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| | Perfect Protein™ Markers, 15-150 kDa |
|  | Cat. No. 69149 |
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| Precisely sized, conveniently spaced for accurate protein size determination | | | The Perfect Protein™ Markers are a novel set of recombinant proteins with defined sizes at convenient intervals. Designed for routine use in SDS-polyacrylamide gel electrophoresis, the Perfect Protein Markers enable highly accurate size determination of unknown samples. Unlike many conventional markers (e.g., ovalbumin, serum albumin, etc.), the Perfect Protein Markers contain no oligosaccharides that cause anomalous migration, heterogeneous "fuzzy" bands, or inaccurate size estimation. The known mass of each Perfect Protein Marker band also enables estimation of concentration of sample proteins. The markers are optimized for use with Coomassie blue staining, but adjusted amounts can also be used with other gel staining methods (e.g., silver staining, fluorescent dyes, etc.).
The Perfect Protein Markers, 15-150 kDa, include protein sizes of 15, 25, 35, 50, 75, 100, and 150 kDa. Each vial contains 400 µg protein. A 5-µl load contains 0.5 µg for each of the protein sizes, except for the 50-kDa band, which contains twice as much protein (1.0 µg).
The Perfect Protein Markers, 10-225 kDa, include the protein sizes listed above and two additional proteins, 10 kDa and 225 kDa, for applications requiring a broader size range. Each vial contains 500 µg protein. A 5-µl load contains 0.5 µg for each of the protein sizes, except for the 50-kDa band, which contains twice as much protein (1.0 µg).
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| Need additional information about this product? Email our Technical Service department at: novatech@novagen.com |
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EMD Chemicals Inc. list price is displayed (pricing with local distributors may vary). NOTE: In Stock status is based on item availability worldwide.
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| - Kenji Kojima, et al. (2008) Roles of functional and structural domains of hepatocyte growth factor activator inhibitor type 1 in the inhibition of matriptase. Journal of Biological Chemistry 283, 2478-2487.
- Athmane Teghanemt, et al. (2008) Novel roles in human MD-2 of phenylalanines 121 and 126 and tyrosine 131 in activation of toll-like receptor 4 by endotoxin. Journal of Biological Chemistry 283, 1257-1266.
- Jim F. White, et al. (2007) Dimerization of the class A G protein-coupled neurotensin receptor NTS1 alters G protein interaction. Procedings of the National Academy of Science 104, 12199-12204.
- Dequan Chen, et al. (2005) Surface calreticulin mediates muramyl dipeptide-induced apoptosis in RK13 cells. Journal of Biological Chemistry 280, 22425-22436.
- Larisa Tsavaler, et al. (2001) Trp-p8, a novel prostate-specific gene, Is up-regulated in prostate cancer and other malignancies and shares high homology with transient receptor potential calcium channel proteins. Cancer Research 61, 3760-3769.
- Kelvin Nurse, et al. (1995) Purification, cloning, and properties of the tRNA ψ55 synthase from Escherichia coli. RNA 1,.
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