The present invention relates to: a method of purifying an antibody, which can prepare a desired antibody with high purity and high quality by removing impurities without using an expensive protein A column, and particularly, can purify an antibody in a high yield while greatly reducing an amount (volume) of a buffer used in an elution process; and an antibody prepared by the method.

A method for producing lithium hydroxide that allows reducing a load of removing divalent or more ions with an ion-exchange resin is provided. The method for producing lithium hydroxide includes steps (1) to (3) below. (1) a neutralization step: a step of adding an alkali to a first lithium chloride containing liquid to obtain a post-neutralization liquid, (2) an ion-exchange step: a step of bringing the post-neutralization liquid into contact with an ion-exchange resin to obtain a second lithium chloride containing liquid, and (3) a conversion step: a step of electrodialyzing the second lithium chloride containing liquid to obtain a lithium hydroxide containing liquid. Since this producing method allows roughly removing divalent or more ions in the neutralization step, a load of metal removal with the ion-exchange resin is reducible.

A process for purifying a composition comprising water, a target substance, impurities and optionally cells, the process comprising the steps (A) and (B): (A) preparing a liquid feedstock by performing step (Ai) and/or (Aii) on the composition: (Ai) removing at least some of the cells from the composition; (Aii) concentrating the composition by removing water therefrom; and (B) passing the liquid feedstock through an apparatus comprising at least two processing units, each such unit producing a product stream containing purified target substance and optionally a waste stream comprising at least some of the impurities, wherein each unit comprises specified components (i) to (v). 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.

In various aspects, the present disclosure pertains to methods of performing a sample enrichment procedure, which comprise: adding a sample fluid that comprises at least one phospholipid and at least one target analyte to a sorbent that comprises a hydrophobic component and a cation exchange component, thereby resulting in sorbent with bound phospholipid and bound target analyte; adding an aqueous solution comprising an acidic compound and a salt; adding an organic solution to the sorbent thereby desorbing at least a portion of the bound phospholipid from the sorbent; and adding an elution solution to the sorbent, thereby desorbing at least a portion of the bound target analyte from the sorbent and forming a solution of the target analyte in the elution solution. In other aspects, the present disclosure pertains to kits, which may be used in conjunction with such methods.

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.

Disclosed herein are methods of electrochemically enhanced amine-based CO.sub.2 capture and systems for performing the methods of amine-based CO.sub.2 capture. The present methods and systems advantageously may be carried out at ambient temperatures and allow for reusing the amine through multiple cycles.

The present disclosure provides methods for producing consumable recombinant proteins that are substantially free from herein-disclosed undesired byproducts.

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.