overexpression of PANK1 in Huh7 and QGY-7701 cells on the half-life of β-catenin protein level was measured. After the cells were stimulated by CHX (50µg/ml) for different periods of time, the β-catenin protein was measured by western blot. The levels of β-catenin protein were quantified and analyze. (F) The effect of PANK1 overexpression in PVTT and QGY-7701 cells on the mRNA level of Axin2 was measured. After being stimulated by Wnt3a for different periods of time, the cells were collected to measure the mRNA level of Axin2. (G) The effect of knocked-down expression of PANK1 in Huh7 and QGY-7701 cells on the mRNA levels of Axin2 was measured. After the cells were stimulated by Wnt3a for different periods of time, they were collected to measure the mRNA level of Axin2. (H) RNA sequencing was performed on Huh7 cells with the knockdown of PANK1 expression, and on control cells, obtaining a volcano plot. (I) Differential expression of target genes of the Wnt/β-catenin signaling pathway from RNA sequencing, shown as a heat map. (J) As shown in the GEPIA database, PANK1 expression is negatively correlated with expression of Axin and SOX9, the target genes of Wnt/β-catenin signaling pathway. ****, P <0.0001.

    Article Snippet: The Wnt3a conditional medium was prepared from the L-Wnt3a cells according to the method from the ATCC.

    Techniques: Activity Assay, Transfection, Over Expression, Western Blot, Expressing, RNA Sequencing Assay

    PANK1 phosphorylates the N-terminal serine and threonine residues of β-catenin. (A) The effect of knockdown or overexpression of PANK1 in Huh7 and QGY-7701 cells on the phosphorylation level of β-catenin was measured. After the cells were stimulated by Wnt3a for different periods of time, the phosphorylation level of β-catenin was measured by western blot. (B) Ubiquitin assay was performed to measure the effect of PANK1 expression on the ubiquitination level of β-catenin. After being treated with MG132 for 10h, the PVTT cells with overexpressed PANK1, Huh7 cells, with down-regulated expression of PANK1, and their respective control cells were lysed for supernatant collection. The antibody against β-catenin was used for CO-IP. Then, a western blot assay was performed, and the antibody against ubiquitin was used for measurement. (C) The interaction between exogenously expressed CK1α (Myc-CK1α) and PANK1 (Flag-PANK1) was measured in 293T cells. The Myc-CK1α and Flag-PANK1 plasmids were transiently transfected into 293T cells. 48h later, CO-IP was performed with an antibody against Myc or the Flag tag. (D) The interaction between endogenous CK1α and PANK1 in Huh7 and QGY-7701 cells was measured. (E) The Wnt3a stimulation-dependent interaction between CK1α and PANK1 in QGY-7701 cells was measured. After treatment with Wnt3a for different periods of time, the QGY-7701 cells with the overexpression PANK1 were lysed and centrifuged for supernatant collection. The antibody against Flag was used for CO-IP. (F) The phosphorylation of β-catenin by PANK was measured through the in vitro kinase reaction. See “Materials and Methods” for the details on the reaction.

    Journal: International Journal of Biological Sciences

    Article Title: Pantothenate Kinase 1 Inhibits the Progression of Hepatocellular Carcinoma by Negatively Regulating Wnt/β-catenin Signaling

    doi: 10.7150/ijbs.67842

    Figure Lengend Snippet: PANK1 phosphorylates the N-terminal serine and threonine residues of β-catenin. (A) The effect of knockdown or overexpression of PANK1 in Huh7 and QGY-7701 cells on the phosphorylation level of β-catenin was measured. After the cells were stimulated by Wnt3a for different periods of time, the phosphorylation level of β-catenin was measured by western blot. (B) Ubiquitin assay was performed to measure the effect of PANK1 expression on the ubiquitination level of β-catenin. After being treated with MG132 for 10h, the PVTT cells with overexpressed PANK1, Huh7 cells, with down-regulated expression of PANK1, and their respective control cells were lysed for supernatant collection. The antibody against β-catenin was used for CO-IP. Then, a western blot assay was performed, and the antibody against ubiquitin was used for measurement. (C) The interaction between exogenously expressed CK1α (Myc-CK1α) and PANK1 (Flag-PANK1) was measured in 293T cells. The Myc-CK1α and Flag-PANK1 plasmids were transiently transfected into 293T cells. 48h later, CO-IP was performed with an antibody against Myc or the Flag tag. (D) The interaction between endogenous CK1α and PANK1 in Huh7 and QGY-7701 cells was measured. (E) The Wnt3a stimulation-dependent interaction between CK1α and PANK1 in QGY-7701 cells was measured. After treatment with Wnt3a for different periods of time, the QGY-7701 cells with the overexpression PANK1 were lysed and centrifuged for supernatant collection. The antibody against Flag was used for CO-IP. (F) The phosphorylation of β-catenin by PANK was measured through the in vitro kinase reaction. See “Materials and Methods” for the details on the reaction.

