Abstract: The translation product of the growth arrest-specific gene 6 (gas6) has been identified as an activator of the Mer receptor protein tyrosine kinase. The invention accordingly provides methods of activating Mer receptor in cells expressing it by exposing them to exogenous gas6 polypeptides. Also provided are methods of enhancing the growth, differentiation, or survival of such cells using gas6 polypeptides.

Abstract: The invention concerns novel members of the endocytic type C lectin family and methods and means for producing them. The native polypeptides of the invention are characterized by containing a signal sequence, a cysteine rich domain, a fibronectin type II domain, 8 type C lectin domains, a transmembrane domain and a cytoplasmic domain. Nucleotide sequences encoding such polypeptides, vectors containing the nucleotide sequences, recombinant host cells transformed with the vectors, and methods for the recombinant production for the novel type C lectins are also within the scope of the invention.

Abstract: This invention concerns new PSTPIP polypeptides which are bound by and dephosphorylated by the PEST family of protein tyrosine phosphatases. The invention specifically concerns native murine PSTPIP polypeptides and their homologues in other mammals, and their functional derivatives. The invention further relates to nucleic acids encoding these proteins, vectors containing and capable of expressing such nucleic acid, and recombinant host cells transformed with such nucleic acid. Methods for inducing the polymerization of actin monomers in eukaryotic cells and assays for identifying antagonists and agonists of the PSTPIP polypeptides of the present invention are also provided.

Abstract: The present invention concerns isolated nucleic acid molecules encoding the novel TIE ligands NL1, NL5, NL8, and NL4, the proteins encoded by such nucleic acid molecules, as well as methods and means for making and using such nucleic acid and protein molecules.

Abstract: This invention concerns new PSTPIP polypeptides which are bound by and dephosphorylated by the PEST family of protein tyrosine phosphatases. The invention specifically concerns native murine PSTPIP polypeptides and their homologues in other mammals, and their functional derivatives. The invention further relates to nucleic acids encoding these proteins, vectors containing and capable of expressing such nucleic acid, and recombinant host cells transformed with such nucleic acid. Methods for inducing the polymerization of actin monomers in eukaryotic cells and assays for identifying antagonists and agonists of the PSTPIP polypeptides of the present invention are also provided.

Abstract: The present invention concerns isolated nucleic acid molecules encoding the novel TIE ligands NL2, NL3 and FLS139, the proteins encoded by such nucleic acid molecules, as well as methods and means for making and using such nucleic acid and protein molecules.

Abstract: The present invention concerns isolated nucleic acid molecules encoding the novel TIE ligands NL1, NL5 and NL8, the proteins encoded by such nucleic acid molecules, as well as methods and means for making and using such nucleic acid and protein molecules.

Abstract: The invention provides purified ACT-4 receptor polypeptides, antibodies against these polypeptides and nucleic acids encoding ACT-4 receptor polypeptides. Also provided are methods of diagnosis and treatment using the same. ACT-4 receptors are preferentially expressed on the surface of activated CD4.sup.+ T-cells. ACT-4 receptors are usually expressed at low levels on the surface of activated CD8.sup.+ cells, and are usually substantially absent on resting T-cells, and on monocytes and B-cells (resting or activated). An exemplary ACT-4 receptor, termed ACT-4-h-1, has a signal sequence, an extracellular domain comprising three disulfide-bonded intrachain loops, a transmembrane domain, and an intracellular domain.

Abstract: Highly repetitive proteins which are relatively insoluble in water are chemically modified to increase solubility. The protein is reacted with a functionalizing agent to introduce additional polar functionalities and disrupt the order of the protein. The solubility of the protein in water is increased by the chemical modification, while adhesive and surfactant properties are retained.