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LABS AT NIBIB

Micro Analytical Immunochemistry

MICROANALYTICAL lab image
MICROANALYTICAL lab image

The Micro Analytical Immunochemistry Unit of the BEPS Shared Resource specializes in the following:

  • Micro-immunoaffinity capillary electrophoresis to quantify analyte concentrations in biological samples
  • Development of novel immunoassays for microliter and sub-microliter biological fluid and tissue samples
  • SELEX via capillary electrophoresis to generate aptamers with specificity for protein targets
  • Multianalyte ELISA arrays using QuansysTM imaging system
  • MALDI-TOF analysis of proteins, antibodies and other biological molecules
  • Characterization of biological molecule interactions using Surface Plasmon Resonance (SPR)
  • Trace metal analysis in biological samples, via Inductively-Coupled-Plasma Optical Emission Spectrometry (ICP-OES)

We are located in Building 13 on the NIH campus. 

This is an image of a multiplex ELISA array with 16 cytokines per well on a 96 well plate

 

This is an image of a micralyne double T chip staged on a Micralyne microchip capillary electrophoresis unit

The mission of the lab is to get as much information out of as little sample as possible. The technology is applicable to all biological samples, from serum and plasma, to cells and tissue. 

  • Develop novel immunoassays to quantitate analyte concentrations
  • Use immunoaffinity capillary electrophoresis to extract analytes from:
    • tissue samples
    • plasma and other biological fluids
    • cells and cell supernatant
  • Identify and quantify cytokines, chemokines, neuropeptides, hormones, and other analytes in microliter and sub-microliter samples
  • Use QuansysTM imaging system to screen for up to 16 cytokines from a single sample using a multiplex ELISA
  • Determine the mass of proteins, antibodies and other biological complexes using MALDI-TOF
  • Screen for high affinity aptamers to specific protein targets using CE-based SELEX
  • Characterize biological molecular interactions using Surface Plasmon Resonance (SPR)


Surface Plasmon Resonance (SPR) Technology 

Characterization of biological molecule interactions using Surface Plasmon Resonance (SPR) optical biosensor technology (Biacore3000)

This is an illustration of a surface plasmon resonance sensor chip containing carboxymethylated dextran attached to a gold surface

  • Interactions include, but are not limited to:
    • Protein-protein, protein-peptide, protein-small molecules, protein-whole cells
    • Nucleic acid-protein, nucleic acid-small molecules
    • Liposome-protein, liposome-small molecules
  • Information yield
    • Yes or no binding
    • Binding specificity
    • Binding affinity (KD - Thermodynamic constant of binding
    • Binding kinetics (kon, koff -kinetic constants of association and dissociation).


Trace Metal Analysis in biological samples (down to te ppb level), via ICP-OES

Selected Publications