Abstract: Methods are provided for identifying whether a cancer patient, and especially a breast cancer patient, will be responsive to treatment. Specified TOPO2A, IDO1 and/or p16 fragment peptides are precisely detected and quantitated by SRM-mass spectrometry directly in cancer cells collected from tumor tissue that was obtained from a cancer patient and compared to reference levels in order to determine if the cancer patient will positively respond to treatment. Measurement of TOPO2A provides a direct indication of whether a patient will respond to anthracycline-containing therapy, and, in particular, neoadjuvant anthracycline-containing therapy. Quantitative levels of IDO1 and p16 are compared to reference levels in order to determine if a breast cancer patient will likely demonstrate a pathologically complete response (pCR) of cancer after cancer therapy treatment, irrespective of the chosen treatment.

Abstract: Methods are provided for identifying whether a tumor, and especially a colon tumor, will be responsive to treatment with the therapeutic agent temozolomide. A specific MGMT fragment peptide is precisely detected and quantitated by SRM-mass spectrometry directly in colon cancer cells collected from colon tumor tissue obtained from a cancer patient. Comparison to reference levels determines if the cancer patient will respond positively or negatively to treatment with the chemotherapeutic agent temozolomide.

Abstract: A method is provided for quantifying the UCK2 protein in biological samples that have been fixed in formalin by the method of Selected Reaction Monitoring (SRM) mass spectrometry and utilizing said quantitation of UCK2 to predict the therapeutic outcome of treating a colon cancer patient with the combinatorial FOLFOX (5-fluorouracil, folinic acid, and oxaliplatin) treatment regimen.

Abstract: Improved methods for treating cancer are provided herein by determining if a cancer patient, particularly a colon cancer patient or a gastric cancer patient, will clinically respond in a favorable manner to a therapeutic strategy comprising the FOLFOX regimen (fluorouracil, leucovorin, and oxaliplatin) or a combination of capecitabine and cisplatin. Diagnostic methods for measuring the OPRT, TYMP, and/or UCK2 proteins in a tissue sample, such as a tumor sample, from the patient are provided.

Abstract: Methods are provided herein for identifying whether a cancer patient, for example a colorectal cancer patient, will be responsive to treatment with a therapeutic strategy comprising administration of the FOLFOX regimen (5-fluorouracil, leucovorin, and oxaliplatin). Specified TYMP and UCK2 fragment peptides are precisely detected and quantitated by SRM-mass spectrometry directly in tumor cells, for example colorectal cancer tumor cells, that are collected from tumor tissue obtained from a cancer patient and compared to reference levels in order to determine if the cancer patients will positively respond to treatment with the combination treatment of FOLFOX (5-fluorouracil, leucovorin, and oxaliplatin).

Abstract: Methods are provided for treating a cancer patient suffering from a glioblastoma (GBM) by administering to the patient an effective amount of temozolomide, wherein a mass spectrometry analysis of a protein digest of a formalin-fixed tumor sample from the patient evidences an amount of a MGMT fragment peptide less than or substantially equal to 150 amol/?g.

Abstract: The current disclosure provides specific peptides, and derived ionization characteristics of the peptides from the estrogen receptor (ER), progesterone receptor (PR), and/or antigen Ki67 (Ki67) proteins that are particularly advantageous for quantifying the ER, PR, and/or Ki67 proteins directly in biological samples that have been fixed in formalin by the method of Selected Reaction Monitoring/Multiple Reaction Monitoring (SRM/MRM) mass spectrometry. Such biological samples are chemically preserved and fixed wherein the biological sample is selected from tissues and cells treated with formaldehyde containing agents/fixatives including formalin-fixed tissue/cells, formalin-fixed/paraffin embedded (FFPE) tissue/cells, FFPE tissue blocks and cells from those blocks, and tissue culture cells that have been formalin fixed and or paraffin embedded.

