Patents by Inventor Todd Hembrough
Todd Hembrough has filed for patents to protect the following inventions. This listing includes patent applications that are pending as well as patents that have already been granted by the United States Patent and Trademark Office (USPTO).
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Publication number: 20150072895Abstract: The current disclosure provides for specific peptides, and derived ionization characteristics of the peptides, from the KRT5, KRT7, NapsinA, TTF1, TP63, and/or MUC1 proteins that are particularly advantageous for quantifying the KRT5, KRT7, NapsinA, TTF1, TP63, and/or MUC1 proteins 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.Type: ApplicationFiled: November 17, 2014Publication date: March 12, 2015Inventors: David B. KRIZMAN, Wei-Li LIAO, Sheeno THYPARAMBIL, Todd HEMBROUGH
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Publication number: 20140336281Abstract: Specific peptides, and derived ionization characteristics of the peptides, from the Ephrin Type-A Receptor 2 (EPHA2) protein are provided that are particularly advantageous for quantifying the EPHA2 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 and are 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.Type: ApplicationFiled: April 4, 2014Publication date: November 13, 2014Inventors: David B. Krizman, Wei-Li Liao, Sheeno Thyparambil, Todd Hembrough
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Publication number: 20140322245Abstract: Specific peptides, and derived ionization characteristics of the peptides, from the Insulin Receptor protein (IR), and its isoforms IR-A and IR-B, that are particularly advantageous for quantifying the IR protein, IR-A isoform and/or IR-B isoform, 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 and are 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.Type: ApplicationFiled: July 10, 2014Publication date: October 30, 2014Inventors: David B. KRIZMAN, Wei-Li LIAO, Sheeno THYPARAMBIL, Todd HEMBROUGH
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Publication number: 20140213478Abstract: Specific peptides, and derived ionization characteristics of the peptides, from the Receptor Tyrosine-Protein Kinase erbB-4 Protein (HER4) protein are provided that are particularly advantageous for quantifying the HER4 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.Type: ApplicationFiled: April 4, 2014Publication date: July 31, 2014Inventors: David B. KRIZMAN, Wei-Li LIAO, Sheeno THYPARAMBIL, Todd HEMBROUGH
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Publication number: 20140206776Abstract: Specific peptides, and derived ionization characteristics of those peptides from Death Receptor 5 (DR5) protein are provided that are particularly advantageous for quantifying the DR5 protein 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.Type: ApplicationFiled: March 24, 2014Publication date: July 24, 2014Inventors: David B. KRIZMAN, Todd HEMBROUGH, Sheeno THYPARAMBIL, Wei-Li LIAO
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Publication number: 20140206775Abstract: Specific peptides, and derived ionization characteristics of the peptides, from the Fatty acid synthase (FASN) protein are provided that are particularly advantageous for quantifying the FASN 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 and are 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.Type: ApplicationFiled: March 21, 2014Publication date: July 24, 2014Inventors: David B. KRIZMAN, Todd HEMBROUGH, Sheeno THYPARAMBIL, Wei-Li LIAO
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Publication number: 20140199717Abstract: 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.Type: ApplicationFiled: March 24, 2014Publication date: July 17, 2014Inventors: David B. KRIZMAN, Todd HEMBROUGH, Sheeno THYPARAMBIL, Wei-Li LIAO
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Patent number: 8728753Abstract: Peptides from the Insulin-Like Growth Factor 1 Receptor (IGF-1R) protein are provided that are particularly advantageous for quantifying the IGF-1 R protein directly in biological samples, such as samples fixed in formalin. The ionization characteristics of the peptides also are disclosed. The peptides may be used in Selected Reaction Monitoring (SRM) mass spectrometry methods, also referred to Multiple Reaction Monitoring (MRM) mass spectrometry methods. The samples are chemically preserved and fixed, such as 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 may be prepared from the biological sample and the IGF-IR protein is quantitated by the method of SRM/MRM mass spectrometry by quantitating one or more of the described peptides.Type: GrantFiled: June 21, 2012Date of Patent: May 20, 2014Assignee: Expression Pathology IncorporatedInventors: David B. Krizman, Todd Hembrough, Sheeno Thyparambil
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Publication number: 20140005282Abstract: Specific peptides are provided, and derived ionization characteristics of those peptides, from the Hepatocyte Growth Factor Receptor (cMET) protein. The peptides are particularly and surprisingly advantageous for quantifying by the method of Selected Reaction Monitoring (SRM) mass spectrometry the cMET protein directly in biological samples that have been fixed in formalin, 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.Type: ApplicationFiled: December 27, 2011Publication date: January 2, 2014Applicant: EXPRESSION PATHOLOGY, INC.Inventors: David Krizman, Todd Hembrough, Sheeno Thyparambil
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Publication number: 20130302334Abstract: 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.Type: ApplicationFiled: July 15, 2013Publication date: November 14, 2013Applicant: EXPRESSION PATHOLOGY, INC.Inventors: David Krizman, Todd Hembrough, Sheeno Thyparambil, Wei-Li Liao
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Publication number: 20130289142Abstract: 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.Type: ApplicationFiled: July 1, 2013Publication date: October 31, 2013Applicant: EXPRESSION PATHOLOGY, INC.Inventors: David Krizman, Todd Hembrough, Sheeno Thyparambil
