A sorbent material is disclosed for the one-step separation of bio-macromolecules in a single pass extraction of DNA from complex mixtures of molecules and chemicals. In one embodiment, the sorbent material comprises a silanized material at least partially coated or formed with a polymer selected from the group consisting of a poly(aryl methacrylate), a poly(aryl acrylate), a poly(heteroaryl methacrylate, a poly(heteroaryl acrylate) and a copolymer thereof.

A sorbent material is disclosed for the one-step separation of bio-macromolecules in a single pass extraction of DNA from complex mixtures of molecules and chemicals. In one embodiment, the sorbent material comprises a silanized material at least partially coated or formed with a polymer selected from the group consisting of a poly(aryl methacrylate), a poly(aryl acrylate), a poly(heteroaryl methacrylate, a poly(heteroaryl acrylate) and a copolymer thereof.

A novel system for the analysis of molecules and cells, comprising clusters where a non-magnetic particle is supplemented with magnetic particles to form a characteristic pattern, fingerprint or bar code. Methods and devices for formation of such particles are also disclosed.

A novel system for the analysis of molecules and cells, comprising clusters where a non-magnetic particle is supplemented with magnetic particles to form a characteristic pattern, fingerprint or bar code. Methods and devices for formation of such particles are also disclosed.

Disclosed herein are methods and compositions for purifying proteins from crude solutions.

Disclosed herein are methods and compositions for purifying proteins from crude solutions.

The invention relates to poly-amide bonded hydrophilic interaction chromatography (HILIC) stationary phases and novel HILIC methods for use in the characterization of large biological molecules modified with polar groups, known to those skilled in the art as glycans. The invention particularly provides novel, poly-amide bonded materials designed for efficient separation of large biomolecules, e.g. materials having a large percentage of larger pores (i.e. wide pores). Furthermore, the invention advantageously provides novel HILIC methods that can be used in combination with the stationary phase materials described herein to effectively separate protein and peptide glycoforms by eliminating previously unsolved problems, such as on-column aggregation of protein samples, low sensitivity of chromatographic detection of the glycan moieties, and low resolution of peaks due to restricted pore diffusion and long intra/inter-particle diffusion distances.

The invention relates to poly-amide bonded hydrophilic interaction chromatography (HILIC) stationary phases and novel HILIC methods for use in the characterization of large biological molecules modified with polar groups, known to those skilled in the art as glycans. The invention particularly provides novel, poly-amide bonded materials designed for efficient separation of large biomolecules, e.g. materials having a large percentage of larger pores (i.e. wide pores). Furthermore, the invention advantageously provides novel HILIC methods that can be used in combination with the stationary phase materials described herein to effectively separate protein and peptide glycoforms by eliminating previously unsolved problems, such as on-column aggregation of protein samples, low sensitivity of chromatographic detection of the glycan moieties, and low resolution of peaks due to restricted pore diffusion and long intra/inter-particle diffusion distances.

There is provided a method of identifying a resin for isolating or enriching a protein of interest using affinity chromatography. The method comprises the steps of: i) providing the three-dimensional structure of the protein of interest; ii) determining and/or calculating one or more parameters of the protein of interest in its two- and/or three-dimensional form; iii) determining and/or calculating one or more parameters of one or more resin in their two- and/or three-dimensional form; and iv) selecting a resin expected to bind complementarily to the protein of interest based upon one or more of the parameters of the protein of interest.

There is provided a method of identifying a resin for isolating or enriching a protein of interest using affinity chromatography. The method comprises the steps of: i) providing the three-dimensional structure of the protein of interest; ii) determining and/or calculating one or more parameters of the protein of interest in its two- and/or three-dimensional form; iii) determining and/or calculating one or more parameters of one or more resin in their two- and/or three-dimensional form; and iv) selecting a resin expected to bind complementarily to the protein of interest based upon one or more of the parameters of the protein of interest.