Badri Prasad Maliwal

age ~74

from Fort Worth, TX

Also known as:
  • Badri P Maliwal
  • Maliwal Badri
  • L Badri

Badri Maliwal Phones & Addresses

  • Fort Worth, TX
  • San Francisco, CA
  • Mountain View, CA
  • Euless, TX
  • 1 Franklin St, Baltimore, MD 21201 • 4102340663
  • 2818 Saint Paul St, Baltimore, MD 21218 • 4108898884

Work

  • Company:
    Tcu
    Nov 2013 to Dec 2014
  • Position:
    Consultant

Education

  • Degree:
    Doctorates, Doctor of Philosophy
  • Specialities:
    Biochemistry

Skills

Fluorescence • Biochemistry • Spectroscopy • Protein Chemistry • Microscopy • Life Sciences • Cell Biology • Science • Bioanalytical Chemistry • Assay Development • Biophysics • Ligand Binding • Cell • Confocal Microscopy • Biotechnology • Research • Fluorescence Microscopy

Interests

Civil Rights and Social Action

Industries

Research

Resumes

Badri Maliwal Photo 1

Badri Maliwal

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Location:
Atlanta, GA
Industry:
Research
Work:
Tcu Nov 2013 - Dec 2014
Consultant

University of North Texas Apr 2010 - Aug 2014
Visiting Research Assistant Professor, on and Off

University of Maryland Medical School 1981 - 2002
Research Associate and Research Assistant Professor

University of Delaware Jun 1986 - May 1987
Visiting Research Scientist

North Carolina State University Oct 1978 - Aug 1981
Post-Doc
Skills:
Fluorescence
Biochemistry
Spectroscopy
Protein Chemistry
Microscopy
Life Sciences
Cell Biology
Science
Bioanalytical Chemistry
Assay Development
Biophysics
Ligand Binding
Cell
Confocal Microscopy
Biotechnology
Research
Fluorescence Microscopy
Interests:
Civil Rights and Social Action

Us Patents

  • Determination Of Metal Ions In Solution By Photoluminescence Anisotropy

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  • US Patent:
    7842491, Nov 30, 2010
  • Filed:
    Nov 8, 2004
  • Appl. No.:
    10/982956
  • Inventors:
    Richard B. Thompson - Baltimore MD, US
    Daniel Elbaum - Newton MA, US
    Vincent L. Feliccia - Arnold MD, US
    David Christianson - Media PA, US
    Marcia W. Patchan - Columbia MD, US
    Zhengfang Ge - Rockville MD, US
    Badri P. Maliwal - San Francisco CA, US
  • International Classification:
    C12Q 1/34
    C12Q 1/00
    G01N 21/00
    G01N 33/20
  • US Classification:
    435232, 436 81, 435975, 435 18
  • Abstract:
    The invention relates to compositions and kits for homogeneous fluorescence polarization (anisotropy) assays for detecting and quantifying metal ions in solution. Metal-dependent binding of a fluorescent ligand to an unlabeled macromolecule effects a measurable change in anisotropy as will the binding of metal ions to a fluorescent labeled macromolecule. Binding of the fluorescent ligand to the unlabeled macromolecule is metal dependent with the change in anisotropy being proportional to the concentration of bound metal ions. Conversely, if the fluorescent label is first conjugated to a macromolecule and the macromolecule is subsequently stripped of metal ion, it may then be used to signal binding of metal ions. The covalently bound fluorescent label exhibits changes in anisotropy proportional to the concentration of bound metal ions. Kits comprise a fluorescent molecule and a macromolecule.
  • Determination Of Metal Ions In Solution By Photoluminescence Anisotropy

