Abstract: Compositions of purified biologically active Wnt proteins are provided. Wnt proteins are found to be hydrophobic and post-translationally modified by addition of a lipid moiety at a conserved cysteine residue. Methods for isolation of Wnt utilize detergents that maintain the solubility of the modified protein.

Abstract: Compositions of purified biologically active Wnt proteins are provided. Wnt proteins are found to be hydrophobic and post-translationally modified by addition of a lipid moiety at a conserved cysteine residue. Methods for isolation of Wnt utilize detergents that maintain the solubility of the modified protein.

Abstract: Compositions of purified biologically active Wnt proteins are provided. Wnt proteins are found to be hydrophobic and post-translationally modified by addition of a lipid moiety at a conserved cysteine residue. Methods for isolation of Wnt utilize detergents that maintain the solubility of the modified protein.

Abstract: Compositions of purified biologically active Wnt proteins are provided. Wnt proteins are found to be hydrophobic and post-translationally modified by addition of a lipid moiety at a conserved cysteine residue. Methods for isolation of Wnt utilize detergents that maintain the solubility of the modified protein.

Abstract: Compositions of purified biologically active Wnt proteins are provided. Wnt proteins are found to be hydrophobic and post-translationally modified by addition of a lipid moiety at a conserved cysteine residue. Methods for isolation of Wnt utilize detergents that maintain the solubility of the modified protein.

Abstract: Compositions of purified biologically active Wnt proteins are provided. Wnt proteins are found to be hydrophobic and post-translationally modified by addition of a lipid moiety at a conserved cysteine residue. Methods for isolation of Wnt utilize detergents that maintain the solubility of the modified protein.

Abstract: Compositions of purified biologically active Wnt proteins are provided. Wnt proteins are found to be hydrophobic and post-translationally modified by addition of a lipid moiety at a conserved cysteine residue. Methods for isolation of Wnt utilize detergents that maintain the solubility of the modified protein.

Abstract: ROR2 is provided as a therapeutic target and prognostic marker for cancers, which include without limitation specific carcinomas and sarcomas. This invention also provides for the use of conjugates comprising an antibody that recognizes and binds ROR2, and a cytotoxic agent. In the cytotoxic conjugates, the cell binding agent has a high affinity for ROR2 and the cytotoxic agent has a high degree of cytotoxicity for cells expressing ROR2, such that the cytotoxic conjugates of the present invention form effective killing agents. In a preferred embodiment, the cell binding agent is an anti-ROR2 antibody or an epitope-binding fragment thereof, more preferably a humanized anti-ROR2 antibody or an epitope-binding fragment thereof, wherein a cytotoxic agent is covalently attached, directly or via a cleavable or non-cleavable linker, to the antibody or epitope-binding fragment thereof.

Abstract: Compositions of purified biologically active Wnt proteins are provided. Wnt proteins are found to be hydrophobic and post-translationally modified by addition of a lipid moiety at a conserved cysteine residue. Methods for isolation of Wnt utilize detergents that maintain the solubility of the modified protein.

Abstract: Methods are provided for contacting a target cell with a biologically active Wnt polypeptide that is coupled to a magnetic particle, for producing biologically active bead-coupled Wnt stimulator and Wnt inhibitor polypeptides, and for enriching a target cell population for Wnt responsive or DKK responsive cells. Compositions and kits for practicing the methods of the invention are also included, and generally include a biologically active Wnt stimulator polypeptide that is coupled to a magnetic particle. Compositions and kits may also include (i) a buffer that is substantially free of detergent, and/or (ii) a biologically active bead-coupled DKK polypeptide.

Abstract: Compositions of purified biologically active Wnt proteins are provided. Wnt proteins are found to be hydrophobic and post-translationally modified by addition of a lipid moiety at a conserved cysteine residue. Methods for isolation of Wnt utilize detergents that maintain the solubility of the modified protein.

Abstract: Composition and methods are provided for the prospective enrichment of human cardiovascular progenitor cells, which can be differentiated into cardiomyocytes, from in vitro cultures of stem cells. The stem cells are cultured in conditions permissive for differentiation into cardiovascular progenitor cells, and cardiovascular progenitor cells are sorted for expression of one or more of the markers ROR2, CD13, KDR and PDGF?R, where the progenitor cells positively express these markers. Highly enriched populations of cardiomyocyte lineage cells can be obtained.

Abstract: Compositions of purified biologically active Wnt proteins are provided. Wnt proteins are found to be hydrophobic and post-translationally modified by addition of a lipid moiety at a conserved cysteine residue. Methods for isolation of Wnt utilize detergents that maintain the solubility of the modified protein.

Abstract: Methods and compositions are provided for the therapeutic use of Wnt proteins, where the Wnt protein is inserted in the non-aqueous phase of a lipid structure. In some embodiments the Wnt protein is presented in its active conformation on an outer liposome membrane or micelle. Pharmaceutical compositions of the present invention can be administered to an animal for therapeutic purposes. In some embodiments of the invention, the compositions are administered locally, e.g. by injection at the site of an injury. For certain conditions it is desirable to provide Wnt activity for short periods of time, and an effective dose will be administered over a defined, short period of time.

Abstract: Mammalian neural progenitor or stem cells are expanded in vitro by culture in the presence of one or more wnt polypeptides. The expanded cells substantially maintain their original phenotype including the ability to give rise to multiple types of differentiated cells.

Abstract: Compositions of purified biologically active Wnt proteins are provided. Wnt proteins are found to be hydrophobic and post-translationally modified by addition of a lipid moiety at a conserved cysteine residue. Methods for isolation of Wnt utilize detergents that maintain the solubility of the modified protein.

Abstract: Wnt receptor compositions and methods of use are disclosed. In particular, methods using Wnt receptors, such as Dfz2, in screens for compounds which modulate the binding of a Wnt polypeptide to a Wnt receptor.

Abstract: Compositions of purified biologically active Wnt proteins are provided. Wnt proteins are found to be hydrophobic and post-translationally modified by addition of a lipid moiety at a conserved cysteine residue. Methods for isolation of Wnt utilize detergents that maintain the solubility of the modified protein.

Abstract: Compositions of purified biologically active Wnt proteins are provided. Wnt proteins are found to be hydrophobic and post-translationally modified by addition of a lipid moiety at a conserved cysteine residue. Methods for isolation of Wnt utilize detergents that maintain the solubility of the modified protein.

Abstract: Compositions of purified biologically active Wnt proteins are provided. Wnt proteins are found to be hydrophobic and post-translationally modified by addition of a lipid moiety at a conserved cysteine residue. Methods for isolation of Wnt utilize detergents that maintain the solubility of the modified protein.