The present invention relates to an esophageal cancer marker and application thereof. The present invention relates to: a marker that includes Glypican-1 or an expression product thereof, or a fragment or derivative thereof, and serves to identify esophageal cancer; a detection agent that includes a substance that binds to Glypican-1 or an expression product thereof; and a composition that includes a Glypican-1 inhibitor and serves to prevent or treat esophageal cancer. Herein, Glypican-1 can be SEQ ID NO: 1 (nucleic acid sequence) or SEQ ID NO: 2 (amino acid sequence), or an equivalent thereof.

The present disclosure provides antibodies that specifically bind to human FAM19A5 and compositions comprising such antibodies. Also provided herein are methods for treating fibrosis or cancer using the anti-FAM19A5 antibodies.

Compositions and methods reduce symptoms of human allergy to cats. The effectiveness of a molecule which specifically binds to Feline domesticus allergen number 1 (Fel D1) is enhanced by prolonging the time the immunoglobulin stays within the mouth of a cat to whom the anti-Fel D1 molecule is administered in a pet food. The compositions and methods use a powder that is a dried hydrogel encapsulating the anti-Fel D1 molecule, and the hydrogel is based on gelatin, collagen peptides, or gelatin and collagen peptides; and carrageenan. The methods of making the powder provide a high encapsulation efficacy, sustained release of the anti-Fel D1 molecule in the cat's mouth, and oral adhesion of the anti-Fel D1 molecule in the cat's mouth.

Provided herein, inter alia, are isolated antibodies that bind an extracellular domain of a human SIRP-α v1 polypeptide (e.g., the D1 domain), an extracellular domain of a human SIRP-α v2 polypeptide, or both. In some embodiments, the antibodies also bind an extracellular domain of a monkey SIRP-α polypeptide, an extracellular domain of a mouse SIRP-α polypeptide, an extracellular domain of a human SIRP-β polypeptide, and/or an extracellular domain of a human SIRP-γ polypeptide. In some embodiments, the antibodies block or do not binding between an extracellular domain of a human SIRP-α polypeptide and an IgSF domain of a human CD47 polypeptide, while in some embodiments, the antibodies reduce the affinity of a human SIRP-α polypeptide for binding an IgSF domain of a human CD47 polypeptide. Further provided herein are methods, polynucleotides, vectors, and host cells related thereto.

Embodiments provided herein are directed to the production and identification of antibodies, libraries of antibodies and libraries of antibodies produced in chickens and methods of using the same.

NT-proBNP can be determined in a biological sample using at least one antibody which recognizes an epitope of NT-proBNP in both a glycosylated and non-glycosylated form of NT-proBNP. Said antibody is preferably an isolated polyclonal antibody or a mixture of monoclonal antibodies coated onto a particle, preferably coated onto said particle in a coating ratio of 6-60%, forming a layer or multiple layers of antibodies on said particle. The assay, realized in the form of a nephelometric or turbidimetric assay, can be applied to a wide range of automated clinical analyzers.

The transgenic plants expressing one or more antagonist IL-10R peptides and anti-IL-10 single domain antibodies that stimulate or modulate the immune system and improve gastrointestinal physiology of an animal fed the transgenic plants or tissues thereof and the genes encoding the antagonist IL-10R peptides and anti-IL-10 single domain antibodies are described. The animal feed additives and animal feed incorporating the transgenic plants or tissues thereof are also described. Methods of stimulating or modulating an animal's immune system, improving an animal's gastrointestinal physiology, improving animal performance by using the transgenic plants or tissues thereof, and treating animals infected with a gastrointestinal pathogen are provided.

A method of making coated avian egg yolk cores includes providing dried avian egg yolk cores having a diameter of 100 to 1500 micrometers, applying avian egg albumen to the dried avian egg yolk cores to provide the coated avian egg yolk cores, and optionally drying the coated avian egg yolk cores, wherein the ratio of dry avian egg albumen to dried avian egg yolk in the coated avian egg yolk cores is 1:10 to 10:1. Also included are the coated avian egg yolk cores, food and feed additives containing the coated avian egg yolk cores and food and feed compositions containing the coated avian egg yolk cores.

The present invention provides compositions, kits, and methods for the detection of host cell proteins (HCPs) in biological samples. In some embodiments, the present invention utilizes immunization of ayes hosts with proteins derived from non-ayes host cells to produce ayes antibodies specific for non-ayes HCPs.

Provided herein, inter alia, are isolated antibodies that bind an extracellular domain of a human SIRP-α v1 polypeptide (e.g., the D1 domain), an extracellular domain of a human SIRP-α v2 polypeptide, or both. In some embodiments, the antibodies also bind an extracellular domain of a monkey SIRP-α polypeptide, an extracellular domain of a mouse SIRP-α polypeptide, an extracellular domain of a human SIRP-β polypeptide, and/or an extracellular domain of a human SIRP-γ polypeptide. In some embodiments, the antibodies block or do not binding between an extracellular domain of a human SIRP-α polypeptide and an IgSF domain of a human CD47 polypeptide, while in some embodiments, the antibodies reduce the affinity of a human SIRP-α polypeptide for binding an IgSF domain of a human CD47 polypeptide. Further provided herein are methods, polynucleotides, vectors, and host cells related thereto.