    Article Snippet: The Wnt3a conditional medium was prepared from the L-Wnt3a cells according to the method from the ATCC.

    Techniques: Over Expression, Western Blot, Ubiquitin Assay, Expressing, Co-Immunoprecipitation Assay, Transfection, FLAG-tag, In Vitro

    Mouse L-Wnt3a cells were cultured according to ATCC recommendations. Cells were then transfected with TOPflash or vector control and treated with Vehicle (DMSO), 5 μM IWP-2, or 10 μM IWP-2. Three days later a luciferase assay was performed and data was normalized to vector control. Data is representative of three separate experiments. *p≤0.05 in comparison to vehicle.

    Journal: PLoS ONE

    Article Title: Porcupine Is Not Required for the Production of the Majority of Wnts from Primary Human Astrocytes and CD8+ T Cells

    doi: 10.1371/journal.pone.0092159

    Figure Lengend Snippet: Mouse L-Wnt3a cells were cultured according to ATCC recommendations. Cells were then transfected with TOPflash or vector control and treated with Vehicle (DMSO), 5 μM IWP-2, or 10 μM IWP-2. Three days later a luciferase assay was performed and data was normalized to vector control. Data is representative of three separate experiments. *p≤0.05 in comparison to vehicle.

    Article Snippet: L-Wnt3a (ATCC CRL-2647) were cultured in complete DMEM with 0.4 mg/ml G-418.

    Techniques: Cell Culture, Transfection, Plasmid Preparation, Luciferase

    Luciferase activity in CHO cells transfected with WT-LRP5 or mutant LRP5 in the presence of Wnt3a-CM (white bars) or L1 control medium (grey bars) . The activities of the signaling pathway are presented in relative luciferase units (RLU) determined by the ratio between the luciferase and β-galactosidase activities and given as a fold change relative to corresponding samples treated with 10% FBS-DMEM. * p < 0.05, ** p < 0.01 as compared with WT-LRP5. Results are expressed as mean ± SD.

    Journal: BMC Medical Genetics

    Article Title: Mutations in LRP5 cause primary osteoporosis without features of OI by reducing Wnt signaling activity

    doi: 10.1186/1471-2350-13-26

    Figure Lengend Snippet: Luciferase activity in CHO cells transfected with WT-LRP5 or mutant LRP5 in the presence of Wnt3a-CM (white bars) or L1 control medium (grey bars) . The activities of the signaling pathway are presented in relative luciferase units (RLU) determined by the ratio between the luciferase and β-galactosidase activities and given as a fold change relative to corresponding samples treated with 10% FBS-DMEM. * p < 0.05, ** p < 0.01 as compared with WT-LRP5. Results are expressed as mean ± SD.

    Article Snippet: Wnt3a-conditioned medium was produced and collected from mouse L1 cells expressing Wnt3a (L Wnt3a; ATCC CRL-2647) according to the manufacturer's instructions.

    Techniques: Luciferase, Activity Assay, Transfection, Mutagenesis

    A) Tph1 gene expression and B) 5- Htr1b gene expression in CHO cells transfected with wild type LRP5 (WT-LRP5) or mutant LRP5 and treated with Wnt3a-CM or L1-CM . Expression of the Tph1 and 5- Htr1b genes is shown as a fold change relative to the untreated control (pcDNA3.1+) and normalized to β-actin . The effects of the LRP5 mutants on the expression of these genes were examined by comparing the results for the mutants with those for WT-LRP5 using Student's t test. The statistical significance of each pair is denoted below the mutant columns; ** p < 0.01 as compared to WT-LRP5. Results are expressed as mean ± SD.

    Journal: BMC Medical Genetics

    Article Title: Mutations in LRP5 cause primary osteoporosis without features of OI by reducing Wnt signaling activity

    doi: 10.1186/1471-2350-13-26

    Figure Lengend Snippet: A) Tph1 gene expression and B) 5- Htr1b gene expression in CHO cells transfected with wild type LRP5 (WT-LRP5) or mutant LRP5 and treated with Wnt3a-CM or L1-CM . Expression of the Tph1 and 5- Htr1b genes is shown as a fold change relative to the untreated control (pcDNA3.1+) and normalized to β-actin . The effects of the LRP5 mutants on the expression of these genes were examined by comparing the results for the mutants with those for WT-LRP5 using Student's t test. The statistical significance of each pair is denoted below the mutant columns; ** p < 0.01 as compared to WT-LRP5. Results are expressed as mean ± SD.

    Article Snippet: Wnt3a-conditioned medium was produced and collected from mouse L1 cells expressing Wnt3a (L Wnt3a; ATCC CRL-2647) according to the manufacturer's instructions.

    Techniques: Expressing, Transfection, Mutagenesis