The present disclosure relates to a dissociation reagent for tumor tissues. The dissociation reagent does not contain collagenase or trypsin but further contains hyaluronidase or a mixture of hyaluronidase and DNase I. The present disclosure also relates to use of the dissociation reagent in dispersing tumor tissues and detecting expression level of molecular markers on cell surface by flow cytometry. The dissociation reagent of the present disclosure does not cause degradation of molecular markers on cell surface such as CD8, PD-1, Tim-3, Lag-3 and the like, thus does not affect downstream assays.

This invention pertains to a fluorescence lifetime imaging microscopy (FLIM)-based method for the quantitative three-dimensional (3D) imaging of the metabolic status of a lesion, including the acquisition of FLIM data of a least one anaerobic glycolysis marker. This method applies in particular to lesions such as wounds and tumours, and to markers such as the NADH/NAD+ ratio, the NAD(P)H/NAD+ ratio, the NADH/FAD ratio, the NAD(P)H/FAD ratio or the FADH/FAD ratio as a first marker, and their optional combination with a second marker such as pH, oxygen tension, glucose, pyruvate and lactate.

Anti-PD-L1 antibodies are disclosed. Also disclosed are pharmaceutical compositions comprising such antibodies, and uses and methods using the same.

The present description relates to peptides, proteins, nucleic acids and cells for use in immunotherapeutic methods. In particular, the present description relates to the immunotherapy of cancer. The present description further relates to tumor-associated T-cell peptide epitopes, alone or in combination with other tumor-associated peptides that can for example serve as active pharmaceutical ingredients of vaccine compositions that stimulate anti-tumor immune responses, or to stimulate T-cells ex vivo and transfer into patients. Peptides bound to molecules of the major histocompatibility complex (MHC), or peptides as such, can also be targets of antibodies, soluble T-cell receptors, and other binding molecules.

The present invention refers to an in vitro method for the diagnosis of colorectal cancer and/or pre-cancerous stage thereof.

The invention provides methods for enriching extracellular vesicles (EVs), including exosomes, from biological fluid samples from subjects, and optionally further testing the EVs for the presence of specific biomarkers.

A method for predicting efficacy of treatment of a lung cancer patient using an immune checkpoint inhibitor includes isolating exosomes from a biological sample derived from the lung cancer patient, and determining an expression level of a protein present in the exosomes by a mass spectrometry method, in which the protein is one or more proteins selected from the group of proteins shown in Table 1-1 to Table 1-6.

Disclosed herein are in vitro methods of multiple staining and slide preparation for a cytopathological sample, such as a urine sample. These methods enable simultaneous staining of biomarkers and cytopathological stains to greatly enhance confidence in identifying atypical cells such as cancer cells. Also disclosed herein are methods of using said staining and preparation methods for the detection of bladder cancer using urine samples from a patient. These methods offer increased sensitivity and specificity over conventional bladder cancer detection methods. Also disclosed herein are the urinary exfoliated cells stained according to the methods provided herein.

This document relates to methods and materials involved in assessing and/or treating mammals (e.g., humans) having cancer (e.g., a SCD1-associated cancer). For example, methods for determining whether or not a cancer is likely to be responsive to one or more stearoyl CoA desaturase 1 (SCD1) polypeptide inhibitors (e.g., a selective SCD1 inhibitor (SSI)) are provided. In some cases, the methods and materials for treating a mammal by administering, to the mammal, one or more cancer treatments that is/are selected based, at least in part, on whether or not the mammal is likely to be responsive to one or more SCD1 polypeptide inhibitors e.g., SSI-4) are provided.

We examined IQGAP1 copy gain and its relationship with clinicopathologic outcomes of thyroid cancer and investigated its role in cell invasion and molecules involved in the process. We found IQGAP1 copy number (CN) gain≧3 in 1 of 30 (3%) of benign thyroid tumor, 24 of 74 (32%) follicular variant papillary thyroid cancer (FVPTC), 44 of 107 (41%) follicular thyroid cancer (FTC), 8 of 16 (50%) tall cell papillary thyroid cancer (PTC), and 27 of 41 (66%) anaplastic thyroid cancer, in increasing order of invasiveness of these tumors. A similar tumor distribution trend of CN≧4 was also seen. IQGAP1 copy gain was positively correlated with IQGAP1 protein expression. It was significantly associated with extrathyroidal and vascular invasion of FVPTC and FTC and, remarkably, a 50%-60% rate of multifocality and recurrence of BRAF mutation-positive PTC (P=0.01 and 0.02, respectively). The siRNA knockdown of IQGAP1 dramatically inhibited thyroid cancer cell invasion and colony formation. Co-immunoprecipitation assay showed direct interaction of IQGAP1 with E-cadherin, a known invasion-suppressing molecule, which was upregulated when IQGAP1 was knocked down. IQGAP1, through genetic copy gain, plays an important role in the invasiveness of thyroid cancer and represents a useful prognostic marker and therapeutic target for this and other cancers.