Abstract: Provided herein are single-chain polypeptides and multi-chain polypeptides that bind specifically to CD3 epsilon (CD3?). Also provided herein are anti-idiotypic antibodies that bind specifically to any of the antigen-binding domains described herein.

Abstract: The invention relates generally to antibodies that bind PSMA, and methods of making and using these anti-PSMA antibodies in a variety of therapeutic, diagnostic and prophylactic indications.

Abstract: Provided herein are single-chain polypeptides and multi-chain polypeptides that bind specifically to CD3 epsilon (CD3?). Also provided herein are anti-idiotypic antibodies that bind specifically to any of the antigen-binding domains described herein.

Abstract: The present invention relates to a mold for manufacturing a sole from a plurality of particles.

Abstract: A sole mold for manufacturing a sole from a plurality of particles includes at least one first opening for supplying the particles, and at least two second openings for supplying a gaseous and/or liquid medium to bond and/or fuse the particles together. At least a portion of the sole mold is manufactured by an additive manufacturing method.

Abstract: The present invention relates to a mold for manufacturing a sole from a plurality of particles, (FIG.

Abstract: A sole mold for manufacturing a sole from a plurality of particles includes at least one first opening for supplying the particles, and at least two second openings for supplying a gaseous and/or liquid medium to bond and/or fuse the particles together. At least a portion of the sole mold is manufactured by an additive manufacturing method.

Abstract: A sole mold for manufacturing a sole from a plurality of particles includes at least one first opening for supplying the particles, and at least two second openings for supplying a gaseous and/or liquid medium to bond and/or fuse the particles together. At least a portion of the sole mold is manufactured by an additive manufacturing method.

Abstract: A sole mold for manufacturing a sole from a plurality of particles includes at least one first opening for supplying the particles, and at least two second openings for supplying a gaseous and/or liquid medium to bond and/or fuse the particles together. At least a portion of the sole mold is manufactured by an additive manufacturing method.

Abstract: This method of tightening a threaded fastener (6) to a predetermined torque comprises steps in which: axial and rotational coupling is begun, by surface shrinking to a tight fit, of the threaded fastener (6) to a tightening member (2) capable of turning the threaded fastener (6) and thereby tightening it, the tightening member (2) and the threaded fastener (6) being able, from an initial coupled configuration between the tightening member and the threaded fastener, to remain rotationally coupled at a rotary drive torque, transmitted by the tightening member to the threaded fastener, that is less than the predetermined tightening torque, and to be rotationally decoupled from each other at a rotary drive torque, transmitted by the tightening member to the threaded fastener, that is equal to the predetermined tightening torque; and from this initial coupled configuration, a rotary movement is applied to the tightening member (2) up to a rotary drive torque, transmitted by the tightening member (2) to the threade

Abstract: Described is a novel family of cell surface serpentine transmembrane antigens. Two of the proteins in this family are exclusively or predominantly expressed in the prostate, as well as in prostate cancer, and thus members of this family have been termed “STEAP” (Six Transmembrane Epithelial Antigen of the Prostate). Four particular human STEAPs are described and characterized herein. The human STEAPs exhibit a high degree of structural conservation among them but show no significant structural homology to any known human proteins. The prototype member of the STEAP family, STEAP-1, appears to be a type IIIa membrane protein expressed predominantly in prostate cells in normal human tissues. Structurally, STEAP-1 is a 339 amino acid protein characterized by a molecular topology of six transmembrane domains and intracellular N- and C-termini, suggesting that it folds in a “serpentine” manner into three extracellular and two intracellular loops.

Abstract: This method of tightening a threaded fastener (6) to a predetermined torque comprises steps in which: axial and rotational coupling is begun, by surface shrinking to a tight fit, of the threaded fastener (6) to a tightening member (2) capable of turning the threaded fastener (6) and thereby tightening it, the tightening member (2) and the threaded fastener (6) being able, from an initial coupled configuration between the tightening member and the threaded fastener, to remain rotationally coupled at a rotary drive torque, transmitted by the tightening member to the threaded fastener, that is less than the predetermined tightening torque, and to be rotationally decoupled from each other at a rotary drive torque, transmitted by the tightening member to the threaded fastener, that is equal to the predetermined tightening torque; and from this initial coupled configuration, a rotary movement is applied to the tightening member (2) up to a rotary drive torque, transmitted by the tightening member (2) to the threade

Abstract: Described is a gene and its encoded secreted tumor antigen, termed 36P6D5, and to diagnostic and therapeutic methods and compositions useful in the management of various cancers which express 36P6D5, particularly including cancers of the bladder, kidney, prostate, breast, colon, ovary and pancreas.

