A fiber for protein adsorption has a water absorption percentage of 1 to 50%, and the fiber includes a polymer containing as repeat units an aromatic hydrocarbon or a derivative thereof, wherein part of aromatic rings contained in the repeat units are cross-linked through a structure represented by Formula (I). A column for protein adsorption uses the fibers. A in Formula (I) is selected from an alkyl aliphatic group, phenyl aromatic group and amino group.

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Tailored chromatographic media and methods for using the tailored chromatographic media to purify mixtures extracted from cannabis to obtain a cannabinoid having greater than about 90% purity. In an embodiment, the tailored chromatographic media may comprise a porous resin and/or porous carbon and have a surface area of greater than about 900 m2/g, wherein the tailored chromatographic media may further comprise micropores, mesopores, macropores, wherein the tailored chromatographic media may further comprise at least two distributions of macroporous pore sizes, wherein the at least two distributions of macroporous pore sizes may comprise a first population having a macroporous pore size denoted x and a second population having a macroporous pore size denoted y, wherein a ratio of x/y may be about 1:1, and wherein the tailored chromatographic media may further comprise an anionic polysaccharide and a functional moiety.

The present invention provides that powder is mainly constituted from secondary particles of hydroxyapatite. The secondary particles are obtained by drying a slurry containing primary particles of hydroxyapatite and aggregates thereof and granulating the primary particles and the aggregates. A bulk density of the powder is 0.65 g/mL or more and a specific surface area of the secondary particles is 70 m.sup.2/g or more. The powder of the present invention has high strength and is capable of exhibiting superior adsorption capability when it is used for an adsorbent an adsorption apparatus has.

A method of processing an aqueous solution, wherein the aqueous solution comprises one or more dissolved sugar, one or more dissolved sugar alcohol, or a mixture thereof, wherein the method comprises bringing the aqueous solution into contact with a collection of resin beads, wherein the resin beads comprise functional groups of structure (S1).

Provided herein are methods of reducing bioburden of a chromatography resin that include exposing a container including a composition including (i) a chromatography resin and (ii) a liquid including at least on alcohol to a dose of gamma-irradiation sufficient to reduce the bioburden of the container and the chromatography resin, where the at least one alcohol are present in an amount sufficient to ameliorate the loss of binding capacity of the chromatography resin after/upon exposure to the dose of gamma-irradiation. Also provided are reduced bioburden chromatography columns including the reduced bioburden chromatography resin, compositions including a chromatography resin and a liquid including at least one alcohol, methods of performing reduced bioburden column chromatography using one of these reduced bioburden chromatography columns, and integrated, closed, and continuous processes for reduced bioburden manufacturing of a purified recombinant protein.

The disclosure relates to chromatography ligands, e.g., chromatography ligands comprising at least two binding units and at least one spacer domain, wherein each binding unit comprises one or two immunoglobulin binding domains.

The subject invention pertains to proteins are purified by a mixed-mode chromatography system formed by attaching a ligand with cation exchange and hydrophobic 1,3-dioxoisoindolin-2-yl group functionalities to a large-pore support matrix, the only linkage between the ligand and the support matrix being a chain having a backbone of one, two, three, four, or five atoms between the hydrophobic group and the support matrix.

The invention relates to a method of isolating an immunoglobulin, comprising the steps of: a) providing a separation matrix comprising multimers of immunoglobulin-binding alkali-stabilized Protein A domains covalently coupled to a porous support: b) contacting a liquid sample comprising an immunoglobulin with the separation matrix; c) washing said separation matrix with a washing liquid; d) eluting the immunoglobulin from the separation matrix with an elution liquid, and e) cleaning the separation matrix with a cleaning liquid, wherein the alkali-stabilized Protein A domains comprise mutants of a parental Fc-binding domain of Staphylococcus Protein A (SpA).

The invention discloses a separation matrix which comprises a plurality of separation ligands, defined by the formula R.sub.1-L.sub.1-N(R.sub.3)-L.sub.2-R, immobilized on a support, wherein R.sub.1 is a five- or six-membered, substituted or non-substituted ring structure or a hydroxyethyl or hydroxypropyl group; L.sub.1 is either a methylene group or a covalent bond; R.sub.2 is a five- or six-membered, substituted or non-substituted ring structure; L.sub.2 is either a methylene group or a covalent bond; R.sub.3 is a methyl group; and wherein if R.sub.1 is a hydroxyethyl group and L.sub.1 is a covalent bond, R.sub.2 is a substituted aromatic ring structure or a substituted or non-substituted aliphatic ring structure.

A mobile phase including a lithium salt flows through a stationary phase including an oxygenated metal compound with affinity to the lithium salt through a Lewis acid-Lewis base interaction so that the oxygenated metal compound captures the lithium salt through the Lewis acid-Lewis base interaction. An eluent flows through the stationary phase to release the lithium salt captured by the oxygenated metal compound into the eluent. The eluent includes a Lewis base or a Lewis acid that disrupts the Lewis acid-Lewis base interaction between the lithium salt and the oxygenated metal compound. The eluent including the released lithium salt is collected after the eluent flows through the stationary phase.