lmw protein ladders sds page Search Results


97
Bio-Rad acrylamide gradient gel
Figure 2. Purification of Penn State ladder proteins by metal affinity chromatography. Panels (a) through (k) show metal affinity purification of the individual 10, 15, 20, 30, 40, 50, 60, 80, 100, 150 and 250 kD ladder proteins respectively, while panels (l) and (m) show the equivalent for the coexpressed 10, 30, 50, 100 kD and the coexpressed 20, 40, 60, 80 ladder proteins respectively. The schematic for each individual protein is shown above each gel, while the schematic showing the order of expression in the coexpression constructs are shown for panels l and m. In each panel, lanes 1 through 7 show the whole cell extract (W), an equivalent volume sample of the pellet fraction after lysis (P), an equivalent volume of the supernatant fraction after lysis (S), an equivalent volume sample of the metal affinity flow through fraction (FT), and the metal affinity elution fractions 1, 2 and 3. The volumes of the whole, pellet, supernatant and flow through samples were approximately 5 ml each, while the volumes of the elution fractions were approximately 0.5 ml each. 5 µl of a 1:4 dilution of each sample was loaded onto 18% <t>acrylamide</t> SDS-PAGE gels and stained with Coomassie Blue. Lane 8 of all panels except for panel k show the Bio-Rad low molecular weight (LMW) markers, while lane 8 of panel k shows the Bio- Rad Precision Plus markers. The location of the band for each protein is shown with an arrow to the left of each gel.
Acrylamide Gradient Gel, 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
https://www.bioz.com/product/lmw+protein+ladders+sds+page/Acrylamide/pm34408191-110-11-17
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acrylamide gradient gel - by Bioz Stars, 2026-10
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98
Bio-Rad lmw protein ladders sds page
Figure 2. Purification of Penn State ladder proteins by metal affinity chromatography. Panels (a) through (k) show metal affinity purification of the individual 10, 15, 20, 30, 40, 50, 60, 80, 100, 150 and 250 kD ladder proteins respectively, while panels (l) and (m) show the equivalent for the coexpressed 10, 30, 50, 100 kD and the coexpressed 20, 40, 60, 80 ladder proteins respectively. The schematic for each individual protein is shown above each gel, while the schematic showing the order of expression in the coexpression constructs are shown for panels l and m. In each panel, lanes 1 through 7 show the whole cell extract (W), an equivalent volume sample of the pellet fraction after lysis (P), an equivalent volume of the supernatant fraction after lysis (S), an equivalent volume sample of the metal affinity flow through fraction (FT), and the metal affinity elution fractions 1, 2 and 3. The volumes of the whole, pellet, supernatant and flow through samples were approximately 5 ml each, while the volumes of the elution fractions were approximately 0.5 ml each. 5 µl of a 1:4 dilution of each sample was loaded onto 18% <t>acrylamide</t> SDS-PAGE gels and stained with Coomassie Blue. Lane 8 of all panels except for panel k show the Bio-Rad low molecular weight (LMW) markers, while lane 8 of panel k shows the Bio- Rad Precision Plus markers. The location of the band for each protein is shown with an arrow to the left of each gel.
Lmw Protein Ladders Sds Page, 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
https://www.bioz.com/product/lmw+protein+ladders+sds+page/SDS/pmc11771338-52-6-12
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lmw protein ladders sds page - by Bioz Stars, 2026-10
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94
Cytiva Europe ladder protein marker
Figure 2. Purification of Penn State ladder proteins by metal affinity chromatography. Panels (a) through (k) show metal affinity purification of the individual 10, 15, 20, 30, 40, 50, 60, 80, 100, 150 and 250 kD ladder proteins respectively, while panels (l) and (m) show the equivalent for the coexpressed 10, 30, 50, 100 kD and the coexpressed 20, 40, 60, 80 ladder proteins respectively. The schematic for each individual protein is shown above each gel, while the schematic showing the order of expression in the coexpression constructs are shown for panels l and m. In each panel, lanes 1 through 7 show the whole cell extract (W), an equivalent volume sample of the pellet fraction after lysis (P), an equivalent volume of the supernatant fraction after lysis (S), an equivalent volume sample of the metal affinity flow through fraction (FT), and the metal affinity elution fractions 1, 2 and 3. The volumes of the whole, pellet, supernatant and flow through samples were approximately 5 ml each, while the volumes of the elution fractions were approximately 0.5 ml each. 5 µl of a 1:4 dilution of each sample was loaded onto 18% <t>acrylamide</t> SDS-PAGE gels and stained with Coomassie Blue. Lane 8 of all panels except for panel k show the Bio-Rad low molecular weight (LMW) markers, while lane 8 of panel k shows the Bio- Rad Precision Plus markers. The location of the band for each protein is shown with an arrow to the left of each gel.
Ladder Protein Marker, supplied by Cytiva Europe, used in various techniques. Bioz Stars score: 94/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/product/lmw+protein+ladders+sds+page/LMW-SDS+Marker+Kit/pmc09674648-147-22-25
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ladder protein marker - by Bioz Stars, 2026-10
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Figure 2. Purification of Penn State ladder proteins by metal affinity chromatography. Panels (a) through (k) show metal affinity purification of the individual 10, 15, 20, 30, 40, 50, 60, 80, 100, 150 and 250 kD ladder proteins respectively, while panels (l) and (m) show the equivalent for the coexpressed 10, 30, 50, 100 kD and the coexpressed 20, 40, 60, 80 ladder proteins respectively. The schematic for each individual protein is shown above each gel, while the schematic showing the order of expression in the coexpression constructs are shown for panels l and m. In each panel, lanes 1 through 7 show the whole cell extract (W), an equivalent volume sample of the pellet fraction after lysis (P), an equivalent volume of the supernatant fraction after lysis (S), an equivalent volume sample of the metal affinity flow through fraction (FT), and the metal affinity elution fractions 1, 2 and 3. The volumes of the whole, pellet, supernatant and flow through samples were approximately 5 ml each, while the volumes of the elution fractions were approximately 0.5 ml each. 5 µl of a 1:4 dilution of each sample was loaded onto 18% acrylamide SDS-PAGE gels and stained with Coomassie Blue. Lane 8 of all panels except for panel k show the Bio-Rad low molecular weight (LMW) markers, while lane 8 of panel k shows the Bio- Rad Precision Plus markers. The location of the band for each protein is shown with an arrow to the left of each gel.

