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Akira Komoriya Phones & Addresses

  • 12950 Dalyn Dr, Potomac, MD 20854 (301) 926-0428
  • 10605 Pine Haven Ter, Rockville, MD 20852 (301) 984-2519
  • Kensington, MD
  • Gaithersburg, MD
  • Miami, FL

Work

Company: Oncoimmunin, inc. Apr 1994 Position: Owner

Education

Degree: Doctorates, Doctor of Philosophy School / High School: Duke University Graduate School 1971 to 1977 Specialities: Chemistry

Skills

Life Sciences • Biochemistry • Molecular Biology • Biotechnology • Technology Transfer • Immunology • R&D • Pharmaceutical Industry • Drug Discovery • Science

Languages

Japanese

Interests

Cooking • Electronics • Gardening • Environment • Home Improvement • Reading • Crafts • Science and Technology • Gourmet Cooking • Human Rights • Arts and Culture • Home Decoration • Health

Industries

Biotechnology

Resumes

Resumes

Akira Komoriya Photo 1

Owner

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Location:
12950 Dalyn Dr, Potomac, MD 20854
Industry:
Biotechnology
Work:
Oncoimmunin, Inc.
Owner

Fda Cber 1987 - 1994
Senior Staff Fellow In Cytokine Biology, Head of Lab of Cell Biology, Reviewed Aids Test Kits

Rorer Biotech May 1984 - May 1988
Principal Investigator

Johns Hopkins University Sep 1983 - May 1984
Associate Research Scientist

Nci Nih 1980 - 1983
Senior Staff Fellow
Education:
Duke University Graduate School 1971 - 1977
Doctorates, Doctor of Philosophy, Chemistry
Franklin & Marshall College 1968 - 1971
Bachelors, Bachelor of Arts, Chemistry
Skills:
Life Sciences
Biochemistry
Molecular Biology
Biotechnology
Technology Transfer
Immunology
R&D
Pharmaceutical Industry
Drug Discovery
Science
Interests:
Cooking
Electronics
Gardening
Environment
Home Improvement
Reading
Crafts
Science and Technology
Gourmet Cooking
Human Rights
Arts and Culture
Home Decoration
Health
Languages:
Japanese

Publications

Us Patents

Homo-Doubly Labeled Compositions For The Detection Of Enzyme Activity In Biological Samples

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US Patent:
6893868, May 17, 2005
Filed:
Dec 22, 2000
Appl. No.:
09/747287
Inventors:
Beverly Packard - Rockville MD, US
Akira Komoriya - Rockville MD, US
Assignee:
Onco Immunin, Inc. - Gaithersburg MD
International Classification:
C12N005/00
C12Q001/37
A61K038/00
US Classification:
435325, 435 23, 435 772, 436172, 514 2, 530300
Abstract:
The present invention provides for novel reagents whose fluorescence changes upon cleavage or a change in conformation of a backbone. The reagents comprise a backbone (e. g. nucleic acid, polypeptide, etc. ) joining two fluorophores of the same species whereby the fluorophores form an H-dimer resulting in quenching of the fluorescence of the fluorophores. When the backbone is cleaved or changes conformation, the fluorophores are separated, no longer forming an H-type dimer, and are de-quenched thereby providing a detectable signal. The use of a single fluorophore rather than an “acceptor-donor” fluoresecence resonance energy transfer system offers synthesis and performance advantages.

Compositions For The Detection Of Enzyme Activity In Biological Samples And Methods Of Use Thereof

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US Patent:
6936687, Aug 30, 2005
Filed:
Sep 10, 1999
Appl. No.:
09/394019
Inventors:
Akira Komoriya - Rockville MD, US
Beverly S. Packard - Rockville MD, US
Assignee:
Onco Immunin, Inc. - Kensington MD
International Classification:
A61K038/00
C12Q001/37
US Classification:
530300, 530324, 530326, 514 2, 514 13, 435 23, 435 24, 435 772
Abstract:
The present invention provides for novel reagents whose fluorescence increases in the presence of particular proteases. The reagents comprise a characteristically folded peptide backbone each end of which is conjugated to a fluorophore. When the folded peptide is cleaved, as by digestion with a protease, the fluorophores provide a high intensity fluorescent signal at a visible wavelength. Because of their high fluorescence signal in the visible wavelengths, these protease indicators are particularly well suited for detection of protease activity in biological samples, in particular in frozen tissue sections. Thus this invention also provides for methods of detecting protease activity in situ in frozen sections.

