AnaSpec Introduces New Selection of Cathelicidin Peptides

San Jose, CA, July 20, 2007 --(PR.com)-- Cathelicidins are cationic peptides that have broad-range antimicrobial activity.1 These peptides belong to the family of anti-microbial peptides which form part of the host’s important innate immunity mechanism.2 In humans, cathelicidins and defensins are expressed in immune cells and at epithelial surfaces.3-5 hCAP18, human cationic antimicrobial protein, with a MW of 18 kD, is the only cathelicidin gene found in humans.2 The N-terminus of this protein consists of a cathelin-like region (similar to the other members of the cathelicidin family) and a C-terminal termed LL-37.6-7 An amphipathic alpha-helical peptide, LL-37 plays an important role in the first line of defense against local infection and systemic invasion of pathogens at sites of inflammation and wounds. Cytotoxic to both bacterial and normal eukaryotic cells, LL-37 is significantly resistant to proteolytic degradation in solution.8-9
Offering one of the world’s largest collections of catalog peptides, AnaSpec is pleased to introduce a wide range of structurally diverse cathelicidin peptides, some of which have not been commercially available until now.
For more information, visit http://www.anaspec.com/products/promotions.asp?col=2&row=1

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. Established in 1993, AnaSpec's ISO9001:2000 certified headquarters and manufacturing facilities are located in San Jose, CA.

For more information, visit www.anaspec.com

References:
1. Zanetti, M. et al. J. Biol. Chem. 268, 522 (1993).
2. Lehrer, R. and T. Ganz. Curr. Opin. Immunol. 11, 23 (1999).
3. Ganz, T. Nat. Rev. Immunol. 3, 710 (2003).
4. Zanetti, M. J. Leukoc. Biol. 75, 39 (2004).
5. Chromek, M. et al. Nature Medicine 12, 636 (2006).
6. Zanetti, M. et al. FEBS Lett. 374, 1 (1995).
7. Sorensen, OE. et al. Blood 97, 3951 (2001).
8. Neville, F. et al. Biophys. J. 90, 1275 (2006)
9. Oren, Z., et al. Biochem. J. 341, 501(1999).
10. Zhao, C. et al. Antimicrob. Ag. Chemother. 45, 2695 (2001).
11. Lopez-Garcia, B. et al. J. Invest. Dermatol. 125, 108 (2005).
12. Termen, S. et al. Cell. Mol. Life Sci. 60, 536 (2003).
13. Saiman, L et al. Antimicrob. Ag. Chemother. 45, 2838 (2001).
14. Travis, S et al. Infect. Immun. 68, 2748 (2000).
15. Wu, M. and REW Hancock J. Biol. Chem. 274, 29 (1999).
16. Selsted, ME. et al. J. Biol. Chem. 267, 4292 (1992).
17. de Soultrait VR. et al. Curr. Med. Chem. 10, 1765 (2003).

###