The application provides a multi-specific antibody-like protein having a N-terminal and a C-terminal, comprising in tandem from the N-terminal to the C-terminal, a first binding domain (D1) at the N-terminal, a second binding domain (D2) comprising a light chain moiety, a Fc region, a third binding domain (D3), and a fourth binding domain (D4) at the C-terminal, wherein the light chain moiety comprises a fifth binding domain (D5) covalently attached to the C-terminal, a sixth binding domain (D6) covalently attached to the N-terminal, or both, and wherein the D1, D2, D3, D4, D5 and D6 each has a binding specificity against a tumor antigen, an immune signaling antigen, or a combination thereof.

Provided are an anti-RS virus antibody with high sensitivity and a test reagent using the antibody.

An anti-RS virus N protein monoclonal antibody, comprising a heavy chain variable region consisting of the amino acid sequence as set forth in SEQ ID NO: 1, and a light chain variable region consisting of the amino acid sequence as set forth in SEQ ID NO: 2, 3 or 4, or an antigen-binding fragment thereof.

High-affinity antibodies recognizing CD3 and B Cell Maturation Factor protein (BCMA) are disclosed. Binding sites from humanized anti-CD3 and anti-BCMA antibodies are incorporated into a Fabs-in-Tandem Immunoglobulin format without significant loss of binding affinity, and the resultant bispecific, multivalent binding proteins are able to bind to both CD3 and BCMA simultaneously. Such antibodies, antigen-binding portions thereof, and bispecific FIT-Ig binding proteins are useful for treating cancer.

The present invention relates to a chromatography ligand, which comprises Domain C from Staphylococcus protein A (SpA), or a functional fragment or variant thereof. The chromatography ligand presents an advantageous capability of withstanding harsh cleaning in place (CIF) conditions, and is capable of binding Fab fragments of antibodies. The ligand may be provided with a terminal coupling group, such as arginine or cysteine, to facilitate its coupling to an insoluble carrier such as beads or a membrane. The invention also relates process of using the ligand in isolation of antibodies, and to a purification protocol which may include washing steps and/or regeneration with alkali.

The present invention relates in part to amino acid sequences that are directed against and/or that can specifically bind to an envelope protein of a virus, as well as to compounds or constructs, and in particular proteins and polypeptides, that comprise or essentially consist of one or more such amino acid sequences.

The present invention relates to novel antibodies and fragments thereof that binds cannabinoid 1 (CB1) receptor. The antibodies and fragments thereof as disclosed herein include humanized antibodies that bind CB1 receptor. The invention also includes uses of the antibodies for treating a disease or disorder responsive to antagonism or agonism of the CB1 receptor.

The disclosure provides methods and compositions that are useful to lessen and/or cure bacterial biofilms and treat diseases or disorders associated with biofilms using one or more novel polypeptide vaccines, antibodies, antibody fragments and compositions. Bacteria that cannot form functional biofilms are more readily cleared by the remainder of the host's immune system and/or traditional antibiotics.

This invention relates to anti-ROR1 antibodies and methods of using them in treating diseases and conditions related to ROR1 activity, e.g., cancer.

The present invention relates to an in vitro method for production of heterodimeric proteins.

The present invention relates to bispecific antibodies comprising a modified C-terminal crossfab fragment that have reduced or no reactivity against preexisting antidrug antibodies.