Category Archives: Biologics

Format of bispecific antibodies (BsAbs)-Hetero heavy chain, Common light chain

Since an IgG antibody has two antigen-binding fragments (Fab) both of which link to an Fc region, there had long been a concept of an asymmetric bispecific IgG antibody capable of binding to two different antigens or epitopes. The asymmetric reengineering technology immunoglobulin (ART-Ig) is a humanized asymmetric bispecific IgG antibody. An asymmetric bispecific IgG […]

Format of bispecific antibodies (BsAbs)-Rat-mouse hybrid IgG

Rat-mouse hybrid IgG is a monoclonal antibody with binding sites for two different antigens, typically CD3 and a tumor antigen, making it a type of bispecific monoclonal antibody. In addition, its intact Fc-part can bind to an fc receptor on accessory cells like conventional monospecific antibodies. The net effect is that this type of drug […]

Format of bispecific antibodies (BsAbs)-(scFv)2-Fab

Tribodies are multifunctional recombinant antibody derivatives. The Fab fragment serves as a specific heterodimerization signal, and the two scFv fragments are each fused to a different Fab chain. In this way we obtain a molecule of intermediate molecular weight (100 kDa) which allows incorporating three different antibody fragments (Fig. 1). This manifold, tribody, can be […]

Format of bispecific antibodies (BsAbs)-Diabody

Diabody is a noncovalent dimer of single-chain Fv (scFv) fragment that consists of the heavy chain variable (VH) and light chain variable (VL) regions connected by a small peptide linker. Another form of diabody is single-chain (Fv)2 in which two scFv fragments are covalently linked to each other. bispecific bivalent dimers are produced by using two […]

Format of bispecific antibodies (BsAbs)-Dual-affinity re-targeting antibody

Dual-affinity re-targeting proteins (DARTs) encompasses of two Fv fragments, containing two single antigen-binding sites formed when two Fv fragments heterodimerize. The Fv1 contains of a VH from antibody A and a VL from antibody B, whereas Fv2 contains VH from antibody B and VL from antibody A in the order of VL (1)-VH (2) and […]

Format of bispecific antibodies (BsAbs)-Tandem scFv

A tandem scFv links two or more scFvs with the helical peptide linkers in the orientation NH2–VL1–VH1–(linker–VL2–VH2)n–COOH, resulting in a single chain bivalent and bi-specific molecule encoded by a single gene (Figure 2). Tandem scFv can be used to target two different antigens on two different cells, two different antigens on the same cell, or […]

Format of bispecific antibodies (BsAbs)-Fc antigen binding site

The production of bispecific antibodies involves the addition of a second antigen-binding site in the Fab arms. Sometimes, these types of bispecific products have problems such as poor stability, immunogenicity and challenges in the manufacturing process. Hence, Mab2 simply replaces the Fc region of an existing antibody with an Fcab that binds to a second […]

Format of bispecific antibodies (BsAbs)-C-terminal linker of Fc

ADAPTIR-FLEX platform technologies can be used to produce monospecific, bispecific, and multispecific immunotherapeutic proteins. These protein candidates bind to one or more targets found on tumor cells, immune cells, or other cells in the body or circulation to either amplify, suppress, or regulate the body’s defense mechanisms to treat cancer and autoimmune diseases. ADAPTIR-FLEX molecules […]

Format of bispecific antibodies (BsAbs)-VH-1-TCR C¦Á x VL-1-TCR C¦Â; VH-2-CH-2-Fc x VL-2-CL-2

WuXiBody, replace one parental mAb’s CH1/CL region by the T cell receptor (TCR) constant domain. WuXiBody’s design ensures cognate HC-LC pairing, the same goal as that being aimed by the CrossMab technology. BsAbs based on WuXiBody can adopt either asymmetric or symmetric format (Fig. 1). For asymmetric WuXiBody-based bsAbs, heterodimerization is promoted by the KiH […]

Format of bispecific antibodies (BsAbs)-VL1-CL1-VH2-CH2-Fc x VH1-CH1 x VL2-CL2

Tetravalent Fabs-In-Tandem immunoglobulins (FIT-Ig™) technology combines Fab fragments of any 2 parental mAbs create a tetravalent, dual-targeting single molecular entity, where the FabA is structurally fused to FabB in tandem at its N-terminus (Fig. 1a). A unique crisscross orientation of 2 sets of VH-CH1 and VL-CL evades any mispairing problem between two short chains and long chain. FIT-Ig have […]