The invention provides means and methods for producing one or more Ig-like molecules in a single host cell. Novel CH3 mutations enabling the production of monospecific and/or bispecific Ig-like molecules of interest are also provided.

The invention provides means and methods for producing one or more Ig-like molecules in a single host cell. Novel CH3 mutations enabling the production of monospecific and/or bispecific Ig-like molecules of interest are also provided.

Disclosed are compositions and methods related to variable lymphocyte receptors (VLRs). More particularly, disclosed are a variety of antigen specific polypeptides, including soluble, monoclonal, and multivalent forms, as well as methods of using the polypeptides, antibodies that bind the antigen specific polypeptides, and nucleic acids, vectors and expression systems that encode the polypeptides. Antigen specific polypeptides that selectively bind pathogens, like anthrax, and carbohydrates, like blood group determinants, are specifically disclosed.

Affinity constructs and affinity molecules to direct insecticidal toxins to insect specific structures of target insects are presented herein. The affinity constructs comprise of at least one affinity molecule that is capable of recognizing, or capable of binding to, or binding to, or being directed to, or being designed to bind to an insect-specific structure in and/or on a target insect, and at least one other affinity molecule capable of binding to, or binding to, or being directed to, or being designed to bind to an insecticidal protein (toxin) wherein the at least two affinity molecules are operably coupled. Presented herein are also methods of making and using these affinity constructs and affinity molecules.

Provided are compositions, methods and kits that are useful for detecting, inhibiting the growth of, and killing bacteria. The compositions include recombinant, chimeric polypeptides that contain at least one immunoglobulin fragment crystallizable region (Fc) segment and at least one additional segment that contains a binding domain that is specific for a bacterial cell wall substrate. The binding domain is one from one or more of a bacterial autolysin, a bacteriophage lysin, a bacteriophage tail or tail fiber, or a bacteriocin. Method of using the polypeptides for detecting, inhibiting the growth of, and killing bacteria are provided and involve contacting bacteria with the polypeptides. Methods of making the polypeptides include expressing the polypeptides in cells, and separating the polypeptides from the cells. Polynucleotides, such as expression vectors, that encode the chimeric polypeptides are also provided.

Affinity constructs to direct insecticidal toxins to insect specific structures of target insects are presented herein. The affinity constructs comprise of at least one affinity molecule that is capable of recognizing, or capable of binding to, or binding to, or being directed to, or being designed to bind to an insect-specific structure in and/or on a target insect, and at least one other affinity molecule capable of binding to, or binding to, or being directed to, or being designed to bind to an insecticidal protein (toxin) wherein the at least two affinity molecules are operably coupled. Presented herein are also methods of making and using these affinity constructs.

The present invention relates to antibodies that are heterodimeric and bind human PD-L1 and human TIM-3, and may be useful for treating cancer alone and in combination with chemotherapy and other cancer therapeutics.

Methods, compositions and kits are provided for treating a subject exposed to or at risk for exposure to a disease agent using a pharmaceutical composition including at least one recombinant binding protein or a source of expression of the binding protein, wherein the binding protein neutralizes a disease agent that is a toxin, for example a Clostridium difficile toxin, a Shiga toxin, a ricin toxin, or an anthrax toxin.

A single-domain antibody (sdAb) is produced by causing a bacteria to express the sdAb into cytoplasm of the bacteria, wherein the sdAb is expressed as a fusion protein with the acid tail of -synuclein. In embodiments, the protein is free of a periplasmic location tag. Such antibodies have the unexpected ability to refold after thermal denaturation.

A nucleic acid encodes a single-domain antibody (sdAb) is produced by causing a bacteria to express the sdAb into cytoplasm of the bacteria, wherein the sdAb is expressed as a fusion protein with the acid tail of -synuclein. In embodiments, the protein is free of a periplasmic location tag. Such antibodies have the unexpected ability to refold after thermal denaturation.