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SDS-Page Analysis of Protein - Coomassie



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SDS-PAGE analysis of protein with Coomassie staining.
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Synonyms: Polyacrylamide Gel Electrophoresis, Gel Electrophoresis, Protein Gel electrophoresis, Coomassie stained PAGE Gels, Protein Analysis, Molecular weight determination by SDS-Page

SDS-Page Analysis of Protein - Coomassie Properties

SDS-PAGE ANALYSIS of PROTEIN - COOMASSIE. Charge applies per protein. Includes reduced and non-reduced lanes and analysis of apparent molecular weight relative to known standards. When applicable, a scan of the gel will be sent to the customer. - CUST56
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SDS-Page Analysis of Protein - Coomassie Description

SDS-PAGE allows both estimation of the purity and apparent molecular weight of protein samples. SDS is an anionic detergent and is used to linearize the proteins and impart a negative charge. The negative charges on SDS removes most of the secondary and tertiary structure of proteins, and are strongly attracted toward the anode in an electric field. Because the charge-to-mass ratio is nearly the same among SDS-denatured proteins, the final separation of proteins is almost entirely dependent on the differences in relative Mw of polypeptides. Some caution has to be put on intrinsic strong negative or strong positively charged proteins because SDS may bind to them differently and their migration in the gel may not be at the expected Mw. In PAGE the relative migration distance of a protein (Rf) is negatively proportional to the log of its Mw. To be able to estimate the Mw of proteins on the SDS-page, proteins of known Mw need to be run simultaneously on the gel. Coomassie Brilliant Blue is the most commonly used protein stain. It is an anionic dye , which non-specifically binds to proteins. The proteins are visualized as blue bands on a clear background.
Disclaimer Note-General
This product is for research use only and is not intended for therapeutic or diagnostic applications. Please contact a technical service representative for more information. All products of animal origin manufactured by Rockland Immunochemicals are derived from starting materials of North American origin. Collection was performed in United States Department of Agriculture (USDA) inspected facilities and all materials have been inspected and certified to be free of disease and suitable for exportation. All properties listed are typical characteristics and are not specifications. All suggestions and data are offered in good faith but without guarantee as conditions and methods of use of our products are beyond our control. All claims must be made within 30 days following the date of delivery. The prospective user must determine the suitability of our materials before adopting them on a commercial scale. Suggested uses of our products are not recommendations to use our products in violation of any patent or as a license under any patent of Rockland Immunochemicals, Inc. If you require a commercial license to use this material and do not have one, then return this material, unopened to: Rockland Inc., P.O. BOX 326, Gilbertsville, Pennsylvania, USA.
General Reference
Rath, Arianna and Glibowicka, Mira and Nadeau, Vincent G. and Chen, Gong and Deber, Charles M. (2009). "Detergent binding explains anomalous SDS-PAGE migration of membrane proteins". Proceedings of the National Academy of Sciences 106 (6): 1760–1765.
Specific Reference
Shapiro AL, Viñuela E, Maizel JV Jr. (September 1967). "Molecular weight estimation of polypeptide chains by electrophoresis in SDS-polyacrylamide gels.". Biochem Biophys Res Commun. 28 (5): 815–820.
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Product Type
Primary Antibodies;
Reacts With
human, mouse, rat, monkey
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Secondary Antibodies;
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Supporting Reagents;
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Conjugation Reference
Molecular Weight
Excitation Wavelength
Conjugation Chemistry