A prestained SDS-PAGE MW marker with contrasting colored reference bands at 10 and 70kDa

The Thermo Scientific PageRuler Prestained Protein Ladder is a mixture of ten (10) blue-, orange- and green-stained recombinant proteins (10 to 170kDa) for use as size standards in protein electrophoresis (SDS-PAGE) and Western blotting.

This prestained protein MW marker is designed for monitoring the progress of SDS-polyacrylamide gel electrophoresis, for assessing transfer efficiency onto PVDF, nylon and nitrocellulose membranes, and for estimating the approximate size of separated proteins that have been made visible with gel stains or Western blot detection reagents. The ladder contains one orange reference band at 70kDa and one green band at 10kDa.

Highlights:

• Size range – 10 proteins spanning 10 to 170kDa
• Ready-to-use – supplied in a loading buffer for direct loading on gels; no need to boil
• Sharp bands – color-coded bands of similar intensity for easy visualization
• Quality tested – each lot evaluated by SDS-PAGE and Western blotting
• Two reference bands – orange at 70kDa and green at 10kDa
• Membrane-compatible – colored bands transfer to membranes for Western blotting

Includes:

• Dye-stained proteins in 62.5mM Tris-H3PO4 (pH 7.5 at 25°C), 1mM EDTA, 2% SDS, 10mM DTT, 1mM NaN3 and 33% glycerol.

Applications:

• Monitoring protein migration during SDS-polyacrylamide gel electrophoresis
• Monitoring protein transfer onto membranes after Western blotting
• Sizing of proteins on SDS-polyacrylamide gels and Western blots

Product Details:

SDS-PAGE band profile of the Thermo Scientific PageRuler Prestained Protein Ladder. Images are from a 4-20% Tris-glycine gel (SDS-PAGE) and subsequent transfer to membrane.

Migration patterns of the PageRuler Prestained Protein Ladder in different electrophoretic conditions. The apparent molecular weight of each protein (kDa) has been determined by calibration of each protein against an unstained protein ladder in specific electrophoresis conditions. Migration patterns were determined using commercial precast mini gels.

References:

1. Laemmli, U.K. (1970). Cleavage of structural proteins during the assembly of the head of bacteriophage T4, Nature, 227, 680-685.
2. Burnette, W.N. (1981). Western blotting: electrophoretic transfer of proteins from sodium dodecyl sulfate – polyacrylamide gels to unmodified nitrocellulose and radiographic detection with antibody and radioiodinated protein A, Anal. Biochem., 112 (2), 195-203.
3. Towbin, H., et al. (1979). Electrophoretic transfer of proteins from polyacrylamide gels to nitrocellulose sheets: procedure and some applications, Proc. Natl. Acad. Sci. USA, 76, 4350-4354.

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