Anti-CD40L antibodies and antigen binding fragments thereof, compositions comprising the antibodies or antigen binding fragments, Anti-CD40L antibodies with reduced effector function, and method of using same for treatment of CD40L-related diseases or disorders.

Antibodies that selectively bind to glycosylated LAG3 relative to unglycosylated LAG3 are provided. In some aspects, LAG3 polypeptides comprising glycosylated amino acid positions are also provided. Methods for making and using such antibodies and polypeptides (e.g., for the treatment of cancer) are also provided.

Isolated antibodies and immunoconjugates that specifically bind Frizzled receptor (FZD) 4 cysteine rich domain (CRD) comprising a light chain variable region and a heavy chain variable region, the heavy chain variable region comprising complementarity determining regions CDR-H1, CDR-H2 and CDR-H3, the light chain variable region comprising complementarity determining region CDR-L1, CDR-L2 and CDR-L3, and with the amino acid sequences of said CDRs comprising or consisting of sequences selected from sequences in Table 1a or 3a. Methods of using the antibodies and immunoconjugates are also provided.

The present invention relates to a method for producing the anti-IL36R antibody spesolimab. More specifically, the present invention relates to a method of producing spesolimab with a serum-free cell culture medium in a fed-batch culture in the presence of reduced copper and increased iron concentrations. In addition, the present invention relates to a composition comprising low levels of basic species of spesolimab and/or low levels of spesolimab species with high mannose structures.

A population of antibodies, wherein less than 80% of the oligosaccharides covalently attached to the population of the antibodies via N297 residues thereof comprise a core fucose residue; and wherein the population of the antibodies comprises an antibody which Fc region comprises K338A and T437R mutations, or K248E and T437R mutations.

The present invention relates to an in vitro method for production of heterodimeric proteins.

The present invention relates to a process for the enzymatic modification of a glycoprotein. The process comprises the step of contacting a glycoprotein comprising a glycan comprising a terminal GlcNAc-moiety, in the presence of glycosyltransferase that is, or is derived from, a β-(1,4)-N-acetylgalactosaminyltransferase, with a non-natural sugar-derivative nucleotide. The non-natural sugar-derivative nucleotide is according to formula (3):

##STR00001##

wherein A is selected from the group consisting of —N.sub.3, —C(O)R.sup.3, —(CH.sub.2).sub.iC≡C—R.sup.4, —SH, —SC(O)R.sup.8, —SC(O)OR.sup.8, —SC(S)OR.sup.8, —F, —Cl, —Br —I, —OS(O).sub.2R.sup.5, terminal C.sub.2-C.sub.24 alkenyl groups, C.sub.3-C.sub.5 cycloalkenyl groups, C.sub.4-C.sub.8 alkadienyl groups, terminal C.sub.3-C.sub.24 allenyl groups and amino groups. The invention further relates to a glycoprotein obtainable by the process according to the invention, to a bioconjugate that can be obtained by conjugating the glycoprotein with a linker-conjugate, and to β-(1,4)-N-acetylgalactosaminyltransferases that can be used in preparing the glycoprotein according to the invention.

The present invention relates to peptides, proteins, nucleic acids and cells for use in immunotherapeutic methods. In particular, the present invention relates to the immunotherapy of cancer. The present invention furthermore relates to tumor-associated T-cell peptide epitopes, alone or in combination with other tumor-associated peptides that can for example serve as active pharmaceutical ingredients of vaccine compositions that stimulate anti-tumor immune responses, or to stimulate T cells ex vivo and transfer into patients. Peptides bound to molecules of the major histocompatibility complex (MHC), or peptides as such, can also be targets of antibodies, soluble T-cell receptors, and other binding molecules.

Provided herein are anti-MARCO antibodies. Provided are also methods of generating and using anti-MARCO antibodies.

The invention provides an oriented and covalent method for immobilizing a glycoprotein and an antibody on a chip. The method includes providing a silver-coated solid surface equipped with alkynes and cuprous oxide nanoparticles. The azido boronic acid tosyl probe is conjugated to the silver-coated solid surface by the cuprous oxide nanoparticles through the self-catalyzed azide-alkyne cycloaddition reaction. The glycan(s) of a glycoprotein or an antibody is provided to the boronic acid tosyl probe, and alcohol groups of the glycan(s) of the glycoprotein or the antibody and the boronic acid group of boronic acid tosyl probe form boronate ester. The nucleophilic residues on the glycoprotein or the antibody replace the tosyl group by SN2 reaction, so as to immobilize the glycoprotein or the antibody through the covalent bond formation.