Sera-Mag™ SpeedBeads™ and Sera-Mag™ Carboxylate-Modified Magnetic Particles combine a fast magnetic response time and high binding capacity with a large surface area, high sensitivity, stability, physical integrity, and fast reaction kinetics. Covalent coupling of biomolecules such as proteins and nucleic acids to carboxyl groups on the surface is easily accomplished using our standard coupling technology. The core of the particle is made by a free radical emulsion polymerization of styrene and acid monomer. One (Sera-Mag™) or two (Sera-Mag™ SpeedBeads™) layers of magnetite are then coated onto this core, while the surface is modified to minimize non-specific binding of proteins.
Sera-Mag™ SpeedBeads™ and Sera-Mag™ Carboxylate-Modified Magnetic Particles combine a fast magnetic response time and high binding capacity with a large surface area, high sensitivity, stability, physical integrity, and fast reaction kinetics. Covalent coupling of biomolecules such as proteins and nucleic acids to carboxyl groups on the surface is easily accomplished using our standard coupling technology. The core of the particle is made by a free radical emulsion polymerization of styrene and acid monomer. One (Sera-Mag™) or two (Sera-Mag™ SpeedBeads™) layers of magnetite are then coated onto this core, while the surface is modified to minimize non-specific binding of proteins.
Sera-Mag™ SpeedBeads™ and Sera-Mag™ Carboxylate-Modified Magnetic Particles combine a fast magnetic response time and high binding capacity with a large surface area, high sensitivity, stability, physical integrity, and fast reaction kinetics. Covalent coupling of biomolecules such as proteins and nucleic acids to carboxyl groups on the surface is easily accomplished using our standard coupling technology. The core of the particle is made by a free radical emulsion polymerization of styrene and acid monomer. One (Sera-Mag™) or two (Sera-Mag™ SpeedBeads™) layers of magnetite are then coated onto this core, while the surface is modified to minimize non-specific binding of proteins.
Sera-Mag™ SpeedBeads™ and Sera-Mag™ Carboxylate-Modified Magnetic Particles combine a fast magnetic response time and high binding capacity with a large surface area, high sensitivity, stability, physical integrity, and fast reaction kinetics. Covalent coupling of biomolecules such as proteins and nucleic acids to carboxyl groups on the surface is easily accomplished using our standard coupling technology. The core of the particle is made by a free radical emulsion polymerization of styrene and acid monomer. One (Sera-Mag™) or two (Sera-Mag™ SpeedBeads™) layers of magnetite are then coated onto this core, while the surface is modified to minimize non-specific binding of proteins.
Sera-Mag™ SpeedBeads™ and Sera-Mag™ Carboxylate-Modified Magnetic Particles combine a fast magnetic response time and high binding capacity with a large surface area, high sensitivity, stability, physical integrity, and fast reaction kinetics. Covalent coupling of biomolecules such as proteins and nucleic acids to carboxyl groups on the surface is easily accomplished using our standard coupling technology. The core of the particle is made by a free radical emulsion polymerization of styrene and acid monomer. One (Sera-Mag™) or two (Sera-Mag™ SpeedBeads™) layers of magnetite are then coated onto this core, while the surface is modified to minimize non-specific binding of proteins.
Sera-Mag™ SpeedBeads™ and Sera-Mag™ Carboxylate-Modified Magnetic Particles combine a fast magnetic response time and high binding capacity with a large surface area, high sensitivity, stability, physical integrity, and fast reaction kinetics. Covalent coupling of biomolecules such as proteins and nucleic acids to carboxyl groups on the surface is easily accomplished using our standard coupling technology. The core of the particle is made by a free radical emulsion polymerization of styrene and acid monomer. One (Sera-Mag™) or two (Sera-Mag™ SpeedBeads™) layers of magnetite are then coated onto this core, while the surface is modified to minimize non-specific binding of proteins.