AnaSpec Presents Late-Breaking In Vivo Imaging Poster at American Peptide Symposium
San Jose, CA, July 13, 2007 --(PR.com)-- At the 2007 annual conference of the American Peptide Society, AnaSpec presented a “late-breaking” technical poster that described in vivo imaging using a tissue-specific near infrared fluorescent peptide conjugate.
Extracellular matrix proteins that contain the Arg-Gly-Asp (RGD) sequence, and integrin receptors which bind this sequence, constitute a major recognition system for cell migration and adhesion processes. In fibronectins and other proteins, the RGD binding sequence is found at the apex of a loop; such conformation has been found to allow for high affinity selectivity to integrin receptors. Cyclic peptides have been shown to be more stable than linear peptides; in the case of RGD cyclic peptide c(RGDyK), its structure also confers increased affinity and selectivity for integrin αvβ3 both in cell culture and in living subjects.
The AnaSpec poster described in vivo testing of an RGD cyclic peptide labeled with a proprietary near infrared fluorescent dye, HiLyte FluorTM 750-labeled RGD peptide, c[RGDyK(HiLyte FluorTM 750)], with excitation and emission wavelengths at 750 and 780 nm. Results demonstrated that in an animal model, this conjugate bound specifically to some tissues in organs that are known to be rich in integrin αvβ3.
For more information visit www.anaspec.com
Company Info
AnaSpec, Inc. is a leading provider of integrated proteomics solutions to pharmaceutical, biotech, and academic research institutions throughout the world. With a vision for innovation through synergy, AnaSpec focuses on three core technologies: peptides, detection reagents, and combinatorial chemistry. Established in 1993, AnaSpec's headquarters and manufacturing facilities are located in San Jose, CA.
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Extracellular matrix proteins that contain the Arg-Gly-Asp (RGD) sequence, and integrin receptors which bind this sequence, constitute a major recognition system for cell migration and adhesion processes. In fibronectins and other proteins, the RGD binding sequence is found at the apex of a loop; such conformation has been found to allow for high affinity selectivity to integrin receptors. Cyclic peptides have been shown to be more stable than linear peptides; in the case of RGD cyclic peptide c(RGDyK), its structure also confers increased affinity and selectivity for integrin αvβ3 both in cell culture and in living subjects.
The AnaSpec poster described in vivo testing of an RGD cyclic peptide labeled with a proprietary near infrared fluorescent dye, HiLyte FluorTM 750-labeled RGD peptide, c[RGDyK(HiLyte FluorTM 750)], with excitation and emission wavelengths at 750 and 780 nm. Results demonstrated that in an animal model, this conjugate bound specifically to some tissues in organs that are known to be rich in integrin αvβ3.
For more information visit www.anaspec.com
Company Info
AnaSpec, Inc. is a leading provider of integrated proteomics solutions to pharmaceutical, biotech, and academic research institutions throughout the world. With a vision for innovation through synergy, AnaSpec focuses on three core technologies: peptides, detection reagents, and combinatorial chemistry. Established in 1993, AnaSpec's headquarters and manufacturing facilities are located in San Jose, CA.
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Contact
AnaSpec, Inc.
Ping Yang
408-452-5055
www.anaspec.com
Contact
Ping Yang
408-452-5055
www.anaspec.com
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