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transblot sd unit  (Bio-Rad)


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    Bio-Rad transblot sd unit
    (A) Plasma membrane proteins were isolated from MCF10A cells cultured with insulin (5 µg/ml) and MCF10HER2 cells cultured without insulin. Isolated membrane proteins were probed for GLUT1, GLUT3 and GLUT4. Transferrin receptor was used as a plasma membrane loading control. Amounts of plasma membrane-localized GLUT1 and GLUT3 appeared to be similar in both samples. Although levels of the insulin-responsive transporter GLUT4 were higher in membrane preparations from MCF10A cells cultured in the presence of insulin, GLUT4 was readily detectable at the plasma membrane in MCF10HER2 cells maintained long-term in the absence of insulin in serum-free media. (B) MCF10HER2 cells were maintained in serum-free media with out insulin and MCF10A cells were incubated for 18 hours in the absence of insulin in serum-free media, then both cell lines were cultured with or without insulin for 30 minutes. Plasma membrane localized proteins were harvested and probed for GLUT4. In MCF10HER2 cells cultured without insulin basal levels of plasma membrane localized GLUT4 were calculated to be 44% higher than basal GLUT4 plasma membrane levels in MCF10A cells cultured without insulin. In both cell types, insulin induced an increase in GLUT4 at the plasma membrane. The highest levels were observed in the MCF10HER2 cells plus insulin condition. (C) bands in (B) were quantified (optical density) by Quantity One software from <t>Bio-Rad</t> Laboratories. Levels of GLUT4 were normalized to transferrin receptor levels in each context and expressed as a ratio. Relative normalized expression is compared to MCF10A minus-insulin results.
    Transblot Sd Unit, supplied by Bio-Rad, used in various techniques. Bioz Stars score: 90/100, based on 1520 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/transblot sd unit/product/Bio-Rad
    Average 90 stars, based on 1520 article reviews
    transblot sd unit - by Bioz Stars, 2026-03
    90/100 stars

    Images

    1) Product Images from "Oncogene Activation Induces Metabolic Transformation Resulting in Insulin-Independence in Human Breast Cancer Cells"

    Article Title: Oncogene Activation Induces Metabolic Transformation Resulting in Insulin-Independence in Human Breast Cancer Cells

    Journal: PLoS ONE

    doi: 10.1371/journal.pone.0017959

    (A) Plasma membrane proteins were isolated from MCF10A cells cultured with insulin (5 µg/ml) and MCF10HER2 cells cultured without insulin. Isolated membrane proteins were probed for GLUT1, GLUT3 and GLUT4. Transferrin receptor was used as a plasma membrane loading control. Amounts of plasma membrane-localized GLUT1 and GLUT3 appeared to be similar in both samples. Although levels of the insulin-responsive transporter GLUT4 were higher in membrane preparations from MCF10A cells cultured in the presence of insulin, GLUT4 was readily detectable at the plasma membrane in MCF10HER2 cells maintained long-term in the absence of insulin in serum-free media. (B) MCF10HER2 cells were maintained in serum-free media with out insulin and MCF10A cells were incubated for 18 hours in the absence of insulin in serum-free media, then both cell lines were cultured with or without insulin for 30 minutes. Plasma membrane localized proteins were harvested and probed for GLUT4. In MCF10HER2 cells cultured without insulin basal levels of plasma membrane localized GLUT4 were calculated to be 44% higher than basal GLUT4 plasma membrane levels in MCF10A cells cultured without insulin. In both cell types, insulin induced an increase in GLUT4 at the plasma membrane. The highest levels were observed in the MCF10HER2 cells plus insulin condition. (C) bands in (B) were quantified (optical density) by Quantity One software from Bio-Rad Laboratories. Levels of GLUT4 were normalized to transferrin receptor levels in each context and expressed as a ratio. Relative normalized expression is compared to MCF10A minus-insulin results.
    Figure Legend Snippet: (A) Plasma membrane proteins were isolated from MCF10A cells cultured with insulin (5 µg/ml) and MCF10HER2 cells cultured without insulin. Isolated membrane proteins were probed for GLUT1, GLUT3 and GLUT4. Transferrin receptor was used as a plasma membrane loading control. Amounts of plasma membrane-localized GLUT1 and GLUT3 appeared to be similar in both samples. Although levels of the insulin-responsive transporter GLUT4 were higher in membrane preparations from MCF10A cells cultured in the presence of insulin, GLUT4 was readily detectable at the plasma membrane in MCF10HER2 cells maintained long-term in the absence of insulin in serum-free media. (B) MCF10HER2 cells were maintained in serum-free media with out insulin and MCF10A cells were incubated for 18 hours in the absence of insulin in serum-free media, then both cell lines were cultured with or without insulin for 30 minutes. Plasma membrane localized proteins were harvested and probed for GLUT4. In MCF10HER2 cells cultured without insulin basal levels of plasma membrane localized GLUT4 were calculated to be 44% higher than basal GLUT4 plasma membrane levels in MCF10A cells cultured without insulin. In both cell types, insulin induced an increase in GLUT4 at the plasma membrane. The highest levels were observed in the MCF10HER2 cells plus insulin condition. (C) bands in (B) were quantified (optical density) by Quantity One software from Bio-Rad Laboratories. Levels of GLUT4 were normalized to transferrin receptor levels in each context and expressed as a ratio. Relative normalized expression is compared to MCF10A minus-insulin results.

