Expression Pathology Inc.

Rockville, MD, United States

Expression Pathology Inc.

Rockville, MD, United States
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Patent
Expression Pathology Inc. | Date: 2017-05-17

The current disclosure provides for specific peptides, and derived ionization characteristics of the peptides, from the GTPase KRas Protein (KRas) that are particulariy advantageous for quantifying the KRas 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,


Patent
Expression Pathology Inc. | Date: 2017-03-22

The present invention is related to a method for measuring the level of Her2 protein and truncated Her2 protein in a protein digest prepared from a biological sample of formalin-fixed tissue, comprising detecting and quantifying a peptide derived from the intracellular domain of Her2 in said protein digest prepared from said biological sample using mass spectrometry; and calculating the level of Her2 protein and truncated Her2 protein in said sample, wherein said peptide is the peptide of SEQ ID NO:7 and wherein said level is an absolute level of both versions of the Her2 protein.


The current disclosure provides for specific peptides, and derived ionization characteristics of the peptides, from the tumor necrosis factor receptor super family member 8 protein (CD30) that are particularly advantageous for quantifying the CD30 protein directly in biological samples that 5 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.


Patent
Expression Pathology Inc. | Date: 2017-05-10

Quantitative analysis of proteins that are targets of chemotherapy by Selected reaction monitoring (SRM)/Multiple Reaction Monitoring (MRM) mass spectrometry, by measuring modified forms of disclosed specific peptides from the ENT1, ERCC1, FOLR1, RRM1, TUBB3, TOP01, and/or TOP02A proteins. These peptides can be quantified if a modified form thereof comprises a phosphorylated, tyrosine, threonine, serine, and/or other amino acid residues within their amino acid sequence. Biological samples that have been fixed in formalin are used for the analysis.


Patent
Expression Pathology Inc. | Date: 2017-05-17

The current disclosure provides for specific peptides, and derived ionization characteristics of the peptides, from the Serine/Threoninc-Protein Kinase B-raf (BRAF) that are particularly advantageous for quantifying the BRAF 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 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.


Patent
Expression Pathology Inc. | Date: 2017-03-08

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. A protein sample is prepared from said biological sample using the Liquid Tissue reagents and protocol and the AXL 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 an AXL peptide is phosphorylation of a tyrosine, threonine, serine, and/or other amino acid residues within the peptide sequence.


Patent
Expression Pathology Inc. | Date: 2017-01-11

The current disclosure provides for specific peptides, and derived ionization characteristics of the peptides, from the GTPase KRas Protein (KRas) that are particularly advantageous for quantifying the KRas protein directly in biological samples that have been fixed in formalin by the 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,


Patent
Expression Pathology Inc. | Date: 2017-01-11

The current disclosure provides for specific peptides, and derived ionization characteristics of the peptides, from the Serine/Threoninc-Protein Kinase B-raf (BRAF) that are particularly advantageous for quantifying the BRAF protein directly in bio-logical 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 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.


Patent
Expression Pathology Inc. | Date: 2017-03-08

The current disclosure provides for specific peptides, and derived ionization characteristics of the peptides, from the Androgen receptor protein (AR) that are particularly advantageous for quantifying the AR 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 AR 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 an AR peptide is phosphorylation of a tyrosine, threonine, serine, and/or other amino acid residues within the peptide sequence.


Patent
Expression Pathology Inc. | Date: 2016-09-12

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.

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