    view source
  • US Patent:
    20020055091, May 9, 2002
  • Filed:
    Aug 31, 2001
  • Appl. No.:
    09/942708
  • Inventors:
    Richard Thompson - Baltimore MD, US
    Daniel Elbaum - Newton MA, US
    Vincent Feliccia - Arnold MD, US
    David Christianson - Media PA, US
    Marcia Patchan - Columbia MD, US
    Zhengfang Ge - Burlington MA, US
    Badri Maliwal - Baltimore MD, US
  • Assignee:
    University of Pennsylvania
  • International Classification:
    G01N033/20
  • US Classification:
    435/004000, 436/074000, 436/079000, 436/080000, 436/081000, 436/083000, 436/084000, 436/166000, 436/172000
  • Abstract:
    Homogeneous fluorescence polarization (anisotropy) assays for detecting and quantifying metal ions in solution, based the metal-dependent binding of a fluorescent ligand to an unlabeled macromolecule, or the binding of a metal ion to a fluorescent labeled macromolecule. The metal-dependent binding of a fluorescent ligand to an unlabeled macromolecule (metallo-macromolecule) effects a measurable change in anisotropy as will the binding of metal ions to a fluorescent labeled macromolecule. Binding of the fluorescent ligand to the unlabeled macromolecule is metal dependent with the change in anisotropy being proportional to the concentration of bound metal ions. No binding of the fluorescent ligand to the macromolecule occurs in the absence of metal ions. Conversely, if the fluorescent label is first conjugated to a metallo-macromolecule and the metallo-macromolecule is subsequently stripped of its metal ion, it may then be used to transduce the binding of metal ions. Transduction is provided wherein the covalently bound fluorescent label exhibits changes in anisotropy proportional to the concentration of bound metal ions. In all methods, the change in anisotropy may be simply related to the metal ion concentration of the test solution.
  • Determination And Quantification Of Saccharides By Luminescence Lifetimes And Energy Transfer

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  • US Patent:
    52468674, Sep 21, 1993
  • Filed:
    Jan 17, 1992
  • Appl. No.:
    7/822382
  • Inventors:
    Joseph R. Lakowicz - Columbia MD
    Badri P. Maliwal - Baltimore MD
    Peter A. Koen - Hillsborough NJ
  • Assignee:
    University of Maryland at Baltimore - MD
    Becton Dickinson & Company - NJ
  • International Classification:
    G01N 2164
    G01N 3366
  • US Classification:
    436 95
  • Abstract:
    A method for measuring the concentration of a saccharide, conjugated saccharide or polysaccharide of interest using luminescent lifetimes and energy transfer in which an energy transfer donor-acceptor pair is added to a sample to be analyzed, the donor of the donor-acceptor pair being photoluminescent. The acceptor is bound to a carrier, while the donor and any saccharide, conjugated saccharide or polysaccharide of interest present in the sample compete for binding sites on the carrier. The sample is irradiated and the resultant emission detected. Energy transfer occurs between the donors and the acceptors, which produces a detectable lifetime change of the fIuorescence of the donor. The lifetime change is reduced or even eliminated by the competitive binding of a saccharide, conjugated saccharide or polysaccharide of interest to the donor. By measuring the apparent luminescent lifetime, the amount of a saccharide, conjugated saccharide or polysaccharide of interest in the sample can be determined.
  • Determination Of Metal Ions In Solution By Photoluminescence Anisotropy

    view source
  • US Patent:
    62845446, Sep 4, 2001
  • Filed:
    Apr 30, 1998
  • Appl. No.:
    9/071351
  • Inventors:
    Richard B. Thompson - Baltimore MD
    Daniel Elbaum - Newton MA
    Vincent L. Feliccia - Arnold MD
    David Christianson - Media PA
    Marcia W. Patchan - Columbia MD
    Zhengfang Ge - Burlington MA
    Badri P. Maliwal - Baltimore MD
  • Assignee:
    University of Pennsylvania - Philadelphia PA
    University of Maryland - Baltimore MD
  • International Classification:
    G01N 3320
  • US Classification:
    436 73
  • Abstract:
    Homogeneous fluorescence polarization (anisotropy) assays for detecting and quantifying metal ions in solution, based the metal-dependent binding of a fluorescent ligand to an unlabeled macromolecule, or the binding of a metal ion to a fluorescent labeled macromolecule. The metal-dependent binding of a fluorescent ligand to an unlabeled macromolecule (metallo-macromolecule) effects a measurable change in anisotropy as will the binding of metal ions to a fluorescent labeled macromolecule. Binding of the fluorescent ligand to the unlabeled macromolecule is metal dependent with the change in anisotropy being proportional to the concentration of bound metal ions. No binding of the fluorescent ligand to the macromolecule occurs in the absence of metal ions. Conversely, if the fluorescent label is first conjugated to a metallo-macromolecule and the metallo-macromolecule is subsequently stripped of its metal ion, it may then be used to transduce the binding of metal ions. Transduction is provided wherein the covalently bound fluorescent label exhibits changes in anisotropy proportional to the concentration of bound metal ions.
  • Photoluminescent Sensors Of Chemical Analytes

