Biogen Idec Ma Inc.

Biogen, Incorporated

Biogen Ma Inc.

Ab Biosciences, Inc.

Ucb Biopharma Sprl

Genentech, Inc.

Ucb Pharma, S.a.

Yen-Ming Hsu

Susan L Kalled

Lihe Su

Christine Ambrose

Jeffrey Thompson

Dingyi Wen

Yaping Sun

Ralph Adams

Kerry Louise Tyson

Ellen A Garber

Andrew George Popplewell

Linda C Burkly

Frederick Robbins Taylor

Martyn Kim Robinson

Derek Thomas Brown

Jeng-Shin Lee

Hsiu-Ching Chang

Janine L Ferrant-Orgettas

Anthony Shock

Huw M Nash

Gerald Wayne Shipps, Jr

Tatiana Novobrantseva

David R Thomas

Yusheng Liao

Lihong Sun

Leonid Gorelik

Zhongli Zheng

Satish Jindal

Flavius Martin

Susan Mrose

George R Lenz

Joanne Quan

Mary-Beth Carter

Leonid Kirkovsky

Compositions of recombinant intravenous immunoglobulin (rIVIG) proteins and methods for purification and use of rIVIG proteins. The compositions comprise oligomeric Fc molecules which bind to Fc receptors with high avidity. The rIVIG proteins are useful as immunomodulatory molecules for the treatment of immune disorders including autoimmune diseases, such as refractory immune thrombocytopenia, chronic inflammatory demyelinating polyneuropathy, multiple sclerosis, lupus, Graves Disease, Kawasaki disease, dermatomyositis, myasthenia gravis, Guillain-Barre syndrome, autoimmune hemolytic anemia, and other immune and inflammatory conditions. The rIVIG proteins can also be used as immunomodulators in patients to reduce the immune rejection of organ transplants, stem cell transplants and bone marrow transplantation. Additionally, the present invention provides rIVIG proteins of non-human origin, for use in veterinary immune disorders, such as canine rIVIG proteins for the treatment of dogs suffering from autoimmune hemolytic anemia, immune thrombocytopenia purpura, rheumatoid arthritis, or other canine immune disorder.

Recombinant intravenous immunoglobulin (RIVIG) compositions and methods for their production and use

Recombinant intravenous immunoglobulin (rIVIG) compositions and methods for their production and use

This invention provides antibodies that recognize the B Cell Maturation Antigen (BCMA) and that bind na&#xef;ve B cells, plasma cells, and/or memory B cells. The invention further provides methods for depleting na&#xef;ve B cells, plasma cells, and memory B cells, and for treating B cell-related disorders, including lymphomas and autoimmune diseases.

Anti-BCMA antibodies

The present invention provides novel, rationally designed human control antibodies for use in various in vivo and in vitro applications. The antibodies of the present invention have well characterized variable domains that have been designed to minimize or eliminate antigen binding without altering gross antibody structure. Using the antibodies of the present invention in various assays allows researchers to distinguish effects that result from specific antigen-antibody interactions from other, non-specific antibody effects.

Human control antibodies and uses therefor

This invention provides binding proteins, including antibodies, antibody derivatives and antibody fragments, that specifically bind a CD154 (CD40L) protein. This invention also provides a chimeric, humanized or fully human antibody, antibody derivative or antibody fragment that specifically binds to an epitope to which a humanized Fab fragment comprising a variable heavy chain sequence according to SEQ ID NO: 1 and comprising a variable light chain sequence according to SEQ ID NO: 2 specifically binds. CD154 binding proteins of this invention may elicit reduced effector function relative to a second anti-CD154 antibody. CD154 binding proteins of this invention are useful in diagnostic and therapeutic methods, such as in the treatment and prevention of diseases including those that involve undesirable immune responses that are mediated by CD154-CD40 interactions.

Binding proteins, including antibodies, antibody derivatives and antibody fragments, that specifically bind CD154 and uses thereof

The present invention provides methods of determining platelet aggregation, methods of determining susceptibility to clotting upon administration of a CD40L-binding moiety, and kits related thereto.

CD40L-binding agent based platelet aggregation assays

The present disclosure provides compositions and methods relating to the evaluation of BAFF in a biological sample from a subject.

Methods of evaluating BAFF

The disclosure provides a non-naturally occurring BAFF-R glycoprotein having a deletion in the extracellular domain which results in an altered O-linked glycosylation pattern. The disclosure also provides methods and pharmaceutical compositions for treating B-cell- and T-cell-mediated disorders.

Method of treating B cell cancers by administering truncated BAFF receptors

BAFF plays a central role in acquired immunity. The disclosure identifies BAFF-responsive genes that are substantially upregulated by administration of BAFF and substantially downregulated by treatment with a BAFF antagonist. Specific genes are: NF-&#x3ba;B2, CD23, H2-M&#x3b2; (the beta chain of H2-DM), Fig-1, and OBF-1. The disclosure provides methods and compositions for: monitoring the activity of a BAFF antagonist in a mammal; monitoring BAFF activity in a mammal; identifying a mammal to be treated with a BAFF antagonist; and related uses. Such methods include detecting one or more molecules selected from the group consisting of Fig-1 molecule, OBF-1 molecule, and H2-M&#x3b2; molecule in a biological sample of the mammal, and optionally further detecting NF-&#x3ba;B2 molecule and/or CD23 molecule in the biological sample.

Methods for use with BAFF antagonists

Platelet aggregation assays using a CD40L-binding agent

The disclosure provides a non-naturally occurring BAFF-R glycoprotein having a deletion in the extracellular domain which results in an altered 0-linked glycosylation pattern. The disclosure also provides methods and pharmaceutical compositions for treating B-cell- and T-cell-mediated disorders.

Method of treating immunological disorders by administering truncated BAFF receptors

Growing community of inventors

Lexington, MA, United States of America

Yen-Ming Hsu