Delivering novel impact

We challenge the status quo because we know what’s at stake.

We have the potential to defy impossible by targeting rare, immune-mediated disease areas with significant unmet need in which the current standard of care falls short.

In doing so, we have the potential to change the future for the patients who inspire us.

Novel Drug Candidates

Product Candidate Indication Preclinical Phase 1 Phase 2
Phase 3
Nipocalimab (M281)
(Anti-FcRn antibody)
Warm Autoimmune
Hemolytic Anemia (wAIHA)
Hemolytic Disease of Fetus
and Newborn (HDFN)
Myasthenia Gravis (MG)
(Hypersialylated IgG)
Immune Thrombocytopenic
Purpura (ITP)
Chronic Inflammatory Demyelinating Polyneuropathy (CIDP)
(Recombinant Fc multimer)
CD38 SIFbody
Novel Drug Candidates

* In collaboration with CSL


Product Candidate Preclinical Phase 1 Phase 2
Phase 3
Proposed Biosimilar to Aflibercept

* In collaboration with Mylan

Nipocalimab (M281)

The presence of pathogenic antibodies which facilitate tissue damage and organ dysfunction is a hallmark of immune-mediated diseases. In clinical settings, therapeutic plasmapheresis and immunoabsorption are often used to remove autoantibodies and other blood components contributing to disease. The clinical benefit of these procedures suggest that the removal of autoantibodies may lead to improvement of symptoms in some autoimmune indications. Removal of autoantibodies may be addressable by targeting FcRn, the neonatal Fc receptor which recycles immunoglobulin G (IgG) into circulation maintaining the long half-life of IgG.

Using proprietary antibody engineering technology, we have developed a fully human IgG1 monoclonal antibody that targets the IgG-binding site of FcRn, called nipocalimab (M281). Blocking FcRn reduces circulating pathogenic IgG through inhibition of IgG recycling and inhibits the transport of pathogenic IgG across the placenta in pregnancy.

M254, Hyper-sialylated IVIgG (hsIVIgG)

Intravenous immunoglobulin (IVIg) is a therapeutic blood product prepared from the pooled plasma of 3,000 to 60,000 healthy donors per batch. IVIg has been used for more than 30 years for the treatment of a variety of acute and chronic autoimmune and systemic inflammatory diseases. The global market for IVIg exceeds $8 billion, with the majority of products currently approved being for use in treatment of autoimmune disease.

Despite the beneficial therapeutic effects of IVIg in inflammatory diseases, consistent therapeutic efficacy and the challenges of administration remain major limitations for patients and physicians using IVIg. These challenges have stimulated our desire to generate therapeutic alternatives that could leverage the broad mechanisms of action of IVIg while improving therapeutic consistency and potency.

The identification of the important anti-inflammatory role of Fc-sialylation has presented us an opportunity to create more potent immunoglobulin therapies. Using proprietary sialylation technology, a method to add sialic acid to protein, we have developed hsIgG, a robust, controlled sialylation process to generate tetra-Fc-sialylated immunoglobulins with consistent enhanced anti-inflammatory activity.


Antigen-autoantibody immune complexes (ICs) are a common pathogenic hallmark of many autoimmune diseases. The multiple Fc domains of ICs aggregate Fcγ receptors (FcγRs), triggering cellular activation processes that play critical roles in inflammation and tissue damage. The rational engineering of therapeutics that broadly antagonize FcγRs has been hampered by a limited understanding of the molecular determinants directing FcγR activation.

Through the engineering and characterization of Fc structures, we were able to derive novel insights into FcγR modulation and have generated a unique recombinant trivalent human IgG1 Fc multimer, referred to as M230, with optimal physiochemical and biological properties. M230 is being developed in collaboration with CSL.