Protein gel electrophoresis is a technique used to separate and visualize proteins based on their size and charge. 1D and 2D gel protein electrophoresis is an invaluable tool for the modern biologist and G-Biosciences provide a full range of products to help achieve the results you need.
A wide variety of sample preparation reagents for 1D and 2D protein gel electrophoresis are available from G-Biosciences. PAGE-Perfect™ is a simple method for removing contaminants and improving resolution for your publication quality gels. Immobilized Reductant is an excellent way to remove reducing agents from your protein preps and improve your downstream results. To remove salts, detergents and other buffering agents we provide PAGE-Optimizer™, a spin column for the preparation of samples for SDS-PAGE.
Two reliable protein standards are available from G-Biosciences. PAGEmark™ Blue Plus is a 12 protein prestained ladder with a molecular weight range from 10-240kDa (in Tris-Glycine buffer) and 9-235kDa (in MOPS or MEPS buffer). PAGEmark™ Tricolor Plus is a three color, 12 protein standard that has a molecular weight range of 5-245kDa (in Tris-Glycine buffer) or 3.5-235kDa (in MOPS or MEPS buffer).
Also available are a wide range of gel stains and destains to insure the best visualization of your gel protein electrophoresis. We offer Coomasie Brilliant Blue, RAPIDstain™, Reversible Copper Stain™, and several other stains optimized for every downstream application.
Our partners for benchtop equipment, BTLabs provide gel electrophoresis boxes, power supplies, dry bath incubators and wide range of buffers and chemicals for your electrophoresis needs.
Our 2D protein gel electrophoresis products are optimized for isoelectric focusing (IEF) and 2D electrophoresis. 2D detergents such as 2-D Detergent™ Triton®X-100 and 2-D Detergent™ Nonidet® P-40 Substitute contain reduced levels of sulfhydryl oxidizing agents, peroxides, salts and carbonyl compounds. Reducing these agents makes the protein less susceptible to oxidation and the formation of Schiff’s bases which interfere with a protein’s native structure.