Large Scale Proteomics Corporation

Large Scale Biology Corporation

Agilent Technologies, Inc.

Anderson Forschung Group LLC

Siscapa Assay Technologies, Invc.

Siscapa Assay Technologies, Inc.

N Leigh Anderson

Norman G Anderson

Jack E Goodman

James A Braatz

Rembert Pieper

Andrew McGrath

John Joseph Lennon

Samuel G Michael

L Eric Wallgren

Methods are provided for estimating the relative amounts of identifiable compartments, such as different types of cells or cell components, within a biological sample. The methods use mass spectrometric analysis to quantitate compartment-specific molecules and thereby allow calculation of the amount of each compartment that is present in a biological sample. The methods can, for example, provide a measurement of hematocrit from a dried blood sample.

Multipurpose mass spectrometric assay panels for peptides

Methods for interpretation of mass spectrometric tests for clinical biomarkers in which the amounts of internal standards are set to equal clinical evaluation thresholds, and preparations for adding stable isotope labeled peptide species to sample digests while minimizing losses and alterations in peptide stoichiometry.

Mass spectrometric assays for peptides

Methods are provided for estimating the relative amounts of identifiable compartments, such as different types of cells or cell components, within a biological sample. The methods use mass spectrometric analysis in quantitate compartment-specific molecules and thereby allow calculation of the amount of each compartment that is present in a biological sample. The methods can, for example, provide a measurement of hematocrit from a dried blood sample.

The instant invention provides an economical flow-through method for determining amount of target proteins in a sample. An antibody preparation (whether polyclonal or monoclonal, or any equivalent specific binding agent) is used to capture and thus enrich a specific monitor peptide (a specific peptide fragment of a protein to be quantitated in a proteolytic digest of a complex protein sample) and an internal standard peptide (the same chemical structure but including stable isotope labels). Upon elution into a suitable mass spectrometer, the natural (sample derived) and internal standard (isotope labeled) peptides are quantitated, and their measured abundance ratio used to calculate the abundance of the monitor peptide, and its parent protein, in the initial sample.

High sensitivity quantitation of peptides by mass spectrometry

Removal of abundant proteins from a sample enhances detection and resolution of less abundant proteins in the sample such as in two-dimensional gel electrophoresis. The removal is accomplished by immunosubtraction of several high abundance, interfering or contaminating proteins simultaneously.

Immunosubtraction method

Microarrays are prepared by using a separate fiber for each compound being used in the microarray. The fibers are bundled and sectioned to form a thin microarray that may be glued to a backing.

Microarrays and their manufacture by slicing

Data acquisition and cataloging are used to classify polypeptides into a reference index or database. The database can be used to identify previously unidentified samples. New polypeptides are characterized and added to the database.

Reference database

A method for separating microorganisms, especially infectious agents, from a mixture by two dimensional centrifugation on the basis of sedimentation rate and isopycnic banding density, for sedimenting such microorganisms through zones of immobilized reagents to which they are resistant, for detecting banded particles by light scatter or fluorescence using nucleic acid specific dyes, and for recovering the banded particles in very small volumes for characterization by mass spectrometry of viral protein subunits and intact viral particles, and by fluorescence flow cytometric determination of both nucleic acid mass and the masses of fragments produced by restriction enzymes. The method is based on the discovery that individual microorganisms, such as bacterial and viral species, are each physically relatively homogeneous, and are distinguishable in their biophysical properties from other biological particles, and from non-biological particles found in nature. The method is useful for distinguishing infections, for identifying known microorganisms, and for discovering and characterizing new microorganisms. The method provides very rapid identification of microorganisms, and hence allows a rational choice of therapy for identified infectious agents. A particularly useful application is in clinical trials of new antibiotics and antivirals, where it is essential to identify at the outset individuals infected with the targeted infectious agent.

Detection and characterization of microorganisms

An automated, computer controlled assembly is provided for continuously processing a large number of electrophoresis gels. The assembly includes a loading assembly for loading a gel onto a carrier, a gel staining assembly and a scanning and cutting assembly. The staining assembly and the scanning and cutting assembly each include a robotic arm that is able to capture a gel and transfer the gel to selected work stations and can transfer the gel between the respective robotic arms.

Automated electrophoresis gel manipulation apparatus

The microarrays of the present invention are prepared by using a separate fiber for each compound being used in the microarray. The fibers are bundled and sectioned to form a thin microarray that is glued to a backing.

Microarrays and their manufacture

Microarrays are prepared by using a separate fiber for each compound being used in the microarray. The fibers are bundled and sectioned to form a thin microarray that is glued to a backing.

Growing community of inventors

Washington, DC, United States of America

N Leigh Anderson