Abstract: A pharmaceutical formulation and method of treatment of prion disease include a RAP agent with a pharmaceutically acceptable carrier and/or excipient, and the administration of same to a subject suffering from or at risk of a prion disease. The RAP agent is an effective means for the prevention and/or treatment of various prion diseases regardless whether the disease is acquired by infection or by genetic mutation.

Abstract: The present invention relates to the fields of molecular biology, combinatorial chemistry and biochemistry. Particularly, the present invention describes methods and kits for dynamically reducing the variance between analyte taken from complex mixtures.

Abstract: The present invention relates to a hemostatic dressing which comprises a plurality of layers that contain resorbable materials and/or coagulation proteins. In particular, the invention includes dressings in which a layer of thrombin is sandwiched between a first and second layer of fibrinogen and wherein the layer of thrombin is not coextensive with the first and/or second layer of fibrinogen. The hemostatic dressings are useful for the treatment of wounded tissue.

Abstract: The invention discloses methods for sequential protein isolation and purification from a biological sample by affinity chromatography. Affinity chromatography is conducted using ligands or ligand support complexes that selectively and specifically bind to proteins in the biological sample. The ligands or ligand support complexes were contacted sequentially in a predetermined order with the biological sample to allow each ligand or ligand-support complex to sequentially bind a protein from the biological sample.

Abstract: A pharmaceutical formulation and method of treatment of prion disease include a RAP agent with a pharmaceutically acceptable carrier and/or excipient, and the administration of same to a subject suffering from or at risk of a prion disease. The RAP agent is an effective means for the prevention and/or treatment of various prion diseases regardless whether the disease is acquired by infection or by genetic mutation.

Abstract: The present invention is methods and compositions for reducing and preventing the excess accumulation of extracellular matrix in a tissue and/or organ or at a wound site using a combination of agents that inhibit TGF?, or using agents that inhibit TGF? in combination with agents that degrade excess accumulated extracellular matrix. The compositions and methods of the invention are used to treat conditions such as fibrotic diseases and scarring that result from excess accumulation of extracellular matrix, impairing tissue or organ function or skin appearance in a subject.

Abstract: Asymmetric cyanine dyes of Formula I bind nucleic acid but not red blood cell membrane, and function as photosensitizers when rigidly bound but not when free in solution. Unbound dye thus causes minimal oxidative damage. The dyes do not substantially accumulate in red blood cells, thereby minimizing hemolysis due to oxidative damage. Biological fluids can be disinfected by mixing the fluid with these asymmetric cyanine dye that binds to nucleic acid, irradiating the mixture, and recovering clinically significant components from the biological fluid and/or assaying the fluid for pathogens.

Abstract: The invention provides an isolated or purified peptide that binds at least one plasma protein. In one embodiment, the isolated or purified peptide binds to fibrinogen, comprises no more than 10 amino acids, and comprises an amino acid sequence Xaa1-Xaa2-Xaa3-Xaa4-Xaa5, an amino acid sequence Gly-Xaa6-Arg-Xaa7, or an amino acid sequence selected from specific amino acid sequences provided herein. Alternatively, the isolated or purified protein binds to ?1 proteinase inhibitor and/or a protein complex comprising Apo-A1 lipoprotein and paraoxonase. The peptide comprises no more than 10 amino acids and comprises an amino acid sequence Xaa8-Xaa8-Xaa1-His-Xaa1-Xaa3, and amino acid sequence His-Xaa8-Xaa9-Xaa1-Xaa10-Xaa2, or an amino acid sequence selected from specific amino acid sequences provided herein. In addition, the invention provides isolated or purified peptide that binds to von Willebrand Factor.

Abstract: The present invention provides a method for purifying butyrylcholinesterase from various biological fluids. Biological fluids include, e.g., blood, blood fractions, plasma, and bioreactor broths, and other such mixtures containing butyrylcholinesterase. In one embodiment, the invention provides a method for the production of purified, virally inactivated butyrylcholinesterase by contacting a biological fluid containing butyrylcholinesterase with a cationic exchange chromatography material, with an affinity chromatography material, and treating the fluid with solvent detergent. The resulting purified butyrylcholinesterase can also be subjected to a pasteurization step, and formulated in a sodium chloride/sodium phosphate solution for storage or lyophilization.

Abstract: A transgenic, non-human mammalian animal is capable of expressing a heterologous gene for human or other recombinant physiologically functional fibrinogen holoprotein or individual subunit chain polypeptides thereof or a modified or fusion fibrinogen in mammary glands of the animals and secreting the expressed product into a body fluid. Methodology employing such a mammal yields recombinant physiologically functional fibrinogens, subunit chain polypeptides thereof, and modified or fusion fibrinogens.

Abstract: The invention provides an isolated or purified peptide that binds at least one plasma protein. In one embodiment, the isolated or purified peptide binds to fibrinogen, comprises no more than 10 amino acids, and comprises an amino acid sequence Xaa1-Xaa2-Xaa3-Xaa4-Xaa5, and amino acid sequence Gly-Xaa6-Arg-Xaa7, or an amino acid sequence selected from specific amino acid sequences provided herein. Alternatively, the isolated or purified protein binds to ?1 proteinase inhibitor and/or a protein complex comprising Apo-A1 lipoprotein and paraoxonase. The peptide comprises no more than 10 amino acids and comprises an amino acid sequence Xaa8-Xaa1-His-Xaa1-Xaa3, and amino acid sequence His-Xaa8-Xaa9-Xaa1-Xaa10-Xaa2, or an amino acid sequence selected from specific amino acid sequence provided herein. In addition, the invention provides isolated or purified peptide that binds to von Willebrand Factor.

