trans blot 1703940 semi dry transfer apparatus Search Results


semidry electroblotting system  (Bio-Rad)
99
Bio-Rad semidry electroblotting system
Semidry Electroblotting System, supplied by Bio-Rad, 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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extra thick blot paper™  (Bio-Rad)
90
Bio-Rad extra thick blot paper™
Extra Thick Blot Paper™, 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
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transblot sd unit  (Bio-Rad)
90
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
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semidry transfer blot  (Bio-Rad)
90
Bio-Rad semidry transfer blot
(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.
Semidry Transfer Blot, 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
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lav blot ii  (Bio-Rad)
90
Bio-Rad lav blot ii
(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.
Lav Blot Ii, 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
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semidry transfer apparatus  (Bio-Rad)
96
Bio-Rad semidry transfer apparatus
(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.
Semidry Transfer Apparatus, supplied by Bio-Rad, used in various techniques. Bioz Stars score: 96/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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0.45-μm nitrocellulose membrane  (Thermo Fisher)
90
Thermo Fisher 0.45-μm nitrocellulose membrane
(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.
0.45 μm Nitrocellulose Membrane, supplied by Thermo Fisher, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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mini trans-blotter  (Bio-Rad)
90
Bio-Rad mini trans-blotter
(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.
Mini Trans Blotter, 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
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lav blot  (Bio-Rad)
90
Bio-Rad lav blot
(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.
Lav Blot, 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
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tran-blot  (Bio-Rad)
90
Bio-Rad tran-blot
(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.
Tran Blot, 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
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transfer blot apparatus  (Bio-Rad)
90
Bio-Rad transfer blot apparatus
(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.
Transfer Blot Apparatus, 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
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heat sealer  (Bio-Rad)
93
Bio-Rad heat sealer
(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.
Heat Sealer, supplied by Bio-Rad, used in various techniques. Bioz Stars score: 93/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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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