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 […]
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 […]
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 […]
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 […]
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 […]
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 […]
cH IgG1 / κλ body involves the formation of in vitro display libraries with common heavy chains against two different antigens. κλ body share the same heavy chain but carry either κ or λ light chains. Three different chains (one heavy and two light) are then co-expressed in a single cell to generate a mixture containing two […]
Hetero H, forced HL IgG1/ DuetMab replaces the native disulfide bond in the CH1-CL interface with an engineered disulfide bond (fig. 1). This enhances cognate light chain pairing. Three different positions in the CH1-CL interface are possible candidates for favoring the formation of a novel disulfide bond. An amino acid on the HC and one […]