Journal: Scientific reports

Article Title: The Penn State Protein Ladder system for inexpensive protein molecular weight markers.

doi: 10.1038/s41598-021-96051-x

Figure Lengend Snippet: Figure 2. Purification of Penn State ladder proteins by metal affinity chromatography. Panels (a) through (k) show metal affinity purification of the individual 10, 15, 20, 30, 40, 50, 60, 80, 100, 150 and 250 kD ladder proteins respectively, while panels (l) and (m) show the equivalent for the coexpressed 10, 30, 50, 100 kD and the coexpressed 20, 40, 60, 80 ladder proteins respectively. The schematic for each individual protein is shown above each gel, while the schematic showing the order of expression in the coexpression constructs are shown for panels l and m. In each panel, lanes 1 through 7 show the whole cell extract (W), an equivalent volume sample of the pellet fraction after lysis (P), an equivalent volume of the supernatant fraction after lysis (S), an equivalent volume sample of the metal affinity flow through fraction (FT), and the metal affinity elution fractions 1, 2 and 3. The volumes of the whole, pellet, supernatant and flow through samples were approximately 5 ml each, while the volumes of the elution fractions were approximately 0.5 ml each. 5 µl of a 1:4 dilution of each sample was loaded onto 18% acrylamide SDS-PAGE gels and stained with Coomassie Blue. Lane 8 of all panels except for panel k show the Bio-Rad low molecular weight (LMW) markers, while lane 8 of panel k shows the Bio- Rad Precision Plus markers. The location of the band for each protein is shown with an arrow to the left of each gel.

Article Snippet: All three ladders produced excellent goodness of fit on the 4–20% acrylamide gradient gel (0.995 for the Bio-Rad LMW, 0.993 for the Penn State protein ladder and 0.997 for the Bio-Rad Precision Plus).

Techniques: Purification, Affinity Chromatography, Affinity Purification, Expressing, Construct, Lysis, SDS Page, Staining, Molecular Weight

Figure 4. Comparison of Penn State protein ladder with commercial protein ladders. (a) SDS-PAGE of Bio-Rad low molecular weight (LMW) markers (lane 1, green), Penn State 10-100 kD ladder (lane 2, red) and Bio-Rad Precision Plus protein ladder (lane 3, blue) on 18% acrylamide gel. Sizes of bands in kD are shown to the sides. Semi-log plots of the LMW markers, Penn State ladder and Precision Plus ladder with R2 goodness of fit for the samples shown in panel (a) are shown in panels (b), (c) and (d) respectively. The equivalent panels for samples electrophoresed through a 4-20% acrylamide gradient gel (Bio-Rad, 456-1093) are shown in panels (e) through (h).

Journal: Scientific reports

Article Title: The Penn State Protein Ladder system for inexpensive protein molecular weight markers.

doi: 10.1038/s41598-021-96051-x

Figure Lengend Snippet: Figure 4. Comparison of Penn State protein ladder with commercial protein ladders. (a) SDS-PAGE of Bio-Rad low molecular weight (LMW) markers (lane 1, green), Penn State 10-100 kD ladder (lane 2, red) and Bio-Rad Precision Plus protein ladder (lane 3, blue) on 18% acrylamide gel. Sizes of bands in kD are shown to the sides. Semi-log plots of the LMW markers, Penn State ladder and Precision Plus ladder with R2 goodness of fit for the samples shown in panel (a) are shown in panels (b), (c) and (d) respectively. The equivalent panels for samples electrophoresed through a 4-20% acrylamide gradient gel (Bio-Rad, 456-1093) are shown in panels (e) through (h).

Article Snippet: All three ladders produced excellent goodness of fit on the 4–20% acrylamide gradient gel (0.995 for the Bio-Rad LMW, 0.993 for the Penn State protein ladder and 0.997 for the Bio-Rad Precision Plus).

Techniques: Comparison, SDS Page, Molecular Weight, Acrylamide Gel Assay