Abstract: This invention provides novel methods of and kits for labeling and isolating lumen-exposed molecules, particularly polypeptides which are expressed in a tissue-specific or organ-specific manner. The methods and kits can be used to isolate molecules exposed on the luminal side of cells lining vascular, ductal, sinus, respiratory, fascial, and other perfusible tissue spaces.

Abstract: The present invention provides novel methods and kits for labeling and isolating tissue-specific or organ-specific lumen-exposed molecules. In addition, the present invention provides tissue-specific or organ-specific lumen-exposed polypeptides, which were isolated by the methods herein. Furthermore the present invention provides therapeutic complexes comprising ligands that bind the tissue-specific or organ-specific lumen-exposed polypeptides attached to therapeutic moieties for targeted treatment and prevention.

Abstract: Methods and compositions for targeting of pharmaceuticals or other therapeutics to specific tissues using tissue-specific endothelial membrane proteins are provided. The compositions comprise a therapeutic complex composed of a ligand, a linker, and a therapeutic moiety, where the therapeutic moiety can enter the cell. The ligand can be an antibody or other molecule that binds to a tissue-specific protein on the endothelial membrane of a specific tissue. The ligand need not activate a receptor, but may activate endocytosis. The therapeutic moiety can be a drug, gene, antisense oligonucleotide, contrast agent, protein, toxin, or any type of molecule that acts on the specific tissue. The linker can be a liposome or a cleavable or noncleavable chemical molecule. Alternatively, the linker may simply be the bond between the ligand and the therapeutic moiety. Alternatively, a lipophilic prodrug may be cleaved and may enter the cell due to its lipophilic properties.

Abstract: A method for specifically immunoprecipitating albumin from a serum sample, using a “collapsible affinity matrix.” Also provided is a method for the co-removal of immunoglobulin using a “collapsible affinity matrix.” Removal of the highly abundant serum proteins, albumin and immunoglobulin, thereby improves the fractionation of the remaining serum proteins. Due to the collapsible nature of the matrix, less protein is trapped in the void space. Through specific removal of the abundant serum proteins by the collapsible affinity matrix and application of a two dimensional gel electrophoresis method, HiCap 2-D PAGE, the concentrations of a large number of low abundant serum proteins are estimated simultaneously, allowing the identification of several disease-related proteins in a relatively short period of time.

Abstract: A method for specifically immunoprecipitating albumin from a serum sample, using a “collapsible affinity matrix.” Also provided is a method for the co-removal of immunoglobulin using a “collapsible affinity matrix.” Removal of the highly abundant serum proteins, albumin and immunoglobulin, thereby improves the fractionation of the remaining serum proteins. Due to the collapsible nature of the matrix, less protein is trapped in the void space. Through specific removal of the abundant serum proteins by the collapsible affinity matrix and application of a two dimensional gel electrophoresis method, HiCap 2-D PAGE, the concentrations of a large number of low abundant serum proteins are estimated simultaneously, allowing the identification of several disease-related proteins in a relatively short period of time.