Research Profile: Focusing on improved SDS-PAGE separations
نویسندگان
چکیده
منابع مشابه
Multiple SDS-PAGE on Vertical Electrophoresis Units.
INTRODUCTION SDS-polyacrylamide gel electrophoresis (SDS-PAGE) represents the second-dimension separation of two-dimensional (2D)-PAGE. Large-scale proteome analysis usually requires simultaneous electrophoresis of batches of second-dimension SDS-PAGE gels to maximize the reproducibility of 2D electrophoresis protein profiles. This requirement is most easily met using multiple, vertical second-...
متن کاملStudy on Outer Membrane Protein (OMP) Profile of Aeromonas Strains using SDS- PAGE
Mesophilic aeromonads are being increasingly reported pathogen of humans and lower vertebrates. Water and foods are considered to be the chief source of Aeromonas spp. At present there are several techniques available for the detection of Aeromonas spp. from water and foods. However, there is still need to develop immunodiagnostics for rapid detection of Aeromonas spp. irrespective of their spe...
متن کاملTricine – SDS - PAGE Hermann Schägger
Tricine–SDS-PAGE is commonly used to separate proteins in the mass range 1–100 kDa. It is the preferred electrophoretic system for the resolution of proteins smaller than 30 kDa. The concentrations of acrylamide used in the gels are lower than in other electrophoretic systems. These lower concentrations facilitate electroblotting, which is particularly crucial for hydrophobic proteins. Tricine–...
متن کاملA Practical Approach on SDS PAGE for Separation of Protein
Polyacrylamide gel electrophoresis (PAGE), describes a technique widely used in biochemistry, forensics, genetics, molecular biology and biotechnology to separate biological macromolecules, usually proteins or nucleic acids, according to their electrophoretic mobility. Mobility is a function of the length, conformation and charge of the molecule. As with all forms of gel electrophoresis, molecu...
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ژورنال
عنوان ژورنال: Analytical Chemistry
سال: 2007
ISSN: 0003-2700,1520-6882
DOI: 10.1021/ac0718748