Compositions For The Detection Of Enzyme Activity In Biological Samples And Methods Of Use Thereof

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US Patent:
7312302, Dec 25, 2007
Filed:
Jun 4, 2001
Appl. No.:
09/874350
Inventors:
Beverly S. Packard - Potomac MD, US
Akira Komoriya - Potomac MD, US
Assignee:
Oncolmmunin, Inc. - Gaithersburg MD
International Classification:
C12Q 1/37
C07K 7/00
US Classification:
530300, 530324, 530326, 514 2, 514 13, 435 23, 435 24, 435 772
Abstract:
The present invention provides for novel reagents whose fluorescence increases in the presence of particular proteases. The reagents comprise a characteristically folded peptide backbone conjugated to two fluorophores such that the fluorophores are located opposite sides of a cleavage site. When the folded peptide is cleaved, as by digestion with a protease, the fluorophores provide a high intensity fluorescent signal at a visible wavelength. Because of their high specificity and their high fluorescence signal in the visible wavelengths, these protease indicators are particularly well suited for detection of protease activity in biological samples, in particular in frozen tissue sections. Thus this invention also provides for methods of detecting protease activity in situ in frozen sections.

Homo-Doubly Labeled Compositions For The Detection Of Enzyme Activity In Biological Samples

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US Patent:
7541143, Jun 2, 2009
Filed:
Dec 15, 2004
Appl. No.:
11/015864
Inventors:
Beverly Packard - Rockville MD, US
Akira Komoriya - Rockville MD, US
Assignee:
OnCoimmunin, Inc. - Gaithersburg MD
International Classification:
C12Q 1/68
C12N 5/00
US Classification:
435 6, 435325, 435 772, 536 231, 530300
Abstract:
The present invention provides for novel reagents whose fluorescence changes upon cleavage or a change in conformation of a backbone. The reagents comprise a backbone (e. g. nucleic acid, polypeptide, etc. ) joining two fluorophores of the same species whereby the fluorophores form an H-dimer resulting in quenching of the fluorescence of the fluorophores. When the backbone is cleaved or changes conformation, the fluorophores are separated, no longer forming an H-type dimer, and are de-quenched thereby providing a detectable signal. The use of a single fluorophore rather than an “acceptor-donor” fluoresecence resonance energy transfer system offers synthesis and performance advantages.

Compositions For The Detection Of Enzyme Activity In Biological Samples And Methods Of Use Thereof

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US Patent:
7879574, Feb 1, 2011
Filed:
Nov 16, 2007
Appl. No.:
11/941766
Inventors:
Beverly S. Packard - Potomac MD, US
Akira Komoriya - Potomac MD, US
Assignee:
Oncoimmunin, Inc. - Gaithersburg MD
International Classification:
C07K 7/00
C12Q 1/37
US Classification:
435 772, 530300, 530324, 530326, 514 2, 514 13, 435 23, 435 24
Abstract:
The present invention provides for novel reagents whose fluorescence increases in the presence of particular proteases. The reagents comprise a characteristically folded peptide backbone conjugated to two fluorophores such that the fluorophores are located opposite sides of a cleavage site. When the folded peptide is cleaved, as by digestion with a protease, the fluorophores provide a high intensity fluorescent signal at a visible wavelength. Because of their high specificity and their high fluorescence signal in the visible wavelengths, these protease indicators are particularly well suited for detection of protease activity in biological samples, in particular in frozen tissue sections. Thus this invention also provides for methods of detecting protease activity in situ in frozen sections.

Visualization And Quantitation Of Cellular Cytotoxicity Using Cell-Permeable Fluorogenic Protease Substrates And Caspase Activity Indicator Markers

