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.

The disclosure provides a HER3 binding polypeptide, comprising a HER3 binding motif, BM, which motif consists of the amino acid sequence selected from i) EX.sub.2X.sub.3X.sub.4A X.sub.6X.sub.7EIW X.sub.11LPNL X.sub.16X.sub.17X.sub.18QX.sub.20 X.sub.21AFIX.sub.25 X.sub.26LX.sub.28D, and ii) an amino acid sequence which has at least 90% identity to the sequence defined in i), wherein the polypeptide binds to the extra-cellular domain of HER3. Also provided is a bispecific ligand having binding affinity for HER3 and for HER2, or for HER3 and for EGFR, and comprising a HER3. binding polypeptide as defined herein and a HER2 binding polypeptide or a EGFR binding polypeptide.

A series of protein A mutants having high alkali resistance, and methods of using the protein A mutants are provided. The protein A mutants have a high binding affinity for regions of immunoglobulin proteins other than the complementarity determining regions. The protein A mutants can be coupled to a solid support for immunoglobulin isolation, or conjugated to a label for immunoglobulin detection. This series of protein A mutants have high chemical stability under alkaline conditions of pH 13-14, and can also be used as chromatography ligands for purification procedures that use alkaline solutions under harsh conditions, such as Clean-In-Place (CIP). Also provided are methods of immunoglobublin separation and purification, and alkali regeneration of affinity chromatography medium that uses protein A as a ligand.

The present application relates to the use of bacterial minicells as targeted delivery agents in vivo and in vitro. Described herein are genetically engineered eubacterial minicells designed to preferentially target and deliver therapeutically relevant agents using a minicell surface coupling molecule capable of binding and displaying antibodies or other Fc-containing targeting moiety fusions and conjugates.

The invention relates to antibody conjugates (e.g., a bispecific antibody), drug and nanoparticle compositions and methods and compositions for generating them. This invention further relates to methods of using these compositions for imaging, diagnosing or treating a disease.

An object of the present invention is to provide a polypeptide having a high binding capacity for an immunoglobulin kappa chain, and having excellent alkali stability, by modifying an amino acid sequence of an immunoglobulin-binding domain of Protein L derived from Peptostreptococcus magnus. A polypeptide having a high binding capacity for an immunoglobulin kappa chain, and having excellent alkali stability can be obtained by substituting specific lysine residues in an immunoglobulin-binding domain of Protein L derived from Peptostreptococcus magnus 3316 strain, with a basic amino acid or a hydroxyl group-containing amino acid.

The invention relates to truncated growth factors and variants thereof. The invention also relates to methods of making and using the truncated growth factors. The invention further relates to compositions including a protease and a growth factor comprising a bone morphogenic protein (BMP) or a variant thereof. The invention also relates to methods of using the composition.

The present invention relates to novel affinity ligands for the affinity purification of ubiquitin muteins. In particular, the alkaline stable affinity ligands are useful for affinity chromatography purification and detection of a ubiquitin mutein (such as Affilin? protein). The novel affinity ligands for a ubiquitin mutein are based on artificial mosaic proteins of Protein A-like structure. The affinity ligands of the invention can be used for the purification and detection of ubiquitin muteins.

The present disclosure concerns agents and their use in the treatment of endocrine, nutritional and/or metabolic diseases in a mammal. The disclosure furthermore concerns novel peptide fragments.

In certain aspects, the present disclosure relates to the insight that a polypeptide comprising a truncated, ligand-binding portion of the extracellular domain of endoglin (ENG) polypeptide may be used to inhibit angiogenesis in vivo, particularly in mammals suffering angiogenesis-related disorders.