The present invention relates to CX3CR1-binding polypeptides, in particular polypeptides comprising specific immunoglobulin domains. The invention also relates to nucleic acids encoding such polypeptides; to methods for preparing such polypeptides; to host cells expressing or capable of expressing such polypeptides; to compositions comprising such polypeptides; and to uses of such polypeptides or such compositions, in particular for prophylactic, therapeutic and diagnostic purposes.

The invention relates to a method of reducing the amount of non-aggregate produce-related impurities (NAPRIs) in a buffered solution of monoclonal antibodies (mAbs), involving the use of a synthetic depth filter. The invention may be of use in the purification of monoclonal 5 antibodies.

Described herein are antibody constructs comprising a 41-1BB binding domain and an antigen-binding domain that binds to a tumor-associated antigen (TAA), wherein the 4-1BB-binding domain and the TAA antigen-binding domain are linked directly or indirectly to a scaffold. The scaffold may be an Fc construct with modifications that reduce its ability to mediate effector function.

Multivalent D-peptidic compounds that specifically bind to a target protein are provided. The multivalent D-peptidic compounds can include two or more distinct variant D-peptidic domains connected via linking components. The D-peptidic compounds can include multiple distinct domains that specifically bind to different binding sites on a target protein to provide for high affinity binding to, and potent activity against, the target protein. D-peptidic variant GA and Z domain polypeptides are also provided, which polypeptides have specificity-determining motifs (SDM) for specific binding to a target protein, such as VEGF-A or PD-1. In some embodiments where the target protein is homodimeric (e.g., VEGF-A, PD-1), the D-peptidic compounds may be similarly dimeric, and include a dimer of multivalent (e.g., bivalent) D-peptidic compounds. Methods for using the compounds are provided, including methods for treating a disease or condition associated with a target protein in a subject.

The invention describes anti-cancer therapies comprising using an LRP5 antagonist in combination with an anti-PD1 antibody, each as described herein.

This disclosure provides dimeric, pentameric, and hexameric Tumor Necrosis Factor (TNF) superfamily receptor protein binding molecules and methods of using such binding molecules to direct apoptosis-mediated killing of TNF receptor-expressing cells.

Provided are anti-TIGIT antibodies that bind to “T cell immunoreceptor with Ig and ITIM domains (TIGIT)”, including multispecific anti-TIGIT antibodies with binding specificity for TIGIT and one or more additional antigen, and methods of using the same. In certain embodiments, the anti-TIGIT antibodies comprises a single domain antibody that binds to TIGIT. In certain embodiments, the one or more additional antigen comprises Programmed cell death ligand 1 (PDL1).

The present invention relates to methods employing soluble multivalent activating agents for the selective in vitro and ex vivo activation and expansion γδ T-cell population(s), including specific γδ T-cell subpopulation(s) of interest and admixtures thereof, and methods for using the same for therapeutic purposes. Methods and compositions of the disclosure are useful in the treatment of various cancers, infectious diseases, and immune disorders.

Provided herein are novel anti-CD28×anti-B7H3 (also referred to as “αCD28×αB7H3”) heterodimeric bispecific antibodies and methods of using such antibodies for the treatment of cancers. Subject αCD28×αB7H3 antibodies are capable of agonistically binding to CD28 costimulatory molecules on T cells and targeting to B7H3 on tumor cells. Thus, such antibodies selectively enhance anti-tumor activity at tumor sites while minimizing peripheral toxicity. The subject antibodies provided herein are particularly useful for enhancing anti-tumor activity when used in combination with other anti-cancer therapies.

The current invention involves a series of fully recombinant multimerized forms of immunoglobulin Fc which thereby present polyvalent immunoglobulin Fc to immune cell receptors. The fusion proteins exist as both homodimeric and highly ordered multimeric fractions, termed stradomers. In comparison to the homodimeric fraction, purified multimeric stradomers have higher affinity and avidity for FcγRs with slower dissociation and are useful in the treatment and prevention of disease. The current invention demonstrates that directly linking IgG1 Fc regions to multimerization domains leads to enhanced multimerization and biological activity.