Abstract: Methods are provided for identifying colon cancer patients whose genome shows either microsatellite stability (MSS) and/or a low tumor mutational burden (TMB) with a good prognosis, irrespective of treatment strategy. Specific protein fragment peptides of the p16 protein are precisely detected and quantitated by SRM-mass spectrometry directly in MSS and/or low TMB colon tumor cells collected from colon tumor tissue that was obtained from a colon cancer patient. The measured p16 levels are compared to p16 reference levels to determine if the MSS and/or low TMB colon cancer patient will have a longer overall survival.

Abstract: The current disclosure provides for specific peptides, and derived ionization characteristics of the peptides, from the tyrosine-protein kinase receptor UFO protein (AXL) that are particularly advantageous for quantifying the AXL protein directly in biological samples that have been fixed in formalin by the method of Selected Reaction Monitoring (SRM) mass spectrometry, or what can also be termed as Multiple Reaction Monitoring (MRM) mass spectrometry. Such biological samples are chemically preserved and fixed wherein said biological sample is selected from tissues and cells treated with formaldehyde containing agents/fixatives including formalin-fixed tissue/cells, formalin-fixed/paraffin embedded (FFPE) tissue/cells, FFPE tissue blocks and cells from those blocks, and tissue culture cells that have been formalin fixed and or paraffin embedded.

Abstract: Methods are provided for identifying whether a tumor, and especially a lung tumor, will be responsive to treatment with a therapeutic regimen that contains a platinum-based agent such as cisplatin and optionally contains a taxane. A specific Schlafen family member 11 (SLFN11) fragment peptide is precisely detected and quantitated by spectrometry directly in lung cancer cells collected from lung tumor tissue obtained from a cancer patient. Comparison to reference levels determines if the cancer patient will respond positively or negatively to treatment with the chemotherapeutic agents taxane plus a platinum-based agent such as cisplatin.

Abstract: The current disclosure provides for specific peptides, and derived ionization characteristics of the peptides, from the tumor necrosis factor receptor superfamily member 8 protein (CD30) that are particularly advantageous for quantifying the CD30 protein directly in biological samples that have been fixed in formalin by the method of Selected Reaction Monitoring (SRM) mass spectrometry, or what can also be termed as Multiple Reaction Monitoring (MRM) mass spectrometry. Such biological samples are chemically preserved and fixed wherein the biological sample is selected from tissues and cells treated with formaldehyde containing agents/fixatives including formalin-fixed tissue/cells, formalin-fixed/paraffin embedded (FFPE) tissue/cells, FFPE tissue blocks and cells from those blocks, and tissue culture cells that have been formalin fixed and or paraffin embedded.

Abstract: Methods are provided for detecting and quantifying the DLL1, DLL3, JAG1, JAG2, Notch1, Notch 2, Notch 3, Notch 4, and/or DLL4 proteins in biological samples, such as a formalin fixed paraffin embedded tissue samples, using mass spectrometry. Additionally, methods are provided for treating cancer based upon the level of the DLL1, DLL3, JAG1, JAG2, Notch1, Notch 2, Notch 3, Notch 4, and/or DLL4 proteins in the biological samples.

Abstract: Methods are provided for identifying whether a lung tumor will be responsive to treatment with the combination of the therapeutic agents cisplatin and pemetrexed. Specified ERCC1, TS, p16, and FR? fragment peptides are precisely detected and quantitated by SRM-mass spectrometry directly in lung tumor cells collected from lung tumor tissue that was obtained from a cancer patient and compared to reference levels in order to determine if the lung cancer patient will positively respond to treatment with the combination of cisplatin and pemetrexed therapeutic agents.

Abstract: Methods are provided for quantifying the cyclin-dependent kinase inhibitor 2A protein (p16) p16 protein directly in biological samples that have been fixed in formalin by SRM/MRM mass spectrometry. A protein sample is prepared from the biological sample using, for example, the Liquid Tissue reagents and protocol and the p16 protein is quantitated in the resulting sample by quantitating in the protein sample at least one fragment peptide from p16. Peptides can be quantitated in modified or unmodified form. An example of a modified form of a p16 peptide is phosphorylation of a tyrosine, threonine, serine, and/or other amino acid residues within the peptide sequence.

