AnaSpec, Inc. Introduces New PKD1 & PKD2 Antibodies

San Jose, CA – October 21, 2008 -- Protein kinase D (PKD), a serine/threonine kinase originally described as a novel PKC family member and termed PKC? (1), belongs to the calcium calmodulin superfamily of kinases (2-3). Three mammalian isoforms have so far been described - PKD1/PKC?, PKD2 and PKD3/PKC?; these isoforms show a high degree of homology, especially in their catalytic domain (4-5). PKDs are major targets for tumor promoting phorbol esters; they are activated via G protein-coupled receptors (GPCRs) and their activation is also dependent on PKC activation (5). PKDs have been implicated in numerous cellular functions, including signal transduction as well as cell survival, migration, differentiation, and proliferation (4-6). They are important regulators of secretory transport at the trans-golgi network (7). Of the three isoforms, PKD1 is the best characterized. It is involved in the regulation of Golgi function, cell proliferation and apoptosis (8) and it mediates oxidative stress signaling regulating cellular detoxification and survival (9). PKD2 has been found to phosphorylate histone H1 more efficiently than aldolase in vitro (10).

AnaSpec is pleased to announce the release of isoform specific PKD1 and PKD2 antibodies. These antibodies were raised using sequences from the C-terminus of PKD1 and PKD2. Anti-PKD1 only recognizes PKD1 and not PKD2 and PKD3. Anti-PKD2 only recognizes PKD2 and not PKD1 or PKD3.

About AnaSpec

AnaSpec is a leading provider of integrated proteomics solutions to the world’s largest biotech, pharmaceutical, and academic research institutions. With a vision for innovation through synergy, AnaSpec focuses on three core technologies: peptides, detection reagents, and combinatorial chemistry.

For more information visit www.anaspec.com

References

1. Johannes, FJ. et al. J. Biol. Chem. 269, 6140 (1994).

2. Manning, G. et al. Science 298, 1912 (2002).

3. Van Lint, J. et al. Trends Cell Biol. 12, 193 (2002).

4. Waldron, RT. et al. J. Biol. Chem. 276, 32606 (2001).

5. Auer, A. et al. Mol. Bio. Cell. 16, 4375 (2005).

6. Rozengurt, E. et al. J. Biol. Chem. 208, 13205 (2005).

7. Yeaman, C. et al. Nature Cell Biol. 6, 106 (2004).

8. Rykx, A. et al. FEBS Lett. 546, 81 (2003).

9. Döppler, H. & P. Storz, et al. J. Biol. Chem. 282, 31873 (2007).

10. Sturany, S. et al. J. Biol. Chem. 276, 3310 (2001).