Abstract: Antibodies that bind specifically to glycosylated PD-L1 relative to unglycosylated PD-L1, block binding of PD-L1 to PD-1 and promote internalization and degradation of PD-L1 are provided. Antibodies that recognize specific epitopes on glycosylated PD-L1 protein and that exhibit the dual functions of both blocking the binding of PD-L1 to PD-1 and also facilitating the internalization of PD-L1 on cells are provided. In some aspects, PD-L1 polypeptides comprising glycosylated amino acid residues at amino and carboxy terminal positions of the PD-L1 extracellular domain are also provided. Methods for using such antibodies for the treatment of cancer, particularly PD-L1 positive cancer, are also provided.

Abstract: Provided herein are molecules, such as antibodies, that selectively bind to glycosylated BTLA (B- and T-lymphocyte attenuator) relative to unglycosylated BTLA. Methods for making and using such molecules are also provided, including methods for treating or diagnosing cancer. In some embodiments, the anti-glycosylated BTLA antibodies provided herein can immunospecifically bind to glycosylated wild-type BTLA (WT). In some embodiments, the anti-glycosylated BTLA antibodies provided herein can immunospecifically bind to one or more BTLA double mutants that retain only a single glycosylation site at BTLA N75, N94 or N110. In some embodiments, the anti-glycosylated BTLA antibodies provided herein show only background binding, if any, to a BTLA triple mutant, that retains none of BTLA's N75, N94, or N110 0-glycosylation sites.

Abstract: An equine therapy boot that has an insulating shaft that can be securely fastened at multiple locations on an equine leg and hold a volume of therapeutic media to treat the equine hoof and leg is disclosed herein. The equine therapy boot includes a sole member, an internal securing mechanism, and an insulating shaft configured to retain therapeutic media. Advantageously, this equine therapy boot secures the horse's hoof to the sole member such that the insulating shaft is not displaced from the horse's hoof and leg during the treatment period. Also disclosed herein are methods of treating a diseased or injured horse's hoof and leg with the disclosed equine therapy boot.

Abstract: Provided herein are molecules having an antigen binding fragment that immuno specifically binds to BTN1A1, such as anti-BTN1A1 antibodies. These molecules include those having an antigen binding fragment that immuno specifically binds to BTN1A1 dimers, such as anti-BTN1A1 dimer antibodies. Methods of making and using these molecules are also provided, including methods of using them in cancer therapies, or as cancer diagnostics.

Abstract: Antibodies that bind specifically to glycosylated PD-L1 relative to unglycosylated PD-L1, block binding of PD-L1 to PD-1 and promote internalization and degradation of PD-L1 are provided. Antibodies that recognize specific epitopes on glycosylated PD-L1 protein and that exhibit the dual functions of both blocking the binding of PD-L1 to PD-1 and also facilitating the internalization of PD-L1 on cells are provided. In some aspects, PD-L1 polypeptides comprising glycosylated amino acid residues at amino and carboxy terminal positions of the PD-L1 extracellular domain are also provided. Methods for using such antibodies for the treatment of cancer, particularly PD-L1 positive cancer, are also provided.

Abstract: Provided herein are molecules, such as antibodies, that selectively bind to glycosylated BTLA (B- and T-lymphocyte attenuator) relative to unglycosylated BTLA. Methods for making and using such molecules are also provided, including methods for treating or diagnosing cancer. In some embodiments, the anti-glycosylated BTLA antibodies provided herein can immunospecifically bind to glycosylated wild-type BTLA (WT). In some embodiments, the anti-glycosylated BTLA antibodies provided herein can immunospecifically bind to one or more BTLA double mutants that retain only a single glycosylation site at BTLA N75, N94 or N110. In some embodiments, the anti-glycosylated BTLA antibodies provided herein show only background binding, if any, to a BTLA triple mutant, that retains none of BTLA's N75, N94, or N110 0-glycosylation sites.