Abstract: A novel gene (designated PHOR-1) that is highly over-expressed in prostate and other cancers and its encoded protein are described. PHOR-1 is a G protein-coupled receptor with homology to receptors involved in olfaction. PHOR-1 in normal human tissues is restricted to prostate, and this gene is highly over-expressed in prostate cancer as well as in cancers of the kidney, uterus, cervix, stomach and rectum. Consequently, PHOR-1 provides a diagnostic and/or therapeutic target for prostate cancer.

Abstract: A novel gene (designated 101P3A11 or PHOR-1) and its encoded protein, and variants thereof, are described wherein 101P3A11 exhibits tissue specific expression in normal adult tissue, and is aberrantly expressed in the cancers listed in Table I. Consequently, 101P3A11 provides a diagnostic, prognostic, prophylactic and/or therapeutic target for cancer. The 101P3A11 gene or fragment thereof, or its encoded protein, or variants thereof, or a fragment thereof, can be used to elicit a humoral or cellular immune response; antibodies or T cells reactive with 101P3A11 can be used in active or passive immunization.

Abstract: A novel gene 0161P2F10B (also designated 161P2F10B) and its encoded protein, and variants thereof, are described wherein 161P2F10B exhibits tissue specific expression in normal adult tissue, and is aberrantly expressed in the cancers listed in Table I. Consequently, 161P2F10B provides a diagnostic, prognostic, prophylactic and/or therapeutic target for cancer. The 161P2F10B gene or fragment thereof, or its encoded protein, or variants thereof, or a fragment thereof, can be used to elicit a humoral or cellular immune response; antibodies or T cells reactive with 161P2F10B can be used in active or passive immunization.

Abstract: Described is a novel family of cell surface serpentine transmembrane antigens. Two of the proteins in this family are exclusively or predominantly expressed in the prostate, as well as in prostate cancer, and thus members of this family have been termed “STEAP” (Six Transmembrane Epithelial Antigen of the Prostate). Four particular human STEAPs are described and characterized herein. The human STEAPs exhibit a high degree of structural conservation among them but show no significant structural homology to any known human proteins. The prototype member of the STEAP family, STEAP-1, appears to be a type IIIa membrane protein expressed predominantly in prostate cells in normal human tissues. Structurally, STEAP-1 is a 339 amino acid protein characterized by a molecular topology of six transmembrane domains and intracellular N- and C-termini, suggesting that it folds in a “serpentine” manner into three extracellular and two intracellular loops.

Abstract: Described is a novel family of cell surface serpentine transmembrane antigens. Two of the proteins in this family are exclusively or predominantly expressed in the prostate, as well as in prostate cancer, and thus members of this family have been termed “STEAP” (Six Transmembrane Epithelial Antigen of the Prostate). Four particular human STEAPs are described and characterized herein. The human STEAPs exhibit a high degree of structural conservation among them but show no significant structural homology to any known human proteins. The prototype member of the STEAP family, STEAP-1, appears to be a type IIIa membrane protein expressed predominantly in prostate cells in normal human tissues. Structurally, STEAP-1 is a 339 amino acid protein characterized by a molecular topology of six transmembrane domains and intracellular N- and C-termini, suggesting that it folds in a “serpentine” manner into three extracellular and two intracellular loops.

Abstract: Described is a novel family of cell surface serpentine transmembrane antigens. Two of the proteins in this family are exclusively or predominantly expressed in the prostate, as well as in prostate cancer, and thus members of this family have been termed “STEAP” (SIX Transmembrane Epithelial Antigens of the Prostate). Four particular human STEAPs are described and characterized herein. The human STEAPs exhibit a high degree of structural conservation among them but show no significant structural homology to any known human proteins. The prototype member of the STEAP family, STEAP-1, appears to be a type IIIa membrane protein expressed predominantly in prostate cells in normal human tissues. Structurally, STEAP-1 is a 339 amino acid protein characterized by a molecular topology of six transmembrane domains and intracellular N— and C-termini, suggesting that it folds in a “serpentine” manner into three extracellular and two intracellular loops.

Abstract: Described is a novel family of cell surface serpentine transmembrane antigens. Two of the proteins in this family are exclusively or predominantly expressed in the prostate, as well as in prostate cancer, and thus members of this family have been termed “STEAP” (Six Transmembrane Epithelial Antigen of the Prostate). Four particular human STEAPs are described and characterized herein. The human STEAPs exhibit a high degree of structural conservation among them but show no significant structural homology to any known human proteins. The prototype member of the STEAP family, STEAP-1, appears to be a type IIIa membrane protein expressed predominantly in prostate cells in normal human tissues. Structurally, STEAP-1 is a 339 amino acid protein characterized by a molecular topology of six transmembrane domains and intracellular N- and C-termini, suggesting that it folds in a “serpentine” manner into three extracellular and two intracellular loops.