| Info. | Vol.6 - No.4 (2012.12.20) |
|---|---|
| Title | Analysis of PKC 棺-mediated tyrosinase phosphorylation using ProteoChip |
| Authors | Chan-Won Park1, Min A Kim2, Youngjin Choi1 & In-Cheol Kang1,2 |
| Institutions | 1BioChip Research Center, Hoseo University & Innopharmascreen
Inc., Asan 336-795, Korea 2Department of Biological Science, Hoseo University, Asan 336-795, Korea Correspondence and requests for materials should be addressed to I.-C. Kang ( ickang@hoseo.edu) |
| Abstract | Phosphorylation of tyrosinase is a major cellular event leading to production of melanin pigments. Protein kinase C 棺 (PKC 棺) is a specific enzyme involved in tyrosinase phosphorylation that has a cytoplasmic domain containing two serine residues regulating melanin production. In this study, we established a ProteoChip-based assay system to analyze protein phosphorylation by protein kinase C 棺 (PKC 棺). Human tyrosinase was used as a substrate immobilized on a ProteoChipTM and incubated with PKC 棺 to phosphorylate serine residues of the substrate. The immobilized substrate was recognized by a phospho-specific monoclonal antibody and Cy5-labeled secondary antibody. The level of phosphorylation was estimated from the fluorescence intensities of the spots. The inhibitory activity of PKC 棺 was successfully tested using this tyrosinase-PKC 棺 kinase assay chip for the identification of novel inhibitors. |
| Keyword | Tyrosinase, PKC 棺, ProteoChipTM, Screening |
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