    view source
  • US Patent:
    61972584, Mar 6, 2001
  • Filed:
    Mar 19, 1999
  • Appl. No.:
    9/273303
  • Inventors:
    Richard B. Thompson - Baltimore MD
    Vincent L. Feliccia - Arnold MD
    Badri P. Maliwal - Baltimore MD
    Carol A. Fierke - Durham NC
  • Assignee:
    University of Maryland, Baltimore - Baltimore MD
  • International Classification:
    G01N 3320
    C12Q 100
  • US Classification:
    422 8207
  • Abstract:
    The invention described in detail herein relates to the detection, determination, and quantitation of certain ions and small molecules in solution. The invention specifically relates to improvements in the area of photoluminescent sensors for use in a detection scheme involving the alteration of a photoluminescent label or moiety attached to or associated with an analyte binding macromolecule. One may use the changes in photoluminescence lifetime, changes in ratios of photoluminescence intensity or changes in photoluminescence polarization (anisotropy) to determine the analyte. The photoluminescence change measured correlates to the concentration of the ion or molecule in solution.
  • Fluorescent Energy Transfer Immunoassay

    view source
  • US Patent:
    56311699, May 20, 1997
  • Filed:
    Jan 19, 1994
  • Appl. No.:
    8/183238
  • Inventors:
    Joseph R. Lakowicz - Columbia MD
    Badri P. Maliwal - Baltimore MD
    Richard Thompson - Baltimore MD
    Alvydas Ozinskas - Dayton MD
  • International Classification:
    G01N 33533
  • US Classification:
    436537
  • Abstract:
    A fluorometric luminescence immunoassay method includes forming a sample by exposing a first immune reaction reactant to a second immune reaction reactant capable of reacting with the first reactant, one of the first and second immune reaction reactants being labelled with a photoluminescent energy transfer donor and the other being labelled with a photoluminescent energy transfer acceptor complementary to the photoluminescent donor. At least the photoluminescent donor has the property of photoluminescence, and the photoluminescent donor and acceptor are chosen so that when the first immune reaction reactant reacts with the second immune reaction reactant, the donor and the acceptor are capable of interacting to produce a detectable luminescence lifetime change. The sample is excited with radiation, and the resulting emission is detected. The apparent luminescent lifetime is then calculated to determine the presence of a reaction product of the first and second immune reaction reactants.
  • Fret Based Multiplex Probes

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  • US Patent:
    20140274797, Sep 18, 2014
  • Filed:
    Mar 12, 2014
  • Appl. No.:
    14/206738
  • Inventors:
    - Fort Worth TX, US
    Rafal Fudala - Fort Worth TX, US
    Badri P. Maliwal - Fort Worth TX, US
  • International Classification:
    C12Q 1/37
  • US Classification:
    506 11, 530300
  • Abstract:
    The present invention includes compositions and methods for fluorescence-based multiplex probe to simultaneously detect one or more enzymatic activities comprising: a first enzymatic target having a first end and a second end, wherein the first end of the first enzymatic target is attached to a central body and the second end of the first enzymatic target is attached to a first fluorophore; a second enzymatic target having a first end and a second end, wherein the first end of the second enzymatic target is attached to the central body and the second end of the second enzymatic target is attached to a third fluorophore; wherein the central body comprises at least one second fluorophore; wherein the first enzymatic target comprises a specific cleavage site of a first enzyme that cleaves the first enzymatic target; and wherein the second enzymatic target comprises a specific cleavage site of a second enzyme.

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