Abstract: The present invention provides novel high affinity antibodies and fragments thereof that bind to the cancer antigen PSCA. The antibodies of the present invention may be used for cancer diagnosis, prognosis, treatment, visualization, and the like. The present invention also provides methods for the detection, visualization, and treatment of various cancers expressing PSCA.

Abstract: The present invention provides methods and compositions useful in the treatment or prevention of Chlamydia infections and cancer. The methods and compositions inhibit the entry of Chlamydia into a host cell expressing EMP2 by interfering with the interaction between the Chlamydia and EMP2. The methods and compositions target cancers which express or overexpress EMP2 nucleic acids and polypeptides by targeting EMP2.

Abstract: The present application provides fully human antibodies against N-Cadherin for therapeutic and diagnostic methods in cancer.

Abstract: Embodiments of the present invention utilize a more efficient CDR grafting technique to generate humanized versions of the T84.66 antibody. The technique used to generate these antibodies utilizes crystallographic structural data to select an immunoglobulin framework having maximum structural overlap with a non-human donor molecule. This technique was used to develop humanized T84.66 antibodies exhibiting in vitro binding affinity and specificity for carcinoembryonic antigen (CEA) nearly identical to that of T84.66 and the ability to specifically target tumors expressing CEA in vivo.

Abstract: The present invention provides anti-CD20 antibody fragments for use as in vivo imaging probes and as therapeutic moieties for the diagnosis and treatment of NHL.

Abstract: Conjugates of a C-terminal modified diabody and a nanoparticle are provided in which the C-terminal modification introduces a cysteine residue at a C-terminus of the diabody and the diabody is covalently linked to the nanoparticle via a heterobiofunctional linker attached to the introduced cysteine residue.

Abstract: The invention provides novel humanized antibody fragments that specifically bind prostate cell-surface antigen (PSCA), a protein which is overexpressed in variety of cancers, including prostate, bladder, and pancreatic cancer. Methods are provided for the use of the compositions of the invention for the treatment of cancer, diagnosis of cancer, to provide a prognosis of cancer progression, and for cancer imaging.

Abstract: The present invention provides methods of metabolically biotinylating recombinant proteins. Cell lines and specific protein and nucleic acid constructs for use in the methods of the present invention are also provided herein.

Abstract: Briefly described, embodiments of this disclosure include polynucleotides that encode mutant Cnidarian luciferases that exhibit modulated properties as compared to the corresponding wild-type luciferases, and the modulated properties include at least one of: modulated stability; enhanced light output; and modulated emission maximum. Embodiments of the present disclosure also include polypeptides or fragments thereof encoded by the polynucleotides, constructs including the polynucleotide, expression cassettes, cells, methods of producing the polynucleotides and polypeptides, antibodies, transgenic cells and/or animals, kits, and the like.

Abstract: A method for detecting the presence of an analyte in a solution. The analyte includes at least two mutually exclusive recognition sites that are capable of binding to corresponding recognition molecules. Biosensors are provided that include the recognition molecules, which are attached to the inactive portions of a split enzyme. The recognition sites are located such that the inactive enzyme portions combine to form a detectable biologically active enzyme when the recognition molecules bind to recognition sites.

Abstract: Embodiments of the present invention utilize a more efficient CDR grafting technique to generate humanized versions of the T84.66 antibody. The technique used to generate these antibodies utilizes crystallographic structural data to select an immunoglobulin framework having maximum structural overlap with a non-human donor molecule. This technique was used to develop humanized T84.66 antibodies exhibiting in vitro binding affinity and specificity for carcinoembryonic antigen (CEA) nearly identical to that of T84.66 and the ability to specifically target tumors expressing CEA in vivo.

Abstract: An antigen binding protein construct or "minibody" which includes the VL and VH domains of a native antibody fused to the hinge region and CH3 domain of the immunoglobulin molecule is described. Minibodies are small versions of whole antibodies which encode in a single chain the essential elements of a whole antibody. Minibodies are expressed by host cells transformed with minibody genes.