Chromatography devices contain chromatography media and methods of making and methods of using chromatography devices. Chromatography devices enable a more efficient, productive and/or environmentally friendly chromatographic operation due to one or more of the following advantages over conventional chromatographic operations: elimination of a device packing step by the user; elimination of clean-in-place (CIP) steps; elimination of clean-in-place (CIP) steps utilizing sodium hydroxide solution; elimination of any validation steps by the user; and use of a chromatography device comprising biodegradable material. The chromatography media includes porous inorganic particles having a functionalized surface and having a median pore size of at least about 300 Angstroms (A), or at least about 300 A up to about 3000 A. The inorganic particles may have a BET surface area of at least about 20 m2/g, or at least about 25 m2/g, or about 30 m2/g, up to about 2000 m2/g.

There is disclosed a relatively simple method to increase the performance of surface localised multi-valent affinity ligands whose target's isoelectric pH differs significantly from the ligand's optimal target-binding pH. This situation can result in ligand binding of target affecting local pH and subsequent binding of more target. Increasing the buffering capacity of the ligand via recombinant or other addition of charge groups to the ligand is expected to partially offset such effects, leading to enhanced binding capacity as well as possible secondary favourable alterations in regard to ligand elution pH, and non-specific surface binding of non-target proteins.

There is disclosed a relatively simple method to increase the performance of surface localised multi-valent affinity ligands whose target's isoelectric pH differs significantly from the ligand's optimal target-binding pH. This situation can result in ligand binding of target affecting local pH and subsequent binding of more target. Increasing the buffering capacity of the ligand via recombinant or other addition of charge groups to the ligand is expected to partially offset such effects, leading to enhanced binding capacity as well as possible secondary favourable alterations in regard to ligand elution pH, and non-specific surface binding of non-target proteins.

The invention relates to an affinity resin functionalized with small molecule inhibitors of glycoside-cleaving enzymes, e.g., α-galactosidase A (α-Gal A), glucocerebrosidase (GCB), β-galactosidase, and acid alpha-glucosidase (GAA), and a method for purifying glycoside-cleaving enzymes produced in a cell line using the small molecule inhibitor-functionalized affinity resin.

The invention relates to an affinity resin functionalized with small molecule inhibitors of glycoside-cleaving enzymes, e.g., α-galactosidase A (α-Gal A), glucocerebrosidase (GCB), β-galactosidase, and acid alpha-glucosidase (GAA), and a method for purifying glycoside-cleaving enzymes produced in a cell line using the small molecule inhibitor-functionalized affinity resin.

A separation material includes a matrix that is bound to a saccharide, enabling the separation from a liquid of substances that selectively bind the saccharide. A method for preparing the separation material and a method for separating substances from a liquid that selectively bind a saccharide of the separation material are also described. A device employs the separation material for separating from a liquid substances that selectively bind to the saccharide of the separation material.

A separation material includes a matrix that is bound to a saccharide, enabling the separation from a liquid of substances that selectively bind the saccharide. A method for preparing the separation material and a method for separating substances from a liquid that selectively bind a saccharide of the separation material are also described. A device employs the separation material for separating from a liquid substances that selectively bind to the saccharide of the separation material.

A first Fab region-binding peptide includes an amino acid sequence selected from the group consisting of SEQ ID NOs: 1 to 5 with substitution of one or more amino acid residues at the 17.sup.th position and the 36.sup.th position, wherein an acid dissociation pH thereof is shifted to a neutral side. A second Fab region-binding peptide further includes deletion, substitution and/or addition of one or more amino acid residues at positions other than the 17.sup.th position and the 36.sup.th position. A third Fab region-binding peptide includes an amino acid sequence with a sequence identity of 80% or more to the amino acid sequence of the first Fab region-binding peptide.

The present disclosure is directed to surface modified materials such as stationary phase materials for performing size exclusion chromatography. Aspects of the present disclosure feature materials surface modified with a moiety including a polyethylene glycol (PEG) functionality and a moiety comprising a diol functionality. Such surface modified materials exhibit a reduced propensity for ionic and hydrophobic secondary interactions.

The present disclosure is directed to surface modified materials such as stationary phase materials for performing size exclusion chromatography. Aspects of the present disclosure feature materials surface modified with a moiety including a polyethylene glycol (PEG) functionality and a moiety comprising a diol functionality. Such surface modified materials exhibit a reduced propensity for ionic and hydrophobic secondary interactions.