standard denaturing sds page procedures Search Results


pre stained protein ladder  (New England Biolabs)
95
New England Biolabs pre stained protein ladder
Pre Stained Protein Ladder, supplied by New England Biolabs, used in various techniques. Bioz Stars score: 95/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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polyacrylamide gel electrophoresis  (Bio-Rad)
98
Bio-Rad polyacrylamide gel electrophoresis
Polyacrylamide Gel Electrophoresis, supplied by Bio-Rad, used in various techniques. Bioz Stars score: 98/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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sds polyacrylamide gels  (Bio-Rad)
96
Bio-Rad sds polyacrylamide gels
Sds Polyacrylamide Gels, 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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polyacrylamide gels  (Bio-Rad)
97
Bio-Rad polyacrylamide gels
[α-sec-EAP] and [unselected proteins,UP] secreted by E(M) are >50 and upto 4 fold higher than those secreted by E(P). (Figure 5 a ) Incubation of the panel of cultures, shown in Figure (with the exception of E(M9)-B, in lane 6) was for 170 hours with supplementation of methanol inducer at 24 hour intervals. Culture supernatants were harvested as determine in the materials and methods. Aliquots (20 μL) of cultures of E(P), h-V, H, E(M9)-B, EM32)-A,-B,-C,-D and E(M44)-A,-B were loaded in the order shown above the lanes (lanes 3–12) and co-electrophoresed with broad range markers (lane 1) and EAP purified from E.coli (0.08 units/lane, lanes2) through denaturing (4%-20%) <t>polyacrylamide</t> gradient gels with Laemmli electrophoresis buffer. The gel was stained with Gel Code Blue (GCB) scanned and saved as TIFF files. The respective ROIs of proteins corresponding to EAP, α-sec-EAP, unselected protein-1 (UP1) and unselected protein 3 (UP3) are identified and color coded on the left and right of the gel. The ROIs corresponding to the above 4 proteins were densitometrically scanned and normalized to UP3 in lane 3 and plotted as their respective ratios to E(P). Normalized ROIs corresponding to EAP, α-sec-EAP and HSA in E(P), v-H, H and E(M) were plotted with Excel programs (Figure 5 b ). Normalized ROIs corresponding to UP1 and UP3 were plotted as their ratios in EAP/E(P), E(P)/E(P), v-H/E(P), H/E(P) and all E(M)/E(P) (Figure 5 c , 5 d ).
Polyacrylamide Gels, supplied by Bio-Rad, used in various techniques. Bioz Stars score: 97/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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sds page procedures  (Bio-Rad)
95
Bio-Rad sds page procedures
[α-sec-EAP] and [unselected proteins,UP] secreted by E(M) are >50 and upto 4 fold higher than those secreted by E(P). (Figure 5 a ) Incubation of the panel of cultures, shown in Figure (with the exception of E(M9)-B, in lane 6) was for 170 hours with supplementation of methanol inducer at 24 hour intervals. Culture supernatants were harvested as determine in the materials and methods. Aliquots (20 μL) of cultures of E(P), h-V, H, E(M9)-B, EM32)-A,-B,-C,-D and E(M44)-A,-B were loaded in the order shown above the lanes (lanes 3–12) and co-electrophoresed with broad range markers (lane 1) and EAP purified from E.coli (0.08 units/lane, lanes2) through denaturing (4%-20%) <t>polyacrylamide</t> gradient gels with Laemmli electrophoresis buffer. The gel was stained with Gel Code Blue (GCB) scanned and saved as TIFF files. The respective ROIs of proteins corresponding to EAP, α-sec-EAP, unselected protein-1 (UP1) and unselected protein 3 (UP3) are identified and color coded on the left and right of the gel. The ROIs corresponding to the above 4 proteins were densitometrically scanned and normalized to UP3 in lane 3 and plotted as their respective ratios to E(P). Normalized ROIs corresponding to EAP, α-sec-EAP and HSA in E(P), v-H, H and E(M) were plotted with Excel programs (Figure 5 b ). Normalized ROIs corresponding to UP1 and UP3 were plotted as their ratios in EAP/E(P), E(P)/E(P), v-H/E(P), H/E(P) and all E(M)/E(P) (Figure 5 c , 5 d ).
