Expression Pathology, Inc. Patent applications |
Patent application number | Title | Published |
20150369818 | HER3 PROTEIN SRM/MRM ASSAY - The current disclosure provides for specific peptides, and derived ionization characteristics of the peptides, from the Receptor Tyrosine-Protein Kinase erbB-3, or Her3, that are particularly advantageous for quantifying the Her3 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. A protein sample is prepared from said biological sample using the Liquid Tissue™ reagents and protocol and the Her3 protein is quantitated in the Liquid Tissue™ sample by the method of SRM/MRM mass spectrometry by quantitating in the protein sample at least one or more of the peptides described. These peptides can be quantitated if they reside in a modified or an unmodified form. An example of a modified form of a Her3 peptide is phosphorylation of a tyrosine, threonine, serine, and/or other amino acid residues within the peptide sequence. | 12-24-2015 |
20140005282 | CMET PROTEIN SRM/MRM ASSAY | 01-02-2014 |
20130302334 | BCL-2-LIKE PROTEIN 11 SRM/MRM ASSAY - Specific peptides, and derived ionization characteristics of those peptides, from the Bcl-2-like protein 11 (BIM) are provided that are particularly advantageous for quantifying the BIM 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). Such biological samples are chemically preserved and fixed where 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. A protein sample is prepared from the biological sample using the Liquid Tissue™ reagents and protocol, and the BIM protein is quantitated in the Liquid Tissue™ sample by the method of SRM/MRM mass spectrometry by quantitating in the protein sample at least one or more of the peptides described. These peptides can be quantitated if they reside in a modified or an unmodified form. An example of a modified form of a BIM peptide is phosphorylation of a tyrosine, threonine, serine, and/or other amino acid residues within the peptide sequence. | 11-14-2013 |
20130302328 | TRUNCATED HER2 SRM/MRM ASSAY - This disclosure provides ten (10) specific peptides, and particular peptide characteristics, from the cell membrane-bound Her2 protein and a diagnostic assay useful for determining the presence and amount of full length and truncated versions of the full-length Her2 protein in cells derived from formalin fixed paraffin embedded tissue. | 11-14-2013 |
20130289142 | HER3 PROTEIN SRM/MRM ASSAY - The current disclosure provides for specific peptides, and derived ionization characteristics of the peptides, from the Receptor Tyrosine-Protein Kinase erbB-3, or Her3, that are particularly advantageous for quantifying the Her3 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. A protein sample is prepared from said biological sample using the Liquid Tissue™ reagents and protocol and the Her3 protein is quantitated in the Liquid Tissue™ sample by the method of SRM/MRM mass spectrometry by quantitating in the protein sample at least one or more of the peptides described. These peptides can be quantitated if they reside in a modified or an unmodified form. An example of a modified form of a Her3 peptide is phosphorylation of a tyrosine, threonine, serine, and/or other amino acid residues within the peptide sequence. | 10-31-2013 |
20130252840 | LIQUID TISSUE PREPARATION FROM HISTOPATHOLOGICALLY PROCESSED BIOLOGICALLY SAMPLES, TISSUES AND CELLS - The current invention provides a method for directly converting histopathologically processed biological samples, tissues, and cells into a multi-use biomolecule lysate. This method allows for simultaneous extraction, isolation, solublization, and storage of all biomolecules contained within the histopathologically processed biological sample, thereby forming a representative library of said sample. This multi-use biomolecule lysate is dilutable, soluble, capable of being fractionated, and used in any number of subsequent experiments. | 09-26-2013 |
20130131195 | c-Src Selected Reaction Monitoring Assay - Objective quantitation of the c-Src protein directly in cancer patient tissue can aid in determining the aggressiveness of an individual patient's tumor as well as help make more informed decisions about choice of therapy. However, the c-Src protein is currently analyzed directly in formalin fixed patient tissue only by immunohistochemistry methodology which is at best subjectively semi-quantitative. This invention describes an objective quantitative assay for the c-Src protein using mass spectrometry as the analytical methodology. Specific peptides, experimentally discovered characteristics about the peptides, and experimentally established assay conditions based on those peptide characteristics are provided for use in a mass spectrometry-based Selected Reaction Monitoring (SRM) assay in order to measure relative or absolute quantitative levels of c-Src directly in a protein preparation obtained from a formalin fixed cancer patient tissue sample. | 05-23-2013 |
