Abstract: The invention discloses a separation matrix which comprises a plurality of separation ligands, defined by the formula R1-L1-N(R3)-L2-R, immobilized on a support, wherein R1 is a five- or six-membered, substituted or non-substituted ring structure or a hydroxyethyl or hydroxypropyl group; L1 is either a methylene group or a covalent bond; R2 is a five- or six-membered, substituted or non-substituted ring structure; L2 is either a methylene group or a covalent bond; R3 is a methyl group; and wherein if R1 is a hydroxyethyl group and L1 is a covalent bond, R2 is a substituted aromatic ring structure or a substituted or non-substituted aliphatic ring structure.

Abstract: The invention discloses a separation matrix for purification of biological particles, comprising a plurality of particles having a porous core entity and a porous shell entity covering the core entity, wherein the core entity comprises at least 50 micromole/ml primary amines present on covalently attached ligands displaying at least two primary amines per ligand and the shell entity comprises less than 20 micromole/ml primary amines The invention further discloses a method of purifying biological particles and a method of manufacturing a separation matrix.

Abstract: The present invention relates to a method for removal of large contaminants, such as virus, in a chromatographic process for purification of a target molecule, preferably monoclonal antibodies, mAbs, by using a specifically designed chromatographic bead having a thin outer layer and a core functionalized with a ligand adsorbing the mAbs or parts thereof.

Abstract: The invention discloses a separation matrix which comprises a plurality of separation ligands, defined by the formula R1-L1-N(R3)-L2-R, immobilized on a support, wherein R1 is a five- or six-membered, substituted or non-substituted ring structure or a hydroxyethyl or hydroxypropyl group; L1 is either a methylene group or a covalent bond; R2 is a five-or six-membered, substituted or non-substituted ring structure; L2 is either a methylene group or a covalent bond; R3 is a methyl group; and wherein if R1 is a hydroxyethyl group and L1 is a covalent bond, R2 is a substituted aromatic ring structure or a substituted or non-substituted aliphatic ring structure.

Abstract: The present invention relates to a method for removal of large contaminants, such as virus, in a chromatographic process for purification of a target molecule, preferably monoclonal antibodies, mAbs, by using a specifically designed chromatographic bead having a thin outer layer and a core functionalized with a ligand adsorbing the mAbs or parts thereof.

Abstract: The present invention relates to a method for removal of large contaminants, such as virus, in a chromatographic process for purification of a target molecule, preferably monoclonal antibodies, mAbs, by using a specifically designed chromatographic bead having a thin outer layer and a core functionalized with a ligand adsorbing the mAbs or parts thereof.

Abstract: The invention discloses a separation matrix which comprises a plurality of separation ligands, defined by the formula R1-L1-N(R3)-L2-R, immobilized on a support, wherein R1 is a five- or six-membered, substituted or non-substituted ring structure or a hydroxyethyl or hydroxypropyl group; L1 is either a methylene group or a covalent bond; R2 is a five-or six-membered, substituted or non-substituted ring structure; L2 is either a methylene group or a covalent bond; R3 is a methyl group; and wherein if R1 is a hydroxyethyl group and L1 is a covalent bond, R2 is a substituted aromatic ring structure or a substituted or non-substituted aliphatic ring structure.

Abstract: The present invention relates to a method for removal of large contaminants, such as virus, in a chromatographic process for purification of a target molecule, preferably monoclonal antibodies, mAbs, by using a specifically designed chromatographic bead having a thin outer layer and a core functionalized with a ligand adsorbing the mAbs or parts thereof.

Abstract: The invention discloses a separation matrix for purification of biological particles, comprising a plurality of particles having a porous core entity and a porous shell entity covering the core entity, wherein the core entity comprises at least 50 micromole/ml primary amines present on covalently attached ligands displaying at least two primary amines per ligand and the shell entity comprises less than 20 micromole/ml primary amines The invention further discloses a method of purifying biological particles and a method of manufacturing a separation matrix.

Abstract: The present invention relates to a method of separating one or more immunoglobulin containing proteins from a liquid. The method includes first contacting the liquid with a separation matrix comprising ligands immobilized to a support; allowing the immunoglobulin containing proteins to adsorb to the matrix by interaction with the ligands; followed by an optional step of washing the matrix containing the immunoglobulin containing proteins adsorbed thereon; and recovering said immunoglobulin containing proteins by contacting the matrix with an eluent which releases the proteins.

Abstract: The invention discloses a separation matrix which comprises a plurality of separation ligands, defined by the formula R1-L1-N(R3)-L2-R, immobilized on a support, wherein R1 is a five- or six-membered, substituted or non-substituted ring structure or a hydroxyethyl or hydroxypropyl group; L1 is either a methylene group or a covalent bond; R2 is a five- or six-membered, substituted or non-substituted ring structure; L2 is either a methylene group or a covalent bond; R3 is a methyl group; and wherein if R1 is a hydroxyethyl group and L1 is a covalent bond, R2 is a substituted aromatic ring structure or a substituted or non-substituted aliphatic ring structure.

Abstract: The present invention is relates to method for production of a biomolecule adsorbent with a pentadentate ligand with very strong chelating properties, and to methods for use thereof for, for example, protein purification, detection or binding. The biomolecule adsorbent comprises the formula: wherein Q is a carrier, S is a spacer, L is an amide linkage, X is COOH, and n=2 or 3.

Abstract: The present invention relates to a method of separating one or more immunoglobulin containing proteins from a liquid. The method includes first contacting the liquid with a separation matrix comprising ligands immobilised to a support; allowing the immunoglobulin containing proteins to adsorb to the matrix by interaction with the ligands; followed by an optional step of washing the matrix containing the immunoglobulin containing proteins adsorbed thereon; and recovering said immunoglobulin containing proteins by contacting the matrix with an eluent which releases the proteins.

Abstract: The present invention is relates to method for production of a biomolecule adsorbent with a pentadentate ligand with very strong chelating properties, and to methods for use thereof for, for example, protein purification, detection or binding. The biomolecule adsorbent comprises the formula: wherein Q is a carrier, S is a spacer, L is an amide linkage, X is COOH, and n=2 or 3.

Abstract: The present invention relates to the field of adherent cell culture. More closely, the invention relates to a method for production of a cell attachment and culture surface, such as a microcarrier, comprising a guanidino-containing ligand, wherein the ligand is coupled via reaction involving a primary amine to the surface which is activated by activation groups such that the final molar ratio of grafted ligand and ungrafted activation groups is above 1.5. Preferably, the ligand density is above 0.5 mmol/g cell culture surface and the remaining activation groups after coupling is less than 0.6 mmol/g cell culture surface. The cell culture surface may be used for various purposes, primarily cell cultivation and virus production.