The present disclosure provides, in some embodiments, devices, methods, and kits for purifying extracellular vesicles (EVs) using size exclusion chromatography in tandem with cation exchange chromatography, which can be referred to as dual-mode chromatography (DMC).

The present invention relates generally to processes for production of heavily glycosylated recombinant proteins (e.g., mucins and mucin-like proteins, such as lubricin), the processes comprising culturing mammalian cells capable of producing a glycoprotein in a liquid medium in a system comprising one or more bioreactors, concentrating and purifying and formulating the glycoprotein, the purification comprising one or more steps of chromatography, an endonuclease step, and at least one step of viral inactivation. In certain aspects the invention relates to pharmaceutical compositions comprising purified recombinant human lubiricin, and methods of treating a subject in need thereof.

The present disclosure provides a process for assaying stability of monovalent and/or multivalent, liquid and lyophilized polysaccharide protein conjugate vaccine compositions using HPLC-SEC method. The method provides stability analysis (lot to lot) of polysaccharide protein conjugate vaccine with respect to aggregation profile, molar mass distribution and/or molecular size distribution, and data can be utilized for quality control during storage and batch release. The method is performed in the presence of multiple carrier proteins, free polysaccharides and excipient, without any interference of said components.

An ion exchange resin bag 5 includes a bag body 51 and a reinforcing body 52. The bag body 51 has a bottom surface portion 511 that is provided at an end portion opposite to an end portion where an opening is provided and forms a bottom surface of the bag body, and a side surface portion 512 that is connected to the bottom surface portion 511 and forms a side surface of the bag body 51. The reinforcing body 52 has a first reinforcing portion 521 that is fixed to a boundary portion of the bottom surface portion 511 and the side surface portion 512, and a second reinforcing portion 522 that is connected to the first reinforcing portion 521 and fixed to at least a part of the side surface portion 512 and extends from the first reinforcing portion 521 toward the opening.

Systems and methods are described in which proteins are isolated from complex solution using successive chromatographic separations that retain the protein of interest in the flow-through. At least one of the chromatography media used is selected to be capable of interacting with both contaminants and the protein of interest, however capacity of this media is selected such that the protein of interest is displaced and remains in the flow-through.

The present invention provides novel and improved protein purification processes which incorporate certain types of carbonaceous materials and result in effective and selective removal of certain undesirable impurities without adversely affecting the yield of the desired protein product.

The present invention relates to a method of preparing a population of antibodies, whereby a desired high-purity and high-quality population of antibodies can be prepared by removing impurities without using an expensive protein A column, and in particular, production costs can be significantly reduced while achieving process automation; and a population of antibodies prepared thereby.

A chromatography device (201; 201′) comprising: – at least one chromatography material unit (203), wherein said chromatography material unit comprises a convection-based chromatography material and is of a substantially rectangular shape having a length (L) and a width (W); - at least one fluid distribution system (207) which is configured to distribute fluid into and out from the at least one chromatography material unit (203), wherein said fluid distribution system (207) comprises a distribution device (209a) and a collection device (209b) between which said chromatography material unit (203) is sandwiched, wherein said distribution device (209a) and said collection device (209b) each comprises a number of parallel grooves (255) for distribution and collection respectively of a fluid to be passed through the chromatography material unit (203), wherein said parallel grooves are reaching over substantially the whole length (L) of the chromatography material unit (203) and are distributed over substantially the whole width (W) of the chromatography material unit (203).

Apparatus for purifying a liquid comprising a target substance comprising at least two units arranged in series such that the feed stream of the second and any subsequent units comprises the product stream from a downstream unit, wherein each unit comprises specified components (i) to (vi), including a a switchable bypass assembly. Also claimed are the units and a flowpath assembly. The units may be essentially the same except for a device they contain, leading to advantages in terms of simplicity, cost and ease of operation, lower risk of operator error, easier maintenance and lower inventory of spare parts.

The disclosure relates to a method for separation and purification of N-acetyl-glucosamine, and belongs to the technical field of biological engineering. In the disclosure, a raw material solution containing N-acetyl-glucosamine is obtained by microbial fermentation or by hydrolyzing the chitin. The raw material solution is subjected to flocculation pretreatment, and continuous centrifugation or pressure filtration is performed to remove suspended solids such as microorganisms, proteins and polysaccharides to obtain clear liquid. Double-stage ion exchange chromatography is performed to remove impurities such as charged organic molecules and inorganic salts. Membrane concentration is performed to efficiently remove water to improve the concentration of the target product. Spray drying or further evaporation concentration and crystallization are performed. Finally drying is performed to obtain an N-acetyl-glucosamine crystal of which the purity is more than 99%.