20130079425 | Urokinase-Type Plasminogen Activator Protein /Plasminogen Activator Inhibitor Type-1 Protein Selected Reaction Monitoring Assay - Specific peptides are provided that are derived from subsequences of the urokinase-type plasminogen activator protein and the plasminogen activator inhibitor type-1 protein along with assays that can measure those peptides directly in complex protein lysate samples, including protein lysates prepared from histologicaly-processed formalin fixed tissue. The presence and amount of those peptides in samples from a subject can be associated with disease, including cancer, in a subject and provide information about the diagnostic stage/grade/status of the disease/cancer. | 03-28-2013 |
20130011408 | Epidermal Growth Factor Receptor (EGFR) Protein SRM Assay - The current disclosure provides for specific peptides from the Epidermal Growth Factor Receptor (EGFR) protein and the derived ionization characteristics of those peptides that are advantageous for quantifying the EGFR directly in formalin fixed biological samples by the method of Selected Reaction Monitoring (SRM) mass spectrometry. Such fixed biological samples include: formalin-fixed tissue/cells, formalin-fixed/paraffin embedded (FFPE) tissue/cells, FFPE tissue blocks and cells from those blocks, and formalin fixed and paraffin embedded tissue culture cells. EGFR protein is quantitated in biological samples by the method of SRM/MRM mass spectrometry by quantitating one or more of the peptides described herein. The peptides can be quantitated if they reside in a modified or an unmodified form. Examples of potentially modified forms of an EGFR peptides include those bearing phosphorylation of a tyrosine, threonine, serine, and/or other amino acid residues within the peptide sequence. | 01-10-2013 |
20120302650 | Insulin-Like Growth Factor 1 Receptor (IGF1R) Protein SRM/MRM Assay - The current disclosure provides for specific peptides from the Insulin-Like Growth Factor 1 Receptor (IGF-1R) protein and the derived ionization characteristics of those peptides that are advantageous for quantifying the IGF-1R directly in formalin fixed biological samples by the method of Selected Reaction Monitoring (SRM) mass spectrometry. Such fixed biological samples include: formalin-fixed tissue/cells, formalin-fixed/paraffin embedded (FFPE) tissue/cells, FFPE tissue blocks and cells from those blocks, and formalin fixed and paraffin embedded tissue culture cells. IGF-1R protein is quantitated in biological samples by the method of SRM/MRM mass spectrometry by quantitating one or more of the peptides described herein. The peptides can be quantitated if they reside in a modified or an unmodified form. Examples of potentially modified forms of an IGF-1R peptides include those bearing phosphorylation of a tyrosine, threonine, serine, and/or other amino acid residues within the peptide sequence. | 11-29-2012 |
20120295990 | Insulin Receptor Substrate 1 (IRS1) Protein SRM/MRM Assay - The current disclosure provides for specific peptides from the Insulin Receptor Substrate 1 (IRS1) protein and the derived ionization characteristics of those peptides that are advantageous for quantifying IRS1 directly in formalin fixed biological samples by the method of Selected Reaction Monitoring (SRM) mass spectrometry. Such fixed biological samples include: formalin-fixed tissue/cells, formalin-fixed/paraffin embedded (FFPE) tissue/cells, FFPE tissue blocks and cells from those blocks, and formalin fixed and paraffin embedded tissue culture cells. IRS1 protein is quantitated in biological samples by the method of SRM/MRM mass spectrometry by quantitating one or more of the peptides described herein. The peptides can be quantitated if they reside in a modified or an unmodified form. Examples of potentially modified forms of IRS1 peptides include those bearing phosphorylation of a tyrosine, threonine, serine, and/or other amino acid residues within the peptide sequence. | 11-22-2012 |
20110028344 | BIOMARKERS FOR ENDOMETRIAL DISEASE - This patent application discloses and describes a list of proteins that are found to be differentially expressed between normal endometrial epithelial cells and early stage cancerous endometrial epithelial cells. These proteins can be used either individually or in specific combinations in diagnostic and prognostic protein assays on various biological samples from endometrial cancer patients, or individuals suspected on having endometrial cancer. In addition, these proteins are also differentially expressed between normal endometrial epithelial cells and epithelial cells of other types of endometrial disease, and thus such diseases can be diagnosed using assays based on these proteins. The full length intact proteins can be assayed or peptides derived from these proteins can be assayed as reporters for these proteins. These proteins can also be identified as “companion diagnostic” proteins, wherein they are not only differentially expressed for use as diagnostic and prognostic indicators of endometrial cancer and other endometrial diseases, but the same proteins are also targets for therapeutic intervention of endometrial cancer and other endometrial diseases. | 02-03-2011 |