Abstract: The present invention provides methods and apparatus for the rapid and efficient collection and purification of activated monocytes. The methods and apparatus of the present invention provide means for effecting the collection and purification in an aseptic environment. The method involves filtering a blood component mixture through a monocyte-adhering filter; washing the blood component mixture; backflushing the filter with a physiological solution; and backflushing the filter with Dextran-40/serum albumin.

Abstract: Disclosed are compounds of the formula (I): wherein R3, R4, R5, R9, and R10 are selected from the group consisting of H and groups or atoms other than H, and R6 and R8 are halo or hydrogen; X1, X2, and X3 are independently O or S; provided that R9 and R10 are not simultaneously H, when all of X1, X2, and X3 are O; and of the formula (II) wherein R11-R14 are selected from the group consisting of H and groups or atoms other than H; X4-X9 are independently O or S; n and m are 0 or 1 but m and n cannot be 0 simultaneously; R15-R24 can be H or any substituent so long as the compound of formula II upon hydrolysis provides a fluorescent compound. These compounds are useful as substrates with high specificity for organophosphatase particularly human paraoxonase and bacterial organophosphorus hydrolase.

Abstract: The present invention provides a method for purifying butyrylcholinesterase from various biological fluids. Biological fluids include, e.g., blood, blood fractions, plasma, and bioreactor broths, and other such mixtures containing butyrylcholinesterase. In one embodiment, the invention provides a method for the production of purified, virally inactivated butyrylcholinesterase by contacting a biological fluid containing butyrylcholinesterase with a cationic exchange chromatography material, with an affinity chromatography material, and treating the fluid with solvent detergent. The resulting purified butyrylcholinesterase can also be subjected to a pasteurization step, and formulated in a sodium chloride/sodium phosphate solution for storage or lyophilization.

Abstract: The present invention relates to full-length WF-HABP, WF-HABP, OE-HABP, and BM-HABP, novel members of the hyaluronan receptor family. The invention provides isolated nucleic acid molecules encoding human to full-length WF-HABP, WF-HABP, OE-HABP, and BM-HABP receptors. Full-length WF-HABP, WF-HABP, OE-HABP, and BM-HABP polypeptides are also provided, as are vectors, host cells and recombinant methods for producing the same. The invention further relates to screening methods for identifying agonists and antagonists of full-length WF-HABP, WF-HABP, OE-HABP, and BM-HABP receptor activity. Also provided are diagnostic methods for detecting disease states related to the aberrant expression of full-length WF-HABP, WF-HABP, OE-HABP, and BM-HABP receptors.

Abstract: A library of mutants of metastable proteins, such as proteinase inhibitors, can be screened for the specific loss of a wild-type capability to bind an antibody, yielding valuable drug-design information which otherwise is unavailable. By this approach, for example, a mutant proteinase inhibitor can be obtained that has the amino acid sequence of a wild-type protein, or an active fragment thereof, save for the presence of one or more mutations in at least one epitope, thereby altering interaction of the mutant with an anti-proteinase inhibitor antibody.

Abstract: This invention provides supplemented and unsupplemented tissue sealants as well as methods for their production and use thereof. Disclosed are tissue sealants supplemented with at least one antibody. The composition may be further supplemented with, for example, one or more analgesics, antimicrobial compositions, anticoagulants, antiproliferatives, anti-inflammatory compounds, cytokines, cytotoxins, drugs, growth factors, interferons, hormones, lipids, demineralized bone or bone morphogenetic proteins, cartilage inducing factors, oligonucleotides polymers, polysaccharides, polypeptides, protease inhibitors, vasoconstrictors or vasodilators, vitamins, minerals, stabilizers and the like.

Abstract: The invention provides an isolated or purified peptide that binds at least one plasma protein. In one embodiment, the isolated or purified peptide binds to fibrinogen, comprises no more than 10 amino acids, and comprises an amino acid sequence Xaa1-Xaa2-Xaa3-Xaa4-Xaa5, an amino acid sequence Gly-Xaa6-Arg-Xaa7, or an amino acid sequence selected from specific amino acid sequences provided herein. Alternatively, the isolated or purified protein binds to ?l proteinase inhibitor and/or a protein complex comprising Apo-A1 lipoprotein and paraoxonase. The peptide comprises no more than 10 amino acids and comprises an amino acid sequence Xaa8-Xaa8-Xaa1-His-Xaa1-Xaa3, and amino acid sequence His-Xaa8-Xaa9-Xaa1-Xaa10-Xaa2, or an amino acid sequence selected from specific amino acid sequences provided herein. In addition, the invention provides isolated or purified peptide that binds to von Willebrand Factor.

Abstract: The invention provides a method of characterizing a target that binds to a ligand. The method comprises providing ligands, optionally attached to a support, and contacting the ligands with targets to allow at least one target to bind to at least one ligand. The method further comprises immobilizing the resulting complexes in a first matrix, such that each complex has a different position within the first matrix, and transferring the target of the complex to a second matrix. The position of the target within the second matrix corresponds to the position of the ligand-support complex within the first matrix. The target on the second matrix is then detected.