The present disclosure provides activated formylglycine-generating enzymes (FGE), methods of producing activated FGE, and their use in methods of producing a protein comprising a formylglycine (FGly) residue. The methods of producing activated FGE, as well as methods of use of activated FGE in producing FGly-containing proteins, include both cell-based and cell-free methods. Compositions and kits that find use, e.g., in practicing the methods of the present disclosure are also provided.

The present invention relates to anti-CLL-1 antibodies including anti-CLL-1 antibodies comprising a CLL-1 binding domain and a CD3 binding domain (e.g., anti-CLL-1/CD3 T cell dependent bispecific (TDB) antibody) and methods of using the same.

The invention generally relates to anti-sclerostin antibodies having C-terminal modifications, and compositions comprising such antibodies.

The present invention provides inhibitors of fucosylation during protein expression from mammalian cells. The inhibitors are derived from rhamnose and act by inhibition of GDP-mannose 4,6-dehydratase (GMD). The invention further provides methods of making proteins with reduced level of fucosylation, such as antibodies and antibodies made by the methods of the present invention. Such hypofucosylated or nonfucosylated antibodies may find use, for example, in treatment of human disease in which is it therapeutically eneficial to direct antibody dependent cellular cytotoxicity (ADCC) mediated killing of cells expressing the antibody target on their surface, for example in depletion of Tregs in cancer patients using a hypofucosylated or nonfucosylated anti-CTLA-4 antibody.

The invention relates to antibodies and derivatives thereof such as bispecific antibodies and chimeric antigen receptors (CARs) with affinity matured and/or humanized targeting domains specific to the ROR2 antigen. The invention encompasses the nucleic acids and vectors encoding said antibodies and derivatives, the cells and pharmaceutical compositions containing them, in particular for their use in cancer therapy.

This invention provides binding proteins, including antibodies, antibody derivatives and antibody fragments, that specifically bind a CD154 (CD4OL) protein. This invention also provides a chimeric, humanized or fully human antibody, antibody derivative or antibody fragment that specifically binds to an epitope to which a humanized Fab fragment comprising a variable heavy chain sequence according to SEQ ID NO: 1 and comprising a variable light chain sequence according to SEQ ID NO: 2 specifically binds. CD154 binding proteins of this invention may elicit reduced effector function relative to a second anti-CD154 antibody. CD154 binding proteins of this invention are useful in diagnostic and therapeutic methods, such as in the treatment and prevention of diseases including those that involve undesirable immune responses that are mediated by CD154-CD40 interactions.

The present invention, in the field of bioengineering and biotechnology, relates to a method for preparing a recombinant antibody with a unique glycan profile produced by a genome-edited CHO host cell. Specifically, according to a method of the present invention, the TALEN technology is used to edit the FUT8 gene in CHO cells that have been adapted for serum-free suspension growth. The edited CHO host cells can produce recombinant antibodies with a unique glycan profile. The unique glycan profile can be characterized by non-fucosylated N-linked oligosaccharide chains of the antibodies, extremely low N-glycosylation heterogeneity and uniform carbohydrate chains. The antibody prepared by the method of the invention exhibit significantly increased ADCC and greater stability.

The present disclosure relates to methods for selectively reducing CysL97 in a preparation of IL-17 antibodies or antigen binding fragments thereof (e.g., a preparation of secukinumab antibodies) that have been recombinantly produced by mammalian cells. Also provided are purified preparations of IL-17 antibodies or antigen binding fragments thereof produced by such methods, e.g., purified preparations of secukinumab, wherein the level of intact IL-17 antibodies or antigen binding fragments thereof (e.g., secukinumab) in the preparation is high, e.g., at least about 90%, as measured by sodium dodecyl sulfate capillary electrophoresis (CE-SDS), and wherein the level of activity of IL-17 antibodies or antigen binding fragments thereof (e.g., secukinumab) in the preparation is high, e.g., at least about 92%, as measured by cation exchange chromatograph (CEX).

A method for refolding an antibody, a process for producing a refolded antibody, a refolded antibody, and uses thereof are provided. A method for refolding an antibody in a liquid phase comprises the steps of denaturing an inactive antibody binding directly or through a linker to a peptide, the peptide having an isoelectric point lower than the isoelectric point of the inactive antibody, and dispersing in a liquid phase the peptide-binding inactive antibody denatured in the step above. Also provided is a process for producing a refolded antibody.

The present disclosure relates to compositions for treating interleukin 5 (IL-5) mediated diseases, and related methods.