Compositions and methods are provided for producing materials having increased immunoglobulin binding capacities, the materials including full-length or truncated forms of protein A, protein G, protein A/G, protein L and other immunoglobulin-binding proteins or peptides, which moieties contain polypeptide domains, or polypeptide-oligopeptide combinations. Also provided are separation matrices containing the moieties and methods of using the separation matrices for separation of immunoglobulins or immunoglobulin containing proteins.

The present disclosure is generally directed to an anucleated cell-based platforms for encapsulation and delivery of agricultural compounds. Disclosed herein are compositions for the stable and targeted delivery of agricultural compounds within achromosomal and/or anucleated cells. The present disclosure also provides methods of improving encapsulation and retention of agricultural compounds in achromosomal and/or anucleated cells,

A method of modifying a glycosylation pattern of a polypeptide-of-interest in a plant or plant cell is provided. The method comprising expressing in a plant or plant cell transformed to express at least one glycosidase in a subcellular compartment, a nucleic acid sequence encoding the polypeptide-of-interest, such that the at least one glycosidase and the polypeptide-of-interest are co-localized to the subcellular compartment of the plant or plant cell, thereby modifying the glycosylation pattern of the polypeptide-of-interest in the plant or plant cell.

The present invention is within the field of protein engineering and purification. The invention relates to a target-binding polypeptide mutant of an IgG binding polypeptide, such as Protein A, Protein G, Protein L or Protein M, comprising a metal binding motif. More closely the invention relates to an Fc binding ligand comprising an engineered protein based on the Protein A derived Z domain, to which a calcium binding EF-loop has been introduced.

A method for detecting the binding of a chromatin-associated factor of interest to a sequence of chromatin DNA in a cell, including: contacting a permeabilized cell or nucleus with a specific binding agent that specifically recognizes the chromatin-associated factor of interest, wherein the specific binding agent is linked to a nuclease that is inactive or an activatable transposome; activating the nuclease or transposase, thereby excising the sequence of chromatin DNA bound to the chromatin-associated factor of interest; isolating the excised DNA; and determining the sequence of the excised DNA, thereby detecting binding of a chromatin-associated factor of interest to a sequence of chromatin DNA in the cell.

A method for detecting the binding of a chromatin-associated factor of interest to a sequence of chromatin DNA in a cell, including: contacting a permeabilized cell or nucleus with a specific binding agent that specifically recognizes the chromatin-associated factor of interest, wherein the specific binding agent is linked to a nuclease that is inactive or an activatable transposome; activating the nuclease or transposase, thereby excising the sequence of chromatin DNA bound to the chromatin-associated factor of interest; isolating the excised DNA; and determining the sequence of the excised DNA, thereby detecting binding of a chromatin-associated factor of interest to a sequence of chromatin DNA in the cell.

Provided herein are methods and compositions for purifying antibodies. Purification is achieved by increasing the binding capacity of protein A chromatography by covalent attachment of a protein A domain (E, D, A, B, C), or domain Z, or a functional variant thereof, to Drosophila melanogaster transcription factor Ultrabithorax (Ubx) materials. The compositions include fusion proteins containing Drosophila melanogaster transcription factor Ultrabithorax (Ubx) or a fragment thereof and an immunoglobulin binding protein. In some embodiments, the immunoglobulin binding protein is a protein A domain, a protein Z domain or a fragment thereof.

Described herein are novel compositions comprising, for example, PDCL3 polypeptides having VEGFR-2 inhibitory activity, inhibitory PDCL3 antibodies and PDCL3-binding fragments thereof, or PDCL3 inhibitory nucleic acid molecules, and methods of their use in anti-angiogenesis and anti-tumor proliferation and invasiveness therapies, such as the treatment of cancer, as well as the treatment of those vascular diseases where pathological angiogenesis plays a role, such as in carotid artery disease, macular degeneration, and plaque neovascularization. Also described herein are novel compositions comprising engineered PDCL3 polypeptides having enhanced chaperone activity, recombinant cells comprising such engineered PDCL3 polypeptides having enhanced chaperone activity, and methods thereof for therapeutic protein production and in vitro protein synthesis.

The present invention pertains to extracellular vesicle (EV) therapeutics, wherein the EVs are coated with proteins containing Fc domains (such as antibodies) for i.a. targeting and therapeutic applications. The coating of EVs is achieved through inventive protein engineering of EV polypeptides. The present invention thus relates to methods for coating of EVs, EVs per se, as well as pharmaceutical compositions and medical applications of such EVs coated with Fc containing proteins.

The present invention relates to the field of protein engineering and purification and relates in particular to novel polypeptides having a triple-helical structure and lacking binding affinity for the Fc domain of immunoglobulin. The invention further relates to uses of the novel non-Fc binding polypeptides in technical applications such as affinity chromatography, as well as in therapy and diagnostics. In addition, the present invention relates to a method of reducing the binding affinity of a polypeptide having a triple-helical structure for the Fc domain of immunoglobulin.