    Techniques Used: Isolation, Cell Culture, Incubation, Software, Expressing



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    transblot sd unit  (Bio-Rad)
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    Bio-Rad transblot sd unit
    (A) Plasma membrane proteins were isolated from MCF10A cells cultured with insulin (5 µg/ml) and MCF10HER2 cells cultured without insulin. Isolated membrane proteins were probed for GLUT1, GLUT3 and GLUT4. Transferrin receptor was used as a plasma membrane loading control. Amounts of plasma membrane-localized GLUT1 and GLUT3 appeared to be similar in both samples. Although levels of the insulin-responsive transporter GLUT4 were higher in membrane preparations from MCF10A cells cultured in the presence of insulin, GLUT4 was readily detectable at the plasma membrane in MCF10HER2 cells maintained long-term in the absence of insulin in serum-free media. (B) MCF10HER2 cells were maintained in serum-free media with out insulin and MCF10A cells were incubated for 18 hours in the absence of insulin in serum-free media, then both cell lines were cultured with or without insulin for 30 minutes. Plasma membrane localized proteins were harvested and probed for GLUT4. In MCF10HER2 cells cultured without insulin basal levels of plasma membrane localized GLUT4 were calculated to be 44% higher than basal GLUT4 plasma membrane levels in MCF10A cells cultured without insulin. In both cell types, insulin induced an increase in GLUT4 at the plasma membrane. The highest levels were observed in the MCF10HER2 cells plus insulin condition. (C) bands in (B) were quantified (optical density) by Quantity One software from <t>Bio-Rad</t> Laboratories. Levels of GLUT4 were normalized to transferrin receptor levels in each context and expressed as a ratio. Relative normalized expression is compared to MCF10A minus-insulin results.
    Transblot Sd Unit, supplied by Bio-Rad, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/transblot sd unit/product/Bio-Rad
    Average 90 stars, based on 1 article reviews
    transblot sd unit - by Bioz Stars, 2026-03
    90/100 stars
    		  Buy from Supplier
    transblot sd semi-dry transfer unit  (Bio-Rad)
    90
    Bio-Rad transblot sd semi-dry transfer unit
    (A) Plasma membrane proteins were isolated from MCF10A cells cultured with insulin (5 µg/ml) and MCF10HER2 cells cultured without insulin. Isolated membrane proteins were probed for GLUT1, GLUT3 and GLUT4. Transferrin receptor was used as a plasma membrane loading control. Amounts of plasma membrane-localized GLUT1 and GLUT3 appeared to be similar in both samples. Although levels of the insulin-responsive transporter GLUT4 were higher in membrane preparations from MCF10A cells cultured in the presence of insulin, GLUT4 was readily detectable at the plasma membrane in MCF10HER2 cells maintained long-term in the absence of insulin in serum-free media. (B) MCF10HER2 cells were maintained in serum-free media with out insulin and MCF10A cells were incubated for 18 hours in the absence of insulin in serum-free media, then both cell lines were cultured with or without insulin for 30 minutes. Plasma membrane localized proteins were harvested and probed for GLUT4. In MCF10HER2 cells cultured without insulin basal levels of plasma membrane localized GLUT4 were calculated to be 44% higher than basal GLUT4 plasma membrane levels in MCF10A cells cultured without insulin. In both cell types, insulin induced an increase in GLUT4 at the plasma membrane. The highest levels were observed in the MCF10HER2 cells plus insulin condition. (C) bands in (B) were quantified (optical density) by Quantity One software from <t>Bio-Rad</t> Laboratories. Levels of GLUT4 were normalized to transferrin receptor levels in each context and expressed as a ratio. Relative normalized expression is compared to MCF10A minus-insulin results.
    Transblot Sd Semi Dry Transfer Unit, supplied by Bio-Rad, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/transblot sd semi-dry transfer unit/product/Bio-Rad
    Average 90 stars, based on 1 article reviews
    transblot sd semi-dry transfer unit - by Bioz Stars, 2026-03
    90/100 stars
    		  Buy from Supplier

