Biogen, Incorporated

Biotransplant, Inc.

Biogen, N.v.

Margaret D Rosa

Barbara P Wallner

Roy R Lobb

Catherine A Hession

Christopher D Benjamin

Glenn T Miller

Susan E Goelz

Laurelee Osborn

Rodney L Monroy

Robert J Hawley

Bernice Z Schacter

Paul D Ronath

Joseph J Rosa

Linda C Burkly

Paul D Pomath

David W Thomas

Patricia L Chisholm

VCAM fusion proteins capable of binding to VLA4, and DNA molecules coding on these fusions.

VCAM fusion proteins and DNA coding therefor

VCAM1 polypeptides and VCAM11/ICAM fusion proteins are disclosed.

Vascular cell adhesion molecule (VCAM) polypeptides

Polypeptides and proteins comprising the CD2-binding domain of LFA-3 are disclosed. DNA sequences that code on expression for those polypeptides and proteins, methods of producing and using those polypeptides and proteins, and therapeutic and diagnostic compositions are also disclosed. Deletion mutants unable to bind CD2 and methods for their use are also disclosed. In addition, fusion proteins which comprise the CD2-binding domain of LFA-3 and a portion of a protein other than LFA-3, DNA sequences encoding those fusion proteins, methods for producing those fusion proteins, and uses of those fusion proteins are disclosed.

Method of using CD2-binding domain of lymphocyte function associated

CD2-binding domain of lymphocyte function associated antigen-3

Anti-CD4 antibody homologs, DNA sequences and recombinant DNA molecules encoding them, prophylactic, immunotherapeutic and diagnostic compositions comprising those antibody homologs, and methods for preventing or treating diseases in mammals, including humans, caused by infective agents whose primary targets are CD4.sup.+ lymphocytes. Such diseases include acquired immune deficiency syndrome ('AIDS'), AIDS related complex, and human immunodeficiency virus infection.

Anti-CD4 antibody homologs useful in prophylaxis and treatment of AIDS,

A method of enhancing tolerance of a porcine transplant in a xenogeneic recipient by administering porcine bone marrow cells to the recipient and of enhancing proliferation and engraftment of the porcine bone marrow cells by exposing said cells to at least one substantially pure porcine cytokine and porcine cytokines that are substantially free of other porcine proteins and preferentially enhance the proliferation and engraftment of porcine bone marrow cells in the presence of bone marrow cells of other species. Protein and DNA sequence(s) for such porcine cytokines.

Porcine cytokines

Inducing xenograft tolerance and porcine cytokines therefor

Methods of inhibiting T-cell dependent proliferation of peripheral blood

Polynucleotides en coding porcine cytokines

CD2-binding domain of lymphocyte function associated antigen 3

DNA sequences encoding endothelial cell-leukocyte adhesion molecules ELAMs, methods for producing such molecules, and ELAMs (including the specific molecules ELAM1 and VLAM1 and 1b) essentially free of normally associated animal proteins are disclosed. DNA sequences encoding molecules involved in leukocyte adhesion (MILAs), methods for producing such molecules and MILAs (including the specific molecule, CDX) essentially free of normally associated animal proteins are also disclosed. Antibody preparations which are reactive for MILAs and also disclosed. Methods for identifying molecules which inhibit binding of leukocytes to endothelial cells, methods for inhibiting leukocyte binding to endothelial cells, and methods for detecting acute inflammation are disclosed.

Endothelial cell-leukocyte adhesion molecules (ELAMs) and molecules

DNA sequences encoding vascular cell adhesion molecules 1 and 1b ('VCAM1' and 'VCAM1B'), recombinant DNA molecules comprising those sequences, and unicellular hosts transformed with those recombinant DNA molecules.

DNA sequences encoding vascular cell adhesion molecules (VCAMS)

Modified human tissue plasminogen activators, the DNA sequences coding on expression for them and methods of making them in hosts transformed with those DNA sequences. The single chain form of these modified human t-PAs, t-PA (Lys 277.fwdarw.X), has a longer half life than the single chain form of native, or recombinant, t-PA, yet, in the two chain form these modified t-PAs have substantially the same affinity for fibrin and substantially the same activity as the two chain form of native, or recombinant, t-PA.

Modified tissue plasminogen activators

Growing community of inventors

Winchester, MA, United States of America

Margaret D Rosa