It is an object of the present invention to provide, for instance, a method for evaluating a function, such as transforming potential, of multiple different genes of interest, and a method capable of evaluating drug sensitivity of a subject having each gene of interest. The present invention relates to, for instance, a method for evaluating multiple different genes of interest, comprising the steps of: integrating, into host cell genomic DNA, polynucleotides each comprising a tag sequence and a gene of interest or a fragment thereof linked to the tag sequence; mixing a plurality of different host cells having the different polynucleotides integrated therein; culturing the mixed host cells; extracting the genomic DNA from the cultured host cells; quantifying each of the polynucleotides in the extracted genomic DNA based on the tag sequence; and determining a relative cell count of each of the host cells having the respective polynucleotides after the culturing, based on the quantified values for the polynucleotides.

Disclosed herein is a novel p53 complex and a collection of compounds that can tightly associate with p53 to efficiently rescue wildtype p53 structure and function, and the methods of making and using the complex and the compounds, including for diagnosis, prognosis, and treatment of p53 related disorders such as cancer and aging.

The present disclosure relates to compositions and methods for cancer diagnosis, research and therapy, including but not limited to, cancer markers. In particular, the present disclosure relates to RAF gene fusions as diagnostic markers and clinical targets for cancer.

The present invention provides antigen binding proteins that specifically bind to Wilms' tumor protein (WT1), including humanized, chimeric and fully human antibodies against WT1, antibody fragments, chimeric antigen receptors (CARs), fusion proteins, and conjugates thereof. The antigen binding proteins and antibodies bind to HLA-A0201-restricted WT1 peptide. Such antibodies, fragments, fusion proteins and conjugates thereof are useful for the treatment of WT1 associated cancers, including for example, breast cancer, ovarian cancer, prostate cancer, chronic myelocytic leukemia, multiple myeloma, acute lymphoblastic leukemia (ALL), acute myeloid/myelogenous leukemia (AML) and myelodysplastic syndrome (MDS). In more particular embodiments, the anti-WT1/A antibodies may comprise one or more framework region amino acid substitutions designed to improve protein stability, antibody binding and/or expression levels.

Methods of reducing chemotherapy-induced metastasis, or chemotherapy-induced cancer cell dissemination, for patients subject to chemotherapy using Tie-2 inhibitors. Methods of reducing chemotherapy-induced metastasis, or chemotherapy-induced cancer cell dissemination, for patients subject to chemotherapy using inhibitors of Mena expression and/or function are also provided.

An integrated dual-modality microfluidic sensor chip and methods for using the same. In one form, the sensor comprises a patterned periodic array of nanoposts coated with a noble metal and graphene oxide (GO) to detect target biomarker molecules in a limited sample volume. The device generates both electrochemical and surface plasmon resonance (SPR) signals from a single sensing area of the metal-GO nanoposts. The metal-GO nanoposts are functionalized with specific receptor molecules, serving as a spatially well-defined nanostructured working electrode for electrochemical sensing, as well as a nanostructured plasmonic crystal for SPR-based sensing via the excitation of surface plasmon polaritons. The integrated dual-modality sensor offers higher sensitivity (through higher surface area and diffusions from nanoposts for electrochemical measurements), as well as the dynamic measurements of antigen-antibody bindings (through the SPR measurement), while operating simultaneously in a same sensing area using a same sample volume.

A manufacturing method of a protein sensor includes the following steps. A hydrophobic material is provided and the hydrophobic material has a surface. An atmospheric pressure plasma process is performed to form a hydrophilic functional group on the surface of the hydrophobic material. A first antibody is immobilized on the surface of the hydrophobic material by the hydrophilic functional group. A mixed solution is prepared. The mixed solution includes a second antibody and an analyte, and the second antibody binds to the analyte. The mixed solution is reacted with the first antibody immobilized on the surface of the hydrophobic material to bind the first antibody to the analyte. Furthermore, a protein sensor manufactured by the above-described manufacturing method of the protein sensor is also provided.

Complexes containing a labeled polypeptide and an antibody, and the use of such complexes as research, diagnostic, and clinical tools, are described herein.

The present disclosure provides micro-array devices for capturing cells in blood and methods of their use. In some aspects, a method for counting cells in a blood sample is provided, the method comprising applying a blood sample onto a CNT device; allowing cells in the blood sample to differentially settle on the CNT device, and identifying and counting cells of preselected type in the blood sample.

Methods for histochemical and cytochemical detection of oncogenic rearrangements of genes that result in expression of a fusion protein; materials, kits, and systems useful in such methods; and products resulting from performance of such methods are disclosed herein. At least two protein binding entities are provided: one targeting a portion of a wild-type protein that is retained in a fusion protein and a one targeting a portion of the wild type protein that is lost during the rearrangement that forms the fusion protein. A sample of a tissue suspected of harboring the fusion protein is stained with each of the two entities (either in simplex format or multiplex format), and the staining pattern resulting from binding of the entities is compared to determine the presence or absence of the fusion protein.