    Image Search Results


    (A) Plasma membrane proteins were isolated from MCF10A cells cultured with insulin (5 µg/ml) and MCF10HER2 cells cultured without insulin. Isolated membrane proteins were probed for GLUT1, GLUT3 and GLUT4. Transferrin receptor was used as a plasma membrane loading control. Amounts of plasma membrane-localized GLUT1 and GLUT3 appeared to be similar in both samples. Although levels of the insulin-responsive transporter GLUT4 were higher in membrane preparations from MCF10A cells cultured in the presence of insulin, GLUT4 was readily detectable at the plasma membrane in MCF10HER2 cells maintained long-term in the absence of insulin in serum-free media. (B) MCF10HER2 cells were maintained in serum-free media with out insulin and MCF10A cells were incubated for 18 hours in the absence of insulin in serum-free media, then both cell lines were cultured with or without insulin for 30 minutes. Plasma membrane localized proteins were harvested and probed for GLUT4. In MCF10HER2 cells cultured without insulin basal levels of plasma membrane localized GLUT4 were calculated to be 44% higher than basal GLUT4 plasma membrane levels in MCF10A cells cultured without insulin. In both cell types, insulin induced an increase in GLUT4 at the plasma membrane. The highest levels were observed in the MCF10HER2 cells plus insulin condition. (C) bands in (B) were quantified (optical density) by Quantity One software from Bio-Rad Laboratories. Levels of GLUT4 were normalized to transferrin receptor levels in each context and expressed as a ratio. Relative normalized expression is compared to MCF10A minus-insulin results.

    Journal: PLoS ONE

    Article Title: Oncogene Activation Induces Metabolic Transformation Resulting in Insulin-Independence in Human Breast Cancer Cells

    doi: 10.1371/journal.pone.0017959

    Figure Lengend Snippet: (A) Plasma membrane proteins were isolated from MCF10A cells cultured with insulin (5 µg/ml) and MCF10HER2 cells cultured without insulin. Isolated membrane proteins were probed for GLUT1, GLUT3 and GLUT4. Transferrin receptor was used as a plasma membrane loading control. Amounts of plasma membrane-localized GLUT1 and GLUT3 appeared to be similar in both samples. Although levels of the insulin-responsive transporter GLUT4 were higher in membrane preparations from MCF10A cells cultured in the presence of insulin, GLUT4 was readily detectable at the plasma membrane in MCF10HER2 cells maintained long-term in the absence of insulin in serum-free media. (B) MCF10HER2 cells were maintained in serum-free media with out insulin and MCF10A cells were incubated for 18 hours in the absence of insulin in serum-free media, then both cell lines were cultured with or without insulin for 30 minutes. Plasma membrane localized proteins were harvested and probed for GLUT4. In MCF10HER2 cells cultured without insulin basal levels of plasma membrane localized GLUT4 were calculated to be 44% higher than basal GLUT4 plasma membrane levels in MCF10A cells cultured without insulin. In both cell types, insulin induced an increase in GLUT4 at the plasma membrane. The highest levels were observed in the MCF10HER2 cells plus insulin condition. (C) bands in (B) were quantified (optical density) by Quantity One software from Bio-Rad Laboratories. Levels of GLUT4 were normalized to transferrin receptor levels in each context and expressed as a ratio. Relative normalized expression is compared to MCF10A minus-insulin results.

    Article Snippet: IR and IGF-IR immunoprecipitates (50% of eluent), whole cell lysates (100 ug) and isolated cell surface proteins (25 ug) were separated on a 7.5% SDS-polyacrylamide gels and transferred to PVDF membranes by semi-dry electrophoretic transfer with a Bio-Rad Transblot SD unit.

    Techniques: Isolation, Cell Culture, Incubation, Software, Expressing