Merrimack Pharmaceuticals, Inc.

National Research Council of Canada

Dyax Corporation

Syntonix Pharmaceuticals, Inc.

Biogen Hemophilia Inc.

Bioverativ Therapeutics Inc.

Arumugam Muruganandam

Michael Feldhaus

Ulrik Bjerl Nielsen

Birgit Schoeberl

David Buckler

Robert Charles Ladner

Aaron Sato

Alan J Bitonti

Clive R Wood

Kevin McDonnell

Jennifer A Dumont

Danica Stanimirovic

Christopher TenHoor

Saran A Narang

Liming Liu

Malini Viswanathan

Jamshid Tanha

James Stattel

James McGivney

Jasmid Tanha

Kevin Mcdonnell

Clive Wood

The present invention provides a novel class of antibodies and antigen binding fragments thereof that bind the extracellular domain of ErbB3 receptor and inhibit various ErbB3 functions. For example, the antibodies and antigen binding fragments described herein are capable of binding to the receptor designated ErbB3 and inhibiting EGF-like ligand mediated phosphorylation of the receptor. Such antibodies and antigen binding fragments thereof have the useful characteristic of inhibiting the proliferation of cancer cells expressing ErbB3.

Antibodies against the ectodomain of ERBB3 and uses thereof

This disclosure provides, inter alia, proteins that bind to FcRn, e.g., immunoglobulins that inhibit FcRn with high affinity and selectivity. The FcRn-binding proteins can be used to treat a variety of disorders including autoimmune disorders.

Antibodies to FeRn and uses thereof

The present invention provides a novel class of monoclonal antibodies which bind ErbB3 receptor and inhibits various ErbB3 functions. For example, the antibodies described herein are capable of binding to ErbB3 and inhibiting EGF-like ligand mediated phosphorylation of the receptor.

Antibodies against ERBB3 and uses thereof

Fc receptor binding proteins

A phage-displayed library of llama single heavy domain antibodies (sdAbs) was enriched for species that selectively bind to and are internalized by human cerebromicrovascular endothelial cells (HCEC). From the enriched library, two sdAbs were selected, sequenced, subcloned, and expressed as fusion proteins with c-myc-Histags (Hisis SEQ ID NO:101). Similarly as phage-displayed sdAbs, these soluble tagged sdAbs were shown to selectively bind to HCEC and to transmigrate across in vitro human blood-brain barrier (BBB) model. In contrast to an unrelated llama sdAb, these sdAbs were also detected in the brain after i.v. injection into mice. These small (&#x2dc;13 kDa) antibody fragments have essential characteristics of brain-specific delivery vectors and can be used to facilitate drug transport across the BBB.

Single domain brain-targeting antibody fragments derived from llama antibodies

Antibodies against the ectodomain of ErbB3 and uses thereof

A phage-displayed library of llama single heavy domain antibodies (sdAbs) was enriched for species that selectively bind to and are internalized by human cerebromicrovascular endothelial cells (HCEC). From the enriched library, two sdAbs were selected, sequenced, subcloned, and expressed as fusion proteins with c-myc-Histags. Similarly as phage-displayed sdAbs, these soluble tagged sdAbs were shown to selectively bind to HCEC and to transmigrate across in vitro human blood-brain barrier (BBB) model. In contrast to an unrelated llama sdAb, these sdAbs were also detected in the brain after i.v. injection into mice. These small (&#x2dc;13 kDa) antibody fragments have essential characteristics of brain-specific delivery vectors and can be used to facilitate drug transport across the BBB.

Single-domain brain-targeting antibody fragments derived from llama antibodies

The present invention provides a novel class of monoclonal antibodies which bind ErbB3 receptor and inhibits various ErbB3 functions. In a particular embodiment, the antibodies are capable of binding to ErbB3 and inhibiting ligand mediated phosphorylation of the receptor.

Antibodies against ErbB3 and uses thereof

Growing community of inventors

Bengaluru, India

Arumugam Muruganandam