Sds Page Procedures, supplied by Bio-Rad, used in various techniques. Bioz Stars score: 95/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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prehybridization buffer  (Thermo Fisher)
99
Thermo Fisher prehybridization buffer
[α-sec-EAP] and [unselected proteins,UP] secreted by E(M) are >50 and upto 4 fold higher than those secreted by E(P). (Figure 5 a ) Incubation of the panel of cultures, shown in Figure (with the exception of E(M9)-B, in lane 6) was for 170 hours with supplementation of methanol inducer at 24 hour intervals. Culture supernatants were harvested as determine in the materials and methods. Aliquots (20 μL) of cultures of E(P), h-V, H, E(M9)-B, EM32)-A,-B,-C,-D and E(M44)-A,-B were loaded in the order shown above the lanes (lanes 3–12) and co-electrophoresed with broad range markers (lane 1) and EAP purified from E.coli (0.08 units/lane, lanes2) through denaturing (4%-20%) <t>polyacrylamide</t> gradient gels with Laemmli electrophoresis buffer. The gel was stained with Gel Code Blue (GCB) scanned and saved as TIFF files. The respective ROIs of proteins corresponding to EAP, α-sec-EAP, unselected protein-1 (UP1) and unselected protein 3 (UP3) are identified and color coded on the left and right of the gel. The ROIs corresponding to the above 4 proteins were densitometrically scanned and normalized to UP3 in lane 3 and plotted as their respective ratios to E(P). Normalized ROIs corresponding to EAP, α-sec-EAP and HSA in E(P), v-H, H and E(M) were plotted with Excel programs (Figure 5 b ). Normalized ROIs corresponding to UP1 and UP3 were plotted as their ratios in EAP/E(P), E(P)/E(P), v-H/E(P), H/E(P) and all E(M)/E(P) (Figure 5 c , 5 d ).
Prehybridization Buffer, supplied by Thermo Fisher, 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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c protein extracts  (Bio-Rad)
99
Bio-Rad c protein extracts
[α-sec-EAP] and [unselected proteins,UP] secreted by E(M) are >50 and upto 4 fold higher than those secreted by E(P). (Figure 5 a ) Incubation of the panel of cultures, shown in Figure (with the exception of E(M9)-B, in lane 6) was for 170 hours with supplementation of methanol inducer at 24 hour intervals. Culture supernatants were harvested as determine in the materials and methods. Aliquots (20 μL) of cultures of E(P), h-V, H, E(M9)-B, EM32)-A,-B,-C,-D and E(M44)-A,-B were loaded in the order shown above the lanes (lanes 3–12) and co-electrophoresed with broad range markers (lane 1) and EAP purified from E.coli (0.08 units/lane, lanes2) through denaturing (4%-20%) <t>polyacrylamide</t> gradient gels with Laemmli electrophoresis buffer. The gel was stained with Gel Code Blue (GCB) scanned and saved as TIFF files. The respective ROIs of proteins corresponding to EAP, α-sec-EAP, unselected protein-1 (UP1) and unselected protein 3 (UP3) are identified and color coded on the left and right of the gel. The ROIs corresponding to the above 4 proteins were densitometrically scanned and normalized to UP3 in lane 3 and plotted as their respective ratios to E(P). Normalized ROIs corresponding to EAP, α-sec-EAP and HSA in E(P), v-H, H and E(M) were plotted with Excel programs (Figure 5 b ). Normalized ROIs corresponding to UP1 and UP3 were plotted as their ratios in EAP/E(P), E(P)/E(P), v-H/E(P), H/E(P) and all E(M)/E(P) (Figure 5 c , 5 d ).
