Category Archives: diagnostic article

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)-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 […]

Format of bispecific antibodies (BsAbs)-VH1-VH2-CH1-Fc1(G1) x VL2-VL1-CL-Fc2(G1)

CODV (cross-over dual variable domains) -Ig, contain four polypeptide chains that form two dual variable domains (four antigen binding sites) with a cross-over orientation (Figure 1), which is attained by inverting the alignment of the cognate domains on one chain. In order to adopt the correct VH/VL pairing, linker combinations were designed and optimized using […]

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

The XmAb enables alterations with desirable effects to the Fc domain of the antibodies. The modification increases affinity to the neonatal Fc receptor which prevents the antibody from degradation. Hence, this interaction extends the antibody’s halflife of this therapeutic drug. In order to construct the XmAb format an antibody heavy and light chain and a […]

Format of bispecific antibodies (BsAbs)-Hetero H, CrossMab

CrossMab technology enforces correct light chain association based on the domain crossover of immunoglobulin domains in the Fab region of the bispecific antibody. CrossMab technology allow the generation of various bispecific antibody formats, including bi- (1+1), tri- (2+1) and tetra-(2+2) valent bispecific antibodies, as well as non-Fc tandem antigen-binding fragment (Fab)-based antibodies. These formats may […]