Abstract: The invention provides devices for the disruption of one or more layers of skin and methods of their use to administer therapeutic agents, e.g., antigens or drugs. The devices are designed to disrupt a defined area of skin. The defined area can approximate the area that a patch or other suitable vehicle for therapeutic agent, e.g., drug or vaccine, delivery is designed to contact. Exemplary devices employ a mask to define the area to be disrupted. Other devices disrupt a defined area by rotating in place. For devices that employ a mask that is secured to the skin, the invention provides methods of disrupting the stratum corneum by first securing the mask to the skin and then disrupting the skin. For rotating devices, the disrupting member is simply placed against the skin and actuated to effect disruption.

Abstract: Addition of a bacterial ADP-ribosylating exotoxin (bARE) to a formulation (e.g., immunogen or vaccine) or a system (e.g., patch or kit) for immunization enhances the immune response in a subject to one or more components of the formulation. Binding of the B subunit of a bARE to ganglioside GM1 of the subject in vivo, however, mediates toxicity and limits the use of native bARE as adjuvants. Mutation or in vitro coupling of the B subunit to ligands such as GM1 inhibits binding to GM1 in vivo, thereby eliminating toxicity but retaining desired adjuvant activity. The use of such detoxified, GM-1 binding deficient exotoxins provides a safe and potent new strategy for development of effective formulation for immunization.

Abstract: Indications associated with dysfunction or malfunction of hematopoiesis or lymphopoiesis are treated with a CIF (TGF-.beta.).

Abstract: Treatment with Transforming Growth Factor-.beta. alone or in combination with a Colony Stimulating Factor therapeutically increases the number of granulocytes and monocyte/macrophages in mammals.

Abstract: Inflammation, acute and/or chronic, is treated with a CIF (TGF-.beta.). The CIF may be administered locally or systemically, depending upon the indication, and does not require coadministration or activator or cofactor for efficacy.

Abstract: Inflammation, acute and/or chronic, is treated with a CIF (TGF-beta). The CIF may be administered locally or systemically, depending upon the indication, and does not require coadministration of activator or cofactor for efficacy.

Abstract: Two proteins that are found in bone and that have in vivo chondrogenic/osteogenic activity in combination with a co-factor are described. Both proteins also were active in combination with EGF in the in vitro TGF-.beta. assay. Each has a molecular weight of approximately 26,000 daltons by SDS-PAGE. Each is reduced to a single polypeptide indicating that the proteins are probably homodimers. One has an N-terminal sequence identical to that of human placenta-derived TGF-.beta. whereas the other has an N-terminal sequence that is different from that of TGF-.beta. derived from human placenta. The two proteins may be purified to hmogeneity using RP-HPLC or acetic acid-urea gel electrophoresis.

Abstract: Two proteins that are found is bone and that have in vivo chondrogenic/osteogenic activity in combination with a co-factor are described. Both proteins also were active in combination with EGF in the in vitro TGF-.beta. assay. Each has a molecular weight of approximately 26,000 daltons by SDS-PAGE. Each is reduced to a single polypeptide indicating that the proteins are probably homodimers. One has an N-terminal sequence identical to that of human placenta-derived TGF-.beta. whereas the other has an N-terminal sequence that is different from that of TGF-.beta. derived from human placenta. The two proteins may be purified to homogeneity using RP-HPLC or acetic acid-urea gel electrophoresis.

Abstract: Inflammation, acute and/or chronic, is treated with a CIF (TGF-.beta.). The CIF may be administered locally or symstemically, depending upon the indication, and does not require coadministraion of activator or cofactor for efficacy.

Abstract: Two proteins that are found in bone and that have in vivo chondrogenic/osteogenic activity in combination with a co-factor are described. Both proteins also were active in combination with EGF in the in vitro TGF-.beta. assay. Each has a molecular weight of approximately 26,000 daltons by SDS-PAGE. Each is reduced to a single polypeptide indicating that the proteins are probably homodimers. One has an N-terminal sequence identical to that of human placenta-derived TGF-.beta. whereas the other has an N-terminal sequence that is different from that of TGF-.beta. derived from human placenta. The two proteins may be purified to homogeneity using RP-HPLC or acetic acid-urea gel electrophoresis.

Abstract: Two proteins that are found in bone and that have in vivo chondrogenic/osteogenic activity in combination with a co-factor are described. Both proteins also were active in combination with EGF in the in vitro TGF-.beta. assay. Each has a molecular weight of approximately 26,000 daltons by SDS-PAGE. Each is reduced to a single polypeptide indicating that the proteins are probably homodimers. One has an N-terminal sequence identical to that of human placenta-derived TGF-.beta. whereas the other has an N-terminal sequence that is different from that of TGF-.beta. derived from human placenta. The two proteins may be purified to homogeneity using RP-HPLC or acetic acid-urea gel electrophoresis.

Abstract: Two proteins that are found is bone and that have in vivo chondrogenic/osteogenic activity in combination with a co-factor are described. Both proteins also were active in combination with EGF in the in vitro TGF-.beta. assay. Each has a molecular weight of approximately 26,000 daltons by SDS-PAGE. Each is reduced to a single polypeptide indicating that the proteins are probably homodimers. One has an N-terminal sequence identical to that of human placenta-derived TGF-.beta. whereas the other has an N-terminal sequence that is different from that of TGF-.beta. derived from human placenta. The two proteins may be purified to homogeneity using RP-HPLC or acetic acid-urea gel electrophoresis.

Abstract: Two proteins that are found in bone and that have in vivo chondrogenic/osteogenic activity in combination with a co-factor are described. Both proteins also were active in combination with EGF in the in vitro TGF-.beta. assay. Each has a molecular weight of approximately 26,000 daltons by SDS-PAGE. Each is reduced to a single polypeptide indicating that the proteins are probably homodimers. One has an N-terminal sequence identical to that of human placenta-derived TGF-.beta. whereas the other has an N-terminal sequence that is different from that of TGF-.beta. derived from human placenta. The two proteins may be purified to homogeneity using RP-HPLC or acetic acid-urea gel electrophoresis.