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Protein domains are small structurally independent units that are part of a single amino acid chain.  Although these domains are often structurally independent, they may rely on synergistic effects to perform their functions as part of a larger protein. Protein domains may be conserved within the same organism, as well as across different organisms.
A limited set of protein domains often duplicate and recombine during evolution. These domains can be organized in different combinations to...
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Analysis of Histone Antibody Specificity with Peptide Microarrays
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SH2 Domain Histochemistry.

Sophia Buhs1, Peter Nollau2

  • 1Research Institute Children's Cancer Center and Department of Pediatric Hematology and Oncology, University Medical Center Hamburg-Eppendorf, Martinistrasse 52, Building N63, 2nd Floor, 20251, Hamburg, Germany.

Methods in Molecular Biology (Clifton, N.J.)
|January 17, 2017
PubMed
Summary
This summary is machine-generated.

SH2 profiling now analyzes tyrosine phosphorylation in fixed tissues, preserving spatial details lost in protein extracts. This method uses SH2 domains for analyzing phosphorylation in routine pathology samples.

Keywords:
CancerHistochemistryPhosphotyrosineSH2 domainSignal amplificationSignal transductionSrc-homology 2Tyrosine phosphorylation

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Area of Science:

  • Biochemistry
  • Cell Biology
  • Molecular Biology

Background:

  • Tyrosine phosphorylation is a critical posttranslational modification in cell signaling.
  • Characterizing tyrosine phosphorylation patterns is vital for understanding cellular states.
  • SH2 domains specifically recognize tyrosine phosphorylated proteins.

Purpose of the Study:

  • To develop a novel SH2 domain-based method for analyzing tyrosine phosphorylation in fixed tissues.
  • To overcome the limitations of existing SH2 profiling methods that lose spatial information.
  • To enable differential characterization of tyrosine phosphorylation in formaldehyde-fixed and paraffin-embedded tissues.

Main Methods:

  • Utilized the specific binding properties of endogenous SH2 domains.
  • Adapted SH2 profiling for formaldehyde-fixed and paraffin-embedded tissue samples.
  • Developed a strategy for differential analysis of tyrosine phosphorylation states.

Main Results:

  • Demonstrated the feasibility of analyzing tyrosine phosphorylation in fixed tissues using SH2 domains.
  • Showcased the ability to retain information on spatial distribution and intensity.
  • Validated the approach for routine pathology laboratory conditions.

Conclusions:

  • SH2 domains are valuable tools for analyzing tyrosine phosphorylation in fixed tissues.
  • The novel strategy allows for differential characterization of phosphorylation states in primary tissues.
  • This method enhances the utility of SH2 profiling for pathological analysis.