c[RGDyK(HiLyte™ Fluor 750)]- In Vivo Imaging


Leveraging its dual expertise in peptides and detection reagents, AnaSpec is pleased to announce the release of c[RGDyK(HiLyte™ Fluor 750)], a labeled RGD peptide that has produced valuable imaging 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™ Fluor 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 peptide labeled with an AnaSpec proprietary near infrared fluorescent dye, HiLyte™ Fluor750-labeled RGD peptide, c[RGDyK(HiLyte™ Fluor 750)], Ex/Em = 750/780 nm, was performed by the University of South Florida. The results were presented in a late-breaking poster at the 20th American Peptide Symposium.

Product

Size

Catalog #

Cyclo[-RGDyK(HiLyte™ Fluor 750)] NEW

1 mg

62333-1

Cyclo[-RGDyK(HiLyte™ Fluor 750)] NEW

0.1 mg

62333-01


Figure 1. In vivo fluorescent imaging of rat injected with 20 nmol c[RGDyK(HiLyte™ Fluor 750)] conjugate 3 hours post injection.

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Reference:
Chen, X., P. Conti, and R. Moats, Cancer Res. 64, 8009 (2004).