Lawrence W. Mathews - Ann Arbor MI Kunihiro Tsuchida - San Diego CA
Assignee:
The Salk Institute for Biological Studies - LaJolla CA
International Classification:
G01N 3353
US Classification:
435 71, 435 6, 530351
Abstract:
In accordance with the present invention, there are provided novel receptor proteins characterized by having the following domains, reading from the N-terminal end of said protein: an extracellular, ligand-binding domain, a hydrophobic, trans-membrane domain, and an intracellular, receptor domain having serine kinase-like activity. The invention receptors optionally further comprise a second hydrophobic domain at the amino terminus thereof. The invention receptor proteins are further characterized by having sufficient binding affinity for at least one member of the activin/TGF- superfamily of polypeptide growth factors such that concentrations of 10 nM of said polypeptide growth factor occupy 50% of the binding sites of said receptor protein. A presently preferred member of the invention superfamily of receptors binds specifically to activins, in preference to inhibins, transforming growth factor-, and other non-activin-like proteins. DNA sequences encoding such receptors, assays employing same, as well as antibodies derived therefrom, are also disclosed.
Lawrence S. Mathews - Ann Arbor MI, US Kunihiro Tsuchida - San Diego CA, US
Assignee:
The Salk Institute for Biological Studies - La Jolla CA
International Classification:
C07K 16/18 A61K 39/395
US Classification:
5303871, 5303881, 4241301
Abstract:
In accordance with the present invention, there are provided novel receptor proteins characterized by having the following domains, reading from the N-terminal end of said protein:.
Cloning And Recombinant Production Of Crf Receptor(S)
In accordance with the present invention, there are provided novel receptor proteins characterized by having the following domains, reading from the N-terminal end of said protein: an extracellular, ligand-binding domain, a hydrophobic, trans-membrane domain, and an intracellular, receptor domain having serine kinase-like activity. The invention receptors optionally further comprise a second hydrophobic domain at the amino terminus thereof. The invention receptor proteins are further characterized by having sufficient binding affinity for at least one member of the activin/TGF-β superfamily of polypeptide growth factors such that concentrations of ≦10 nM of said polypeptide growth factor occupy ≦50% of the binding sites of said receptor protein. A presently preferred member of the invention superfamily of receptors binds specifically to activins, in preference to inhibins, transforming growth factor-β, and other non-activin-like proteins. DNA sequences encoding such receptors, assays employing same, as well as antibodies derived therefrom, are also disclosed.
Lawrence W. Mathews - Ann Arbor MI Wylie W. Vale - La Jolla CA Kunihiro Tsuchida - San Diego CA
Assignee:
The Salk Institute for Biological Studies - La Jolla CA
International Classification:
C07K 1471 C12N 1512
US Classification:
530350
Abstract:
In accordance with the present invention, there are provided novel receptor proteins characterized by having the following domains, reading from the N-terminal end of said protein: an extracellular, ligand-binding domain, a hydrophobic, trans-membrane domain, and an intracellular, receptor domain having serine kinase-like activity. The invention receptors optionally further comprise a second hydrophobic domain at the amino terminus thereof. The invention receptor proteins are further characterized by having sufficient binding affinity for at least one member of the activin/TGF-. beta. superfamily of polypeptide growth factors such that concentrations of. ltoreq. 10 nM of said polypeptide growth factor occupy. gtoreq. 50% of the binding sites of said receptor protein.
Amazon Jun 2008 - Dec 2008
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Glendale Elementary School District Jun 2008 - Dec 2008
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City of Detroit Law Department Oct 2001 - Aug 2006
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Education:
Michigan State University College of Law 1996
Jd, Michigan State University School of Law 1996
Bachelors, Bachelor of Business Administration