C Protein Extracts, 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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denaturing sodium dodecyl sulfate ‒ polyacrylamide gel electrophoresis  (Bio-Rad)
97
Bio-Rad denaturing sodium dodecyl sulfate ‒ polyacrylamide gel electrophoresis
[α-sec-EAP] and [unselected proteins,UP] secreted by E(M) are >50 and upto 4 fold higher than those secreted by E(P). (Figure 5 a ) Incubation of the panel of cultures, shown in Figure (with the exception of E(M9)-B, in lane 6) was for 170 hours with supplementation of methanol inducer at 24 hour intervals. Culture supernatants were harvested as determine in the materials and methods. Aliquots (20 μL) of cultures of E(P), h-V, H, E(M9)-B, EM32)-A,-B,-C,-D and E(M44)-A,-B were loaded in the order shown above the lanes (lanes 3–12) and co-electrophoresed with broad range markers (lane 1) and EAP purified from E.coli (0.08 units/lane, lanes2) through denaturing (4%-20%) <t>polyacrylamide</t> gradient gels with Laemmli electrophoresis buffer. The gel was stained with Gel Code Blue (GCB) scanned and saved as TIFF files. The respective ROIs of proteins corresponding to EAP, α-sec-EAP, unselected protein-1 (UP1) and unselected protein 3 (UP3) are identified and color coded on the left and right of the gel. The ROIs corresponding to the above 4 proteins were densitometrically scanned and normalized to UP3 in lane 3 and plotted as their respective ratios to E(P). Normalized ROIs corresponding to EAP, α-sec-EAP and HSA in E(P), v-H, H and E(M) were plotted with Excel programs (Figure 5 b ). Normalized ROIs corresponding to UP1 and UP3 were plotted as their ratios in EAP/E(P), E(P)/E(P), v-H/E(P), H/E(P) and all E(M)/E(P) (Figure 5 c , 5 d ).
Denaturing Sodium Dodecyl Sulfate ‒ Polyacrylamide Gel Electrophoresis, supplied by Bio-Rad, used in various techniques. Bioz Stars score: 97/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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sds page gels  (Bio-Rad)
99
Bio-Rad sds page gels
[α-sec-EAP] and [unselected proteins,UP] secreted by E(M) are >50 and upto 4 fold higher than those secreted by E(P). (Figure 5 a ) Incubation of the panel of cultures, shown in Figure (with the exception of E(M9)-B, in lane 6) was for 170 hours with supplementation of methanol inducer at 24 hour intervals. Culture supernatants were harvested as determine in the materials and methods. Aliquots (20 μL) of cultures of E(P), h-V, H, E(M9)-B, EM32)-A,-B,-C,-D and E(M44)-A,-B were loaded in the order shown above the lanes (lanes 3–12) and co-electrophoresed with broad range markers (lane 1) and EAP purified from E.coli (0.08 units/lane, lanes2) through denaturing (4%-20%) <t>polyacrylamide</t> gradient gels with Laemmli electrophoresis buffer. The gel was stained with Gel Code Blue (GCB) scanned and saved as TIFF files. The respective ROIs of proteins corresponding to EAP, α-sec-EAP, unselected protein-1 (UP1) and unselected protein 3 (UP3) are identified and color coded on the left and right of the gel. The ROIs corresponding to the above 4 proteins were densitometrically scanned and normalized to UP3 in lane 3 and plotted as their respective ratios to E(P). Normalized ROIs corresponding to EAP, α-sec-EAP and HSA in E(P), v-H, H and E(M) were plotted with Excel programs (Figure 5 b ). Normalized ROIs corresponding to UP1 and UP3 were plotted as their ratios in EAP/E(P), E(P)/E(P), v-H/E(P), H/E(P) and all E(M)/E(P) (Figure 5 c , 5 d ).
