An improved method for purifying Gc protein to a high purity, and a method for producing GcMAF are provided.

According to the present disclosure, Gc protein is purified through a combination of affinity chromatography and anion exchange chromatography, and thus, Gc protein can be purified to a higher purity as compared with a conventional purification method using affinity chromatography alone. As a result, GcMAF can be efficiently produced.

The present invention relates to the field of molecular biology and cell biology. More specifically, the present invention relates to a CRISPR-Cas system for a Labyrinthulomycetes host cell.

The present invention relates to the field of molecular biology and cell biology. More specifically, the present invention relates to a CRISPR-Cas system for a Labyrinthulomycetes host cell.

Microorganisms and bioprocesses are provided that convert gaseous substrates, such as renewable H.sub.2 and waste CO.sub.2 producer gas, or syngas into high-protein biomass that may be used directly for human nutrition, or as a nutrient for plants, fungi, or other microorganisms, or as a source of soil carbon, nitrogen, and other mineral nutrients. Renewable H.sub.2 used in the processes described herein may be generated by electrolysis using solar or wind power. Producer gas used in the processes described herein may be derived from sources that include gasification of waste feedstock and/or biomass residue, waste gas from industrial processes, or natural gas, biogas, or landfill gas.

The present invention relates to the finding of methods to shift the glycosylation profile of recombinant produced semm glycoproteins to the predominant bi-antennary form found in human plasma. This is accomplished by providing a mammalian cell line according to the invention with a series of gene disruptions and/or gene insertions that facilitate this shift.

The present invention contemplates a method of producing a recombinant protein comprising (a) fermenting a prokaryotic host cell wherein said prokaryotic host cell has been transformed with a nucleic acid encoding said recombinant protein, and (b) harvesting said recombinant protein under conditions where dO.sub.2 levels are greater than 0%, and (c) purifying said recombinant protein to a filtered bulk, wherein said filtered bulk does not contain detectable DHNA-recombinant protein adduct, as measured by an IEC assay at 310 nm. The present invention also contemplates a method of producing a recombinant protein comprising (a) fermenting a menE gene-deleted prokaryotic host cell wherein said prokaryotic host cell has been transformed with a nucleic acid encoding said recombinant protein, (b) harvesting said recombinant protein; and (c) purifying said recombinant protein to a filtered bulk, wherein said filtered bulk does not contain detectable DHNA-recombinant protein adduct, as measured by an IEC assay at 310 nm, and wherein the recombinant protein yield is increased by about 20% or greater.

The present invention contemplates a method of producing a recombinant protein comprising (a) fermenting a prokaryotic host cell wherein said prokaryotic host cell has been transformed with a nucleic acid encoding said recombinant protein, and (b) harvesting said recombinant protein under conditions where dO.sub.2 levels are greater than 0%, and (c) purifying said recombinant protein to a filtered bulk, wherein said filtered bulk does not contain detectable DHNA-recombinant protein adduct, as measured by an IEC assay at 310 nm. The present invention also contemplates a method of producing a recombinant protein comprising (a) fermenting a menE gene-deleted prokaryotic host cell wherein said prokaryotic host cell has been transformed with a nucleic acid encoding said recombinant protein, (b) harvesting said recombinant protein; and (c) purifying said recombinant protein to a filtered bulk, wherein said filtered bulk does not contain detectable DHNA-recombinant protein adduct, as measured by an IEC assay at 310 nm, and wherein the recombinant protein yield is increased by about 20% or greater.

This invention relates generally to pharmaceutical compositions and preparations of circular polyribonucleotides and uses thereof.

This invention relates generally to pharmaceutical compositions and preparations of circular polyribonucleotides and uses thereof.

The invention is a method of preventing the generation of pink color during antibody manufacturing by either preventing the reduction of antibodies during manufacturing and harvest or inhibiting the conversion of cyanocobalamin (CN-Cbl) to hydroxocobalamin (HO-Cbl) during manufacturing and harvest. Replacement of white light in the cell culture media preparation and storage areas with red light inhibits the conversion of CN-Cbl to HO-Cbl. Addition of peroxides to the clarified bulk at harvest inhibits reduction of the antibody disulfide bonds.