Abstract: In certain embodiments, the disclosure provides an IgG4 antibody comprising a heavy chain and a light chain, wherein the heavy chain comprises: (a) a modified IgG4 CH1 region having a substitution of the lysine residue at position 196; or (b) a modified IgG4 hinge region having a substitution of the serine residue at position 217, the glycine residue at position 220, the proline residue at position 224 or the proline residue at position 225. Preferably, the IgG4 antibody further comprises a substitution of the serine residue at position 228 in the heavy chain hinge region.

Abstract: In certain embodiments, the disclosure provides an IgG4 antibody comprising a heavy chain and a light chain, wherein the heavy chain comprises: (a) a modified IgG4 CH1 region having a substitution of the lysine residue at position 196; or (b) a modified IgG4 hinge region having a substitution of the serine residue at position 217, the glycine residue at position 220, the proline residue at position 224 or the proline residue at position 225. Preferably, the IgG4 antibody further comprises a substitution of the serine residue at position 228 in the heavy chain hinge region.

Abstract: The present invention describes methods and processes for the production of proteins, particularly glycoproteins, by animal cell or mammalian cell culture, preferably, but not limited to, fed-batch cell cultures. In one aspect, the methods comprise the addition of glucocorticoid compound during the culturing period. The addition of glucocorticoid compound sustain a high viability of the cultured cells, and can yield an increased end titer of protein product, and a high quality of protein product, as determined, e.g., by sialic acid content of the produced protein.

Abstract: The present invention describes methods and processes for the production of proteins, particularly glycoproteins, by animal cell or mammalian cell culture, preferably, but not limited to, fed-batch cell cultures. In one aspect, the methods comprise the addition of glucocorticoid compound during the culturing period. The addition of glucocorticoid compound sustain a high viability of the cultured cells, and can yield an increased end titer of protein product, and a high quality of protein product, as determined, e.g., by sialic acid content of the produced protein.

Abstract: The present invention provides methods for reducing glycoprotein aggregation by optimizing the number of O-linked glycosylation sites.

Abstract: The present invention describes methods and processes for the production of proteins, particularly glycoproteins, by animal cell or mammalian cell culture, preferably, but not limited to, fed-batch cell cultures. In one aspect, the methods comprise the addition of glucocorticoid compound during the culturing period. The addition of glucocorticoid compound sustain a high viability of the cultured cells, and can yield an increased end titer of protein product, and a high quality of protein product, as determined, e.g., by sialic acid content of the produced protein.

Abstract: The present invention describes methods and processes for the production of proteins, particularly glycoproteins, by animal cell or mammalian cell culture, preferably, but not limited to, fed-batch cell cultures. In one aspect, the methods comprise the addition of glucocorticoid compound during the culturing period. The addition of glucocorticoid compound sustain a high viability of the cultured cells, and can yield an increased end titer of protein product, and a high quality of protein product, as determined, e.g., by sialic acid content of the produced protein.

Abstract: The present invention describes methods and processes for the production of proteins, particularly glycoproteins, by animal cell or mammalian cell culture, preferably, but not limited to, fed-batch cell cultures. In one aspect, the methods comprise the addition of glucocorticoid compound during the culturing period. The addition of glucocorticoid compound sustain a high viability of the cultured cells, and can yield an increased end titer of protein product, and a high quality of protein product, as determined, e.g., by sialic acid content of the produced protein.

Abstract: The present invention describes a method for producing an antibody in Pichia pastoris, such as by fed-batch fermentation. The method includes the addition of about 2.0-5.0 g/L of hydroxyurea during the fermentation process to sustain a constant cell density and enhance the whole broth titer of the antibody. The method may also include a strategy of increasing the ethanol concentration to about 18-22 g/L and then maintaining the ethanol level at about 5-17 g/L to stabilize the cell mass and enhance the production rate of the antibody. The method may further include a respiratory quotient control for monitoring the ethanol profile and to improve the quality of the antibody by, for example, eliminating clipping of the heavy chain.

Abstract: The present invention describes a method for producing an antibody in Pichia pastoris, such as by fed-batch fermentation. The method includes a respiratory quotient control for monitoring the ethanol profile and to improve the quality of the antibody by, for example, eliminating clipping of the heavy chain. The method may also include a strategy of increasing the ethanol concentration to about 18-22 g/L and then maintaining the ethanol level at about 5-17 g/L to stabilize the cell mass and enhance the production rate of the antibody. The method may also include the addition of about 2.0-5.0 g/L of hydroxyurea during the fermentation process to sustain a constant cell density and enhance the whole broth titer of the antibody.

Abstract: The present invention provides methods for reducing glycoprotein aggregation by optimizing the number of O-linked glycosylation sites.

Abstract: The present invention describes a method for producing an antibody in Pichia pastoris, such as by fed-batch fermentation. The method may include a strategy of increasing the ethanol concentration to 18-22 g/L and then maintaining the ethanol level at 5-17 g/L to stabilize the cell mass and enhance the production rate of the antibody. The method may also include the addition of 2.0-5.0 g/L of hydroxyurea during the fermentation process to sustain a constant cell density and enhance the whole broth titer of the antibody. The method may further include a respiratory quotient control for monitoring the ethanol profile and to improve the quality of the antibody by, for example, eliminating clipping of the heavy chain.

Abstract: The present invention describes a method for producing an antibody in Pichia pastoris, such as by fed-batch fermentation. The method may include a strategy of increasing the ethanol concentration to 18-22 g/L and then maintaining the ethanol level at 5-17 g/L to stabilize the cell mass and enhance the production rate of the antibody. The method may also include the addition of 2.0-5.0 g/L of hydroxyurea during the fermentation process to sustain a constant cell density and enhance the whole broth titer of the antibody. The method may further include a respiratory quotient control for monitoring the ethanol profile and to improve the quality of the antibody by, for example, eliminating clipping of the heavy chain.

Abstract: The present invention describes methods and processes for the production of proteins, particularly glycoproteins, by animal cell or mammalian cell culture, preferably, but not limited to, fed-batch cell cultures. In one aspect, the methods comprise the addition of glucocorticoid compound during the culturing period. The addition of glucocorticoid compound sustain a high viability of the cultured cells, and can yield an increased end titer of protein product, and a high quality of protein product, as determined, e.g., by sialic acid content of the produced protein.