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Publication number: 20130072581Abstract: The current disclosure provides for specific peptides from the Secreted Protein Acidic and Rich in Cysteine (SPARC) protein and the derived ionization characteristics of those peptides that are advantageous for quantifying SPARC 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. SPARC 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 SPARC peptides include those bearing phosphorylation of a tyrosine, threonine, serine, and/or other amino acid residues within the peptide sequence.Type: ApplicationFiled: June 21, 2012Publication date: March 21, 2013Inventors: David B. KRIZMAN, Todd Hembrough, Sheeno Thyparambil
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Publication number: 20130011408Abstract: 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.Type: ApplicationFiled: June 21, 2012Publication date: January 10, 2013Applicant: EXPRESSION PATHOLOGY, INC.Inventors: David B. Krizman, Todd Hembrough, Sheeno Thyparambil
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Publication number: 20120302650Abstract: 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.Type: ApplicationFiled: June 21, 2012Publication date: November 29, 2012Applicant: EXPRESSION PATHOLOGY, INC.Inventors: David B. Krizman, Todd Hembrough, Sheeno Thyparambil
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Publication number: 20120295990Abstract: 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.Type: ApplicationFiled: June 21, 2012Publication date: November 22, 2012Applicant: EXPRESSION PATHOLOGY, INCInventors: David B. KRIZMAN, Todd Hembrough, Sheeno Thyparambil
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Publication number: 20080234243Abstract: The compounds of the present invention can be used to inhibit formation of beta-amyloid protein. The present invention provides methods of preventing, delaying onset of, or treating diseases or conditions characterized or mediated by amyloidosis. In particular, the present invention is useful for preventing, delaying onset of, and treating Alzheimer's disease and related diseases causing dementia.Type: ApplicationFiled: January 31, 2008Publication date: September 25, 2008Inventors: Theresa M. LaVallee, Anthony M. Treston, Todd A. Hembrough
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Publication number: 20080090760Abstract: Compositions and methods effective in inhibiting abnormal or undesirable cell proliferation, particularly endothelial cell proliferation and angiogenesis related to neovascularization and tumor growth are provided. The compositions comprise peptide molecules, optionally containing one or more individual peptide chains covalently linked, and optionally modified with polyethylene glycol (PEG). The methods involve administering to a human or animal the composition described herein in a dosage sufficient to inhibit cell proliferation, particularly endothelial cell proliferation. The methods are useful for treating diseases and processes mediated by undesired and uncontrolled cell proliferation, such as cancer, particularly by inhibiting angiogenesis. Administration of the composition to a human or animal having prevascularized, metastasized tumors is useful for preventing the growth or expansion of such tumors.Type: ApplicationFiled: December 8, 2006Publication date: April 17, 2008Inventors: Todd Hembrough, Christopher Holmes, Qun Yin, Genet Zemede, Yvonne Angell, Brian Frederick, Caiding Xu
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Publication number: 20060142203Abstract: Compositions and methods comprising protein activated receptor antagonists are provided More particularly, the present invention relates to the use of proteins, peptides and biomolecules that bind to protein activated receptor 2, and inhibit the processes associated with the activation of that receptor. More specifically, the present invention provides novel compositions and methods for the treatment of disorders and diseases such as those associated with abnormal cellular proliferation, angiogenesis, inflammation and cancer.Type: ApplicationFiled: June 26, 2003Publication date: June 29, 2006Inventors: Todd Hembrough, Victor Pribluda
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Publication number: 20060063930Abstract: Compositions and methods comprising proteinase activated receptor antagonists are provided. More particularly, the present invention relates to the use of proteins, peptides and molecules that bind to proteinase activated receptor 2, and inhibit the processes associated with the activation of that receptor. More specifically, the present invention provides novel compositions and methods for the treatment of disorders and diseases such as those associated with abnormal cellular proliferation, angiogenesis, inflammation and cancer.Type: ApplicationFiled: August 19, 2005Publication date: March 23, 2006Inventors: Gregory Agoston, Todd Hembrough, Theresa LaVallee, Jamshed Shah, Lita Suwandi, Anthony Treston
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Publication number: 20060025329Abstract: Compositions and methods effective in inhibiting abnormal or undesirable cell proliferation, particularly endothelial cell proliferation and angiogenesis related to neovascularization and tumor growth are provided. The compositions comprise a naturally occurring or synthetic protein, peptide, or protein fragment containing all or an active portion of the C-terminal portion of proteinase inhibitors such as TFPI. The methods involve administering to a human or animal the composition described herein in a dosage sufficient to inhibit cell proliferation, particularly endothelial cell proliferation. The methods are useful for treating diseases and processes mediated by undesired and uncontrolled cell proliferation, such as cancer, particularly by inhibiting angiogenesis. Administration of the composition to a human or animal having prevascularized, metastasized tumors is useful for preventing the growth or expansion of such tumors.Type: ApplicationFiled: July 18, 2005Publication date: February 2, 2006Inventors: Todd Hembrough, Victor Pribluda, Adonia Papathanassiu, Shawn Green