Sds Page Gels, 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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sds page electrophoresis  (Bio-Rad)
96
Bio-Rad sds page electrophoresis
[α-sec-EAP] and [unselected proteins,UP] secreted by E(M) are >50 and upto 4 fold higher than those secreted by E(P). (Figure 5 a ) Incubation of the panel of cultures, shown in Figure (with the exception of E(M9)-B, in lane 6) was for 170 hours with supplementation of methanol inducer at 24 hour intervals. Culture supernatants were harvested as determine in the materials and methods. Aliquots (20 μL) of cultures of E(P), h-V, H, E(M9)-B, EM32)-A,-B,-C,-D and E(M44)-A,-B were loaded in the order shown above the lanes (lanes 3–12) and co-electrophoresed with broad range markers (lane 1) and EAP purified from E.coli (0.08 units/lane, lanes2) through denaturing (4%-20%) <t>polyacrylamide</t> gradient gels with Laemmli electrophoresis buffer. The gel was stained with Gel Code Blue (GCB) scanned and saved as TIFF files. The respective ROIs of proteins corresponding to EAP, α-sec-EAP, unselected protein-1 (UP1) and unselected protein 3 (UP3) are identified and color coded on the left and right of the gel. The ROIs corresponding to the above 4 proteins were densitometrically scanned and normalized to UP3 in lane 3 and plotted as their respective ratios to E(P). Normalized ROIs corresponding to EAP, α-sec-EAP and HSA in E(P), v-H, H and E(M) were plotted with Excel programs (Figure 5 b ). Normalized ROIs corresponding to UP1 and UP3 were plotted as their ratios in EAP/E(P), E(P)/E(P), v-H/E(P), H/E(P) and all E(M)/E(P) (Figure 5 c , 5 d ).
Sds Page Electrophoresis, 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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denaturing  (Bio-Rad)
97
Bio-Rad denaturing
[α-sec-EAP] and [unselected proteins,UP] secreted by E(M) are >50 and upto 4 fold higher than those secreted by E(P). (Figure 5 a ) Incubation of the panel of cultures, shown in Figure (with the exception of E(M9)-B, in lane 6) was for 170 hours with supplementation of methanol inducer at 24 hour intervals. Culture supernatants were harvested as determine in the materials and methods. Aliquots (20 μL) of cultures of E(P), h-V, H, E(M9)-B, EM32)-A,-B,-C,-D and E(M44)-A,-B were loaded in the order shown above the lanes (lanes 3–12) and co-electrophoresed with broad range markers (lane 1) and EAP purified from E.coli (0.08 units/lane, lanes2) through denaturing (4%-20%) <t>polyacrylamide</t> gradient gels with Laemmli electrophoresis buffer. The gel was stained with Gel Code Blue (GCB) scanned and saved as TIFF files. The respective ROIs of proteins corresponding to EAP, α-sec-EAP, unselected protein-1 (UP1) and unselected protein 3 (UP3) are identified and color coded on the left and right of the gel. The ROIs corresponding to the above 4 proteins were densitometrically scanned and normalized to UP3 in lane 3 and plotted as their respective ratios to E(P). Normalized ROIs corresponding to EAP, α-sec-EAP and HSA in E(P), v-H, H and E(M) were plotted with Excel programs (Figure 5 b ). Normalized ROIs corresponding to UP1 and UP3 were plotted as their ratios in EAP/E(P), E(P)/E(P), v-H/E(P), H/E(P) and all E(M)/E(P) (Figure 5 c , 5 d ).
