Herein is reported a cultivation system for cultivating a pool of ovine B-cells or single deposited ovine B-cells in the presence of phorbol myristate acetate (PMA).

The present invention relates to the identification of a genomic integration site for heterologous polynucleotides in Chinese Hamster Ovary (CHO) cells resulting in high RNA and/or protein production. More specifically it relates to CHO cells comprising at least one heterologous polynucleotide stably integrated into the S100A gene cluster of the CHO genome and to methods for the production of said CHO cells. Further, the invention relates to a method for the production of a protein of interest using said CHO cell and to the use of said CHO cell for producing a protein of interest at high yield. Integration within these specific target regions leads to reliable, stable and high yielding production of an RNA and/or protein of interest, encoded by the heterologous polynucleotide.

Provided is an antibody or antibody fragment. The antibody or the antibody fragment includes HCDR1 selected from GYTFSSFS, GYTFSTFA, or GYSFTAYT, HCDR2 selected from ILPGSNST, ILPGINNT, ILPGGNNT, or INPYNGGT, and HCDR3 selected from SSYWFAY, STYWFAY, or AREGNYYGSRGDFDY; and LCDR1 selected from QSLLNSGNQKNY or QTIVTN, LCDR2 selected from GAS or YAS, and LCDR3 selected from QNAHSYPPT, QNAHSYPPA, or QQSHSWPFT. The provided antibody can be used for treating cancer.

The invention provides an antibody comprising human IgG1 or IgG3 heavy chain constant domains that are glycosylated with a sugar chain at Asn297, said antibody being characterized in that the amount of fucose within said sugar chain is at least 99%, and in addition the amount of NGNA is 1% or less and/or the amount of N-terminal alpha 1,3 galactose is 1% or less, and uses thereof.

The invention provides an antibody comprising human IgG1 or IgG3 heavy chain constant domains that are glycosylated with a sugar chain at Asn297, said antibody being characterized in that the amount of fucose within said sugar chain is at least 99%, and in addition the amount of NGNA is 1% or less and/or the amount of N-terminal alpha 1,3 galactose is 1% or less, and uses thereof.

The invention discloses methods for the generation of chimaeric human—non-human antibodies and chimaeric antibody chains, antibodies and antibody chains so produced, and derivatives thereof including fully humanised antibodies; compositions comprising said antibodies, antibody chains and derivatives, as well as cells, non-human mammals and vectors, suitable for use in said methods.

The invention discloses methods for the generation of chimaeric human—non-human antibodies and chimaeric antibody chains, antibodies and antibody chains so produced, and derivatives thereof including fully humanised antibodies; compositions comprising said antibodies, antibody chains and derivatives, as well as cells, non-human mammals and vectors, suitable for use in said methods.

The invention provides a method for culturing mammalian cells. The method provides greater control over cell o growth to achieve high product titer cell cultures.

The present disclosure is directed to methods for tuning the release profile of a biologic disposed in a hydrogel. Parameters that can be used for the tuning include a molar ratio of a nucleophilic group to an electrophilic group, the number of the nucleophilic groups in the first precursor, the number of the electrophilic groups in the second precursor, the molecular weight of the first precursor, the molecular weight of the second precursor, a weight ratio of the biologic and excipient to the hydrogel, a weight percentage of the biologic in a solid state formulation, and a ratio of surface area to volume of the hydrogel. The methods described herein allow the formation of hydrogel with different release profiles suitable for different therapeutic applications.

The present disclosure is directed to methods for tuning the release profile of a biologic disposed in a hydrogel. Parameters that can be used for the tuning include a molar ratio of a nucleophilic group to an electrophilic group, the number of the nucleophilic groups in the first precursor, the number of the electrophilic groups in the second precursor, the molecular weight of the first precursor, the molecular weight of the second precursor, a weight ratio of the biologic and excipient to the hydrogel, a weight percentage of the biologic in a solid state formulation, and a ratio of surface area to volume of the hydrogel. The methods described herein allow the formation of hydrogel with different release profiles suitable for different therapeutic applications.