Abstract: The invention describes amino acid residues of the Smad2 protein which are important for phosphorylation and activity, and Smad2 polypeptide fragments and biologically functional variants thereof. Included and dominant-negative variants of Smad2 and antibodies relating thereto. Also included are nucleic acids which encode such variants. Antibodies which selectively bind pathway-restricted Smad proteins phosphorylated at the C-terminal tail also are provided. Methods and products for using such nucleic acids and polypeptides also are provided.

Abstract: The invention describes amino acid residues of the Smad2 protein which are important for phosphorylation and activity, and Smad2 polypeptide fragments and biologically functional variants thereof. Included and dominant-negative variants of Smad2 and antibodies relating thereto. Also included are nucleic acids which encode such variants. Antibodies which selectively bind pathway-restricted Smad proteins phosphorylated at the C-terminal tail also are provided. Methods and products for using such nucleic acids and polypeptides also are provided.

Abstract: Platelet-derived endothelial cell growth factor (PD-ECGF) is a 45 kDa endothelial cell mitogen that has been purified to homogeneity from human platelets. It does not bind to heparin and does not stimulate the proliferation of fibroblasts, in contrast to other endothelial mitogens of the fibroblast growth factor (FGF) family. PD-ECGF appears to be the only endothelial cell growth factor in human platelets and recent data indicate that it has angiogenic activity in vitro, i.e., the ability to stimulate the formation of new blood vessels and chemotactic activity, in vitro. The present invention provides a homogeneous PD-ECGF in substantially greater yields than available in the past, the primary structure of PD-ECGF, antibodies against PD-ECGF, clones of its cDNA, and variants thereof. The invention also provides a therapeutic preparation of PD-ECGF.

Abstract: In accordance with this invention, an RPE cell membrane associated protein which has a molecular weight of about 32 kd, as determined by SDS-PAGE, has now been discovered. This protein, referred to an "p32," forms an oligomeric protein complex with the previously characterized p63 protein, a component of the membrane receptor for RBP. A nucleic acid molecule which codes for the p32 protein has also been isolated and sequence analysis shows that the p32 protein belongs to the family of short chain alcohol dehydrogenases, and exhibits 11-cis retinol dehydrogenase activity, the enzyme which catalyzes conversion of 11-cis-retinol into 11-cis retinaldehyde.

Abstract: The invention relates to a family of substantially pure, receptor like TGF-.beta.1 binding glycoproteins. These molecules are characterized by molecular masses of 160 kd, 70-80 kd, and 30-40 kd as determined by SDS-PAGE, and the ability to bind the TGF-.beta.1 molecule. This family of molecules is useful in identifying and/or quantifying TGF-.beta.1 in a sample, as well as inhibiting its effect on cells. Also described are nucleic acid sequences which code for the protein monomer making up the molecules.

Abstract: The invention relates to a family of substantially pure, receptor like TGF-.beta.1 binding glycoproteins. These molecules are characterized by molecular masses of 160 kd, 70-80 kd, and 30-40 kd as determined by SDS-PAGE, and the ability to bind the TGF-.beta.1 molecule. This family of molecules is useful in identifying and/or quantifying TGF-.beta.1 in a sample, as well as inhibiting its effect on cells. Also described are nucleic acid sequences which code for the protein monomer making up the molecules.

Abstract: The invention relates to a family of substantially pure, receptor like TGF-.beta.1 binding glycoproteins. These molecules are characterized by molecular masses of 160 kd, 70-80 kd, and 30-40 kd as determined by SDS-PAGE, and the ability to bind the TGF-.beta.1 molecule. This family of molecules is useful in identifying and/or quantifying TGF-.beta.1 in a sample, as well as inhibiting its effect on cells.

Abstract: Platelet-derived endothelial cell growth factor (PD-ECGF) is a 45 kDa endothelial cell mitogen that has been purified to homogeneity from human platelets. It does not bind to heparin and does not stimulate the proliferation of fibroblasts, in contrast to other endothelial mitogens of the fibroblast growth factor (FGF) family. PD-ECGF appears to be the only endothelial cell growth factor in human platelets and recent data indicate that it has angiogenic activity in vitro, i.e., the ability to stimulate the formation of new blood vessels and chemotactic activity, in vitro. The present invention provides a homogeneous PD-ECGF in substantially greater yields than available in the past, the primary structure of PD-ECGF, antibodies against PD-ECGF, clones of its cDNA, and variants thereof. The invention also provides a therapeutic preparation of PD-ECGF.

Abstract: Purified protein known as platelet TGF-.beta.1-BP (transforming growth factor-.beta.1-binding protein) is described. The protein is useful for purposes such as the production of antisera which are useful in identifying complexes containing the binding protein, as well as in formation of labeled probes. Also described are purified DNA which expresses the protein, as well as messenger RNA translated into the protein. The protein contains 16 epidermal growth factors (EGF) like repeats, and 3 repeats not found in other proteins. The DNA for the protein is found to contain consensus sequences for hydroxylation of asparagine/aspartic acid residues, and, in the purified protein beta hydroxylated asparagine residues were found.