Next-Generation C-Terminal Technology
HP Automated Protein Sequence Analysis
Newly developed chemical advances for the
automated C-terminal protein sequence analysis with the HP
sequencing system have been making significant contributions in
protein laboratories around the world.
Crucial Structural Information
HP recently introduced next-generation chemical
advances and critical applications solutions for
automated C-terminal protein sequence analysis.
The HP technology (Routine Method 2.0 for the
HP G1009A C-terminal protein sequencing system)
includes sequence analysis through any of the 20
common amino acid residues, high-sensitivity analysis
at the 100-pmole level, analysis of SDS gel samples,
and a fast and efficient sample throughput. These
capabilities combine to provide crucial protein-structural
information for bioscientists in industrial
and academic laboratories.
A Variety of Applications
The C-terminal sequence analysis
facilitated the detection and identification of a novel
biochemical modification observed for a class of recombinant
interleukin-6 protein molecules discovered by Dr. Richard Simpson
and colleagues at the Ludwig Institute for Cancer Research in
Melbourne, Australia. The recombinant proteins are expressed in
E. coli bacterial strains and exhibit a common C-terminal peptide
that has compelling biological implications.
Scientists at Glaxo Wellcome Research Laboratories,
Research Triangle Park, NC, obtained C-terminal
sequence information on a sample of phosphodiesterase
recovered from SDS gel electrophoresis in an examination
of protein processing. The results provided critical
information on the nature and extent of intracellular
C-terminal processing of the protein molecule.
The University of Michigan Protein Structure Facility, in
collaboration with the laboratory of Dr. Kotoku Kurachi of the
University of Michigan Medical School, used the HP C-terminal
protein sequencer to identify an anomalous processing site for
canine Factor IX. Factor IX is a essential component of the
blood-clotting system; functional defects in the protein lead to
hemophilia B.
These current applications are being applied to the
investigation of many important protein systems in
biochemistry and in the development and characterization
of protein therapeutics.
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