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

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 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.

Rapid, animal protein free, chromatographic processes and systems for obtaining high potency, high yield botulinum neurotoxin for research, therapeutic and cosmetic use.

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.

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 wash buffer comprising a surfactant for use in affinity and cation exchange chromatography to purify proteins of interest from protein aggregates and to remove and/or inactivate viruses. When used during affinity or cation exchange chromatography for the purification of a protein of interest, such as an antibody, the wash buffer significantly improves viral clearance from the preparation, while also reducing the levels of host cell proteins and protein aggregates. Following affinity or cation exchange chromatography with the wash buffer, the protein of interest may be further purified using other chromatography and filtration operations.

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%.