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US Patent:
7927871, Apr 19, 2011
Filed:
Jan 30, 2007
Appl. No.:
11/669080
Inventors:
Beverly Packard - Potomac MD, US
Akira Komoriya - Rockville MD, US
Assignee:
Oncoimmunin, Inc. - Gaithersburg MD
International Classification:
C12N 5/00
C12Q 1/37
G01N 33/53
US Classification:
435325, 435 772, 435 23
Abstract:
This invention provides a non-radioactive assay to monitor and quantify the target-cell killing activities mediated by cytotoxic T lymphocytes (CTLs). This assay is predicated on the discovery that apoptosis pathway activation and, in particular, granzyme B activity, provides a measure of cytotoxic effector cell activity. In one embodiment, measurement of CTL-induced granzyme B activation in target cells is achieved through detection of the specific cleavage of fluorogenic granzyme B substrates. This assay reliably detects antigen-specific CTL killing of target cells, and provides a more sensitive, more informative and safer alternative to the standard Cr-release assay most often used to quantify CTL responses. The assay can be used to study CTL-mediated killing of primary host target cells of different cell lineages, and enables the study of antigen-specific cellular immune responses in real time at the single-cell level. As such, the assay can provide a valuable tool for studies of infectious disease pathogenesis and development of new vaccines and immunotherapies.

Visualization And Quantitiation Of Cellular Cytotoxicity Using Cell-Permeable Fluorogenic Protease Substrates And Caspase Activity Indicator Markers

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US Patent:
20030211548, Nov 13, 2003
Filed:
Jan 28, 2003
Appl. No.:
10/353791
Inventors:
Beverly Packard - Rockville MD, US
Martin Brown - Germantown MD, US
Mark Feinberg - Atlanta GA, US
Luzheng Liu - Brookline MA, US
Guido Silvestri - Decatur GA, US
Ann Chahroudi - Atlanta GA, US
Akira Komoriya - Rockville MD, US
Assignee:
Oncolmmunin, Inc.
International Classification:
C12Q001/70
G01N033/53
G01N033/567
C12Q001/37
US Classification:
435/007200, 435/023000, 435/005000
Abstract:
This invention provides a non-radioactive assay to monitor and quantify the target-cell killing activities mediated by cytotoxic T lymphocytes (CTLs). This assay is predicated on the discovery that apoptosis pathway activation and, in particular, caspase activity, provides a measure of cytotoxic effector cell activity. In one embodiment, measurement of CTL-induced caspase activation in target cells is achieved through detection of the specific cleavage of fluorogenic caspase substrates. This assay reliably detects antigen-specific CTL killing of target cells, and provides a more sensitive, more informative and safer alternative to the standard Cr-release assay most often used to quantify CTL responses. The assay can be used to study CTL-mediated killing of primary host target cells of different cell lineages, and enables the study of antigen-specific cellular immune responses in real time at the single-cell level. As such, the assay can provide a valuable tool for studies of infectious disease pathogenesis and development of new vaccines and immunotherapies.

Visualization And Quantitiation Of Cellular Cytotoxicity Using Cell-Permeable Fluorogenic Protease Substrates And Caspase Activity Indicator Markers

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US Patent:
20090263830, Oct 22, 2009
Filed:
Mar 3, 2009
Appl. No.:
12/396736
Inventors:
BEVERLY PACKARD - Potomac MD, US
MARTIN J. BROWN - Germantown MD, US
MARK FEINBERG - Atlanta GA, US
LUZHENG LIU - Brookline MA, US
GUIDO SILVESTRI - Decatur GA, US
ANN CHAHROUDI - Atlanta GA, US
AKIRA KOMORIYA - Potomac MD, US
Assignee:
Oncoimmunin, Inc. - Gaithersburg MD
International Classification:
G01N 33/53
C12Q 1/37
C12Q 1/02
US Classification:
435 74, 435 23, 435 29
Abstract:
This invention provides a non-radioactive assay to monitor and quantify the target-cell killing activities mediated by cytotoxic T lymphocytes (CTLs). This assay is predicated on the discovery that apoptosis pathway activation and, in particular, caspase activity, provides a measure of cytotoxic effector cell activity. In one embodiment, measurement of CTL-induced caspase activation in target cells is achieved through detection of the specific cleavage of fluorogenic caspase substrates. This assay reliably detects antigen-specific CTL killing of target cells, and provides a more sensitive, more informative and safer alternative to the standard Cr-release assay most often used to quantify CTL responses. The assay can be used to study CTL-mediated killing of primary host target cells of different cell lineages, and enables the study of antigen-specific cellular immune responses in real time at the single-cell level. As such, the assay can provide a valuable tool for studies of infectious disease pathogenesis and development of new vaccines and immunotherapies.
Akira K Komoriya from Potomac, MD, age ~76 Get Report