Abstract: Methods are provided for quantifying the fibroblast growth factor receptor 2 protein (FGFR2) directly in biological samples that have been fixed in formalin by the method of Selected Reaction Monitoring (SRM)/Multiple Reaction Monitoring (MRM) mass spectrometry. The biological sample may be selected from tissues and cells treated with formaldehyde containing agents/fixatives including formalin-fixed tissue/cells, formalin-fixed/paraffin embedded (FFPE) tissue/cells, FFPE tissue blocks and cells from those blocks, and tissue culture cells. A protein sample is prepared from the biological sample and the FGFR2 protein is quantitated in the sample using the method of SRM/MRM mass spectrometry by quantitating in the protein sample at least one fragment peptide derived from FGFR2.

Abstract: Improved methods for treating lung cancer are provided. Tumor samples from patients are analyzed (i) by DNA sequencing to detect the presence of HER2 mutations and (ii) by mass spectrometric proteomic analysis to determine whether HER2 protein is expressed in the tumor cells. Patients respond to therapy with trastuzumab emtansine (T-DM1) or an equivalent antibody-drug conjugate when unique HER2 protein fragments are detected in the patient's tumor cells that harbor HER2 mutations. Conversely, patients do not respond to T-DM1 therapy when the tumor cells contain HER2 mutations but the unique protein fragments are not detected. Detection of HER3 in the tumor cells is a positive predictor of response to treatment.

Abstract: Methods are provided for quantifying specific proteins directly in biological samples that have been fixed in formalin by SRM/MRM assay. Such biological samples are chemically preserved and fixed wherein said biological sample is selected from tissues and cells treated with formaldehyde containing agents/fixatives including formalin-fixed tissue/cells, formalin-fixed/paraffin embedded (FFPE) tissue/cells, FFPE tissue blocks and cells from those blocks. A protein digest is prepared from the biological sample using, for example, the Liquid Tissue reagents and protocol and a designated protein is quantitated in the digest sample by the method of SRM/MRM mass spectrometry by quantitating in the protein sample at least one or more of the described peptides. The proteins that can be detected and/or quantitated are CD3D, B7H3, B7-2, STAT1, GBP1, GPNMB, CD27, CD3E, and CD8.

Abstract: SRM/MRM assays are used to detect and quantitate proteins involved in the process of initiating, inhibiting, maintaining, and/or otherwise modulating a tumor immune response directly in patient tumor tissue. The assays provide an immune profile of the tissue microenvironment, and may be used as part of improved methods of immune-based treatment using agents that manipulate the cancer immune response together with cancer therapeutic agents.

Abstract: Methods of treating breast cancer are provided where a quantitative Her2 assay is used to identify whether a breast tumor will be responsive to treatment with anti-Her2 therapeutic agents such as lapatinib and trastuzumab, followed by selection of a suitable treatment regimen and administration of the regimen. A specific Her2 fragment peptide is precisely quantitated by SRM-mass spectrometry directly in breast tumor cells collected from breast tumor tissue that was obtained from a cancer patient and compared to a reference level in order to determine if the breast cancer patient will positively respond to treatment with a therapeutic agent that specifically targets the Her2 protein.

Abstract: Methods are provided for quantifying the TYMS, TYMP, UCK1, UCK2, UPP1, OPRT, dCK, TK1, DPYD, CDA, RRM1, and/or RRM2 proteins directly in biological samples that have been fixed in formalin by the method of Selected Reaction Monitoring/Multiple Reaction Monitoring (SRM/MRM). The biological samples are chemically preserved with formaldehyde-containing agents/fixatives including formalin-fixed tissue/cells, formalin-fixed/paraffin embedded (FFPE) tissue/cells, FFPE tissue blocks and cells from those blocks, and tissue culture cells that have been formalin fixed and or paraffin embedded. A protein digest sample is prepared from the biological sample and the TYMS, TYMP, UCK1, UCK2, UPP1, OPRT, dCK, TK1, DPYD, CDA, RRM1, and/or RRM2 proteins are quantitated in the digest by SRM/MRM mass spectrometry.