Denaturing, supplied by Bio-Rad, used in various techniques. Bioz Stars score: 97/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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fibronectin antibody biotin conjugated  (Rockland Immunochemicals)
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Anti-Fibronectin (RABBIT) Antibody Biotin Conjugated - 600-406-117
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Image Search Results


[α-sec-EAP] and [unselected proteins,UP] secreted by E(M) are >50 and upto 4 fold higher than those secreted by E(P). (Figure 5 a ) Incubation of the panel of cultures, shown in Figure (with the exception of E(M9)-B, in lane 6) was for 170 hours with supplementation of methanol inducer at 24 hour intervals. Culture supernatants were harvested as determine in the materials and methods. Aliquots (20 μL) of cultures of E(P), h-V, H, E(M9)-B, EM32)-A,-B,-C,-D and E(M44)-A,-B were loaded in the order shown above the lanes (lanes 3–12) and co-electrophoresed with broad range markers (lane 1) and EAP purified from E.coli (0.08 units/lane, lanes2) through denaturing (4%-20%) polyacrylamide gradient gels with Laemmli electrophoresis buffer. The gel was stained with Gel Code Blue (GCB) scanned and saved as TIFF files. The respective ROIs of proteins corresponding to EAP, α-sec-EAP, unselected protein-1 (UP1) and unselected protein 3 (UP3) are identified and color coded on the left and right of the gel. The ROIs corresponding to the above 4 proteins were densitometrically scanned and normalized to UP3 in lane 3 and plotted as their respective ratios to E(P). Normalized ROIs corresponding to EAP, α-sec-EAP and HSA in E(P), v-H, H and E(M) were plotted with Excel programs (Figure 5 b ). Normalized ROIs corresponding to UP1 and UP3 were plotted as their ratios in EAP/E(P), E(P)/E(P), v-H/E(P), H/E(P) and all E(M)/E(P) (Figure 5 c , 5 d ).

Journal: Microbial Cell Factories

Article Title: A screen for over-secretion of proteins by yeast based on a dual component cellular phosphatase and immuno-chromogenic stain for exported bacterial alkaline phosphatase reporter

doi: 10.1186/1475-2859-12-36

Figure Lengend Snippet: [α-sec-EAP] and [unselected proteins,UP] secreted by E(M) are >50 and upto 4 fold higher than those secreted by E(P). (Figure 5 a ) Incubation of the panel of cultures, shown in Figure (with the exception of E(M9)-B, in lane 6) was for 170 hours with supplementation of methanol inducer at 24 hour intervals. Culture supernatants were harvested as determine in the materials and methods. Aliquots (20 μL) of cultures of E(P), h-V, H, E(M9)-B, EM32)-A,-B,-C,-D and E(M44)-A,-B were loaded in the order shown above the lanes (lanes 3–12) and co-electrophoresed with broad range markers (lane 1) and EAP purified from E.coli (0.08 units/lane, lanes2) through denaturing (4%-20%) polyacrylamide gradient gels with Laemmli electrophoresis buffer. The gel was stained with Gel Code Blue (GCB) scanned and saved as TIFF files. The respective ROIs of proteins corresponding to EAP, α-sec-EAP, unselected protein-1 (UP1) and unselected protein 3 (UP3) are identified and color coded on the left and right of the gel. The ROIs corresponding to the above 4 proteins were densitometrically scanned and normalized to UP3 in lane 3 and plotted as their respective ratios to E(P). Normalized ROIs corresponding to EAP, α-sec-EAP and HSA in E(P), v-H, H and E(M) were plotted with Excel programs (Figure 5 b ). Normalized ROIs corresponding to UP1 and UP3 were plotted as their ratios in EAP/E(P), E(P)/E(P), v-H/E(P), H/E(P) and all E(M)/E(P) (Figure 5 c , 5 d ).

Article Snippet: Each set comprising of samples and standards was electrophoresed through standard denaturing polyacrylamide gels (15% polyacrylamide , acrylamide : bisacrylamide ratio of 29:1 , 5% SDS, 4% stacking and 15% resolving layers) with Tris-Glycine-SDS running buffer (25 mM tris, 250 mM Glycine (BioRad electrophoresis grade) (pH 8.3) and 0.1% SDS).

Techniques: Incubation, Purification, Electrophoresis, Staining