AnaSpec Introduces Labeled RGD Peptide for In Vivo Imaging
San Jose, CA, October 18, 2007 --(PR.com)-- Leveraging its dual expertise in peptides and detection reagents, AnaSpec has released c[RGDyK(HiLyte FluorTM 750)], a labeled RGD peptide that has produced significant imaging results in a recent in vivo research study.
Extracellular matrix proteins containing the Arg-Gly-Asp (RGD) motif, 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 conjugate, c[RGDyK(HiLyte FluorTM 750)], binds specifically to some tissues in organs that are known to be rich in integrin αvβ3 (see Figure 1).
In vivo testing of this HiLyte FluorTM 750-labeled was performed by the University of South Florida. The results were presented in a late-breaking poster at the 20th American Peptide Symposium.
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 (dyes, assay kits, & antibodies), and combinatorial chemistry.
For more information, visit www.anaspec.com
Reference:
Chen, X., P. Conti, and R. Moats, Cancer Res. 64, 8009 (2004).
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Extracellular matrix proteins containing the Arg-Gly-Asp (RGD) motif, 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 conjugate, c[RGDyK(HiLyte FluorTM 750)], binds specifically to some tissues in organs that are known to be rich in integrin αvβ3 (see Figure 1).
In vivo testing of this HiLyte FluorTM 750-labeled was performed by the University of South Florida. The results were presented in a late-breaking poster at the 20th American Peptide Symposium.
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 (dyes, assay kits, & antibodies), and combinatorial chemistry.
For more information, visit www.anaspec.com
Reference:
Chen, X., P. Conti, and R. Moats, Cancer Res. 64, 8009 (2004).
###
Contact
AnaSpec, Inc.
Ping Yang
408-452-5055
www.anaspec.com
Contact
Ping Yang
408-452-5055
www.anaspec.com
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