Format of bispecific antibodies (BsAbs)-C-terminal linker of Fc
Virus-like particles (VLP) Platforms for immunogens, vaccines and drug carriers
Antibody-drug Conjugate (ADC): Pre-made ADC benchmark, MOA, Production and QC
Neutralizing antibodies of virus (SARS2, HIV, HBV, Rabies, RSV, Ebola, Influenza)
Immunoglobulin Fc receptors for Fc&Fc Receptor binding assay
ILIBRA-HuEasy Monoclonal antibody (mab) humanization service (fully humanized ab)
Single domain antibody (Nanobody)
SOCAIL MEDIA
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 are composed of two different polypeptides that form a dimer through modifying specific sequences in the Fc region of each polypeptide. Each end of the polypeptide may contain one or two different binding domains, enabling the ADAPTIR-FLEX molecules to bind up to four targets. In addition, the ADAPTIR-FLEX platform can be used to modify the valency of binding to each target, which means it can bind a target, through one binding domain or through multiple binding domains, to a specific target to enable modifying the strength of binding to a specific target.
Formats of bispecific antibodies (BsAbs)
Many formats have been developed for BsAb generation as listed in the following table.
| Format | Schematic structure | Description | Example BsAb | Trademark | Company |
|---|---|---|---|---|---|
| tandem VHH | Tandem VHH fragment-based BsAb | N/A | |||
| tandem scFv |  | Tandem ScFv fragment-based BsAb | AMG330 | BiTETM | Amgen |
| Dual-affinity re-targeting antibody |  | Tandem domain-exchanged Fv (can also be used to fuse with Fc domain to create whole Abs) | Flotetuzumab | DARTTM | Macrogenics |
| Diabody |  | dimer of single-chain Fv (scFv) fragment | vixtimotamab | ReSTORETM | Amphivena Therapeutics |
| (scFv)2-Fab |  | a Fab domain and two scFv domains bind | A-337 | ITabTM | Generon/EVIVE Biotech |
| Rat–mouse hybrid IgG |  | Full-size IgG-like half antibodies from two different species | Catumaxomab | TriomabTM | Trion Pharma |
| Hetero heavy chain, Common light chain |  | Hetero heavy chain, Common light chain | Emicizumab | ART-IgTM | Genentech/ Chugai/Roche |
| Controlled Fab arm exchange |  | Recombin the parental half antibodies | JNJ-64007957 | DuobodyTM | Genmab/ Janssen |
| Hetero H, forced HL IgG1 |  | KIH technology for heterodimerization of 2 distinct H chains, replacing the native disulfide bond in one of the CH1-CL interfaces with an engineered disulfide bond to enhance the cognate of H and L paring | MEDI5752 | DuetMabTM | MedImmune/ AstraZeneca |
| cH IgG1 |  | Identical heavy chains; 2 different light chains: one kappa (κ) and one lambda (λ) | NI-1701 | κλ bodyTM | Novimmune SA |
| Hetero H, CrossMab |  | KIH technology; domain crossover of immunoglobulin domains in the Fab region | Vanucizumab | CrossMabTM | Roche |
| scFv-Fab IgG |  | Fab-Fc; ScFv-Fc | Vibecotamab; M802 | XmabTM (the engineered Fc to enhance the generation of heterodimeric Fc); YBODYTM | Xencor/Amgen; YZYBio |
| VH1-VH2-CH1-Fc1(G1) x VL2-VL1-CL-Fc2(G1) |  | 2 binding motif in one half antibody | SAR440234 | CODV-IgTM | Sanofi |
| VL1-CL1-VH2-CH2-Fc x VH1-CH1 x VL2-CL2 |  | 2 binding motif in one half antibody | EMB-01 | FIT-IgTM | EPIMAB BIOTHERAPEUTICS |
| VH-1-TCR Cα x VL-1-TCR Cβ; VH-2-CH-2-Fc x VL-2-CL-2 |  | KIH technology; TCR Cα/Cβ is used to substitute the CH1 and CL domain in one arm | WuXibodyTM | WuXi Biologics | |
| C-terminal linker of Fc |  | Link the other molecules at the C-terminal of Fc | APVO442 | ADAPTIR-FLEXTM | Aptevo Therapeutics |
| Fc antigen binding site |  | 2 natural binding sites; 2 additional binding sites in the Fc loop | FS118 | mAb2 | F-star Therapeutics |
