Article ID | Journal | Published Year | Pages | File Type |
---|---|---|---|---|
2432213 | Fish & Shellfish Immunology | 2011 | 8 Pages |
Abstract
Heat shock protein 90 (HSP90) is a highly conserved and multi-functional molecular chaperone that plays an essential role in both cellular metabolism and stress response. Here, we report the cloning of the HSP90 homologue in Crassostrea hongkongensis (ChHSP90) through SSH in combination with RACE from cDNA of haemocytes. The full-length cDNA of ChHSP90 is 2459 bp in length, consisting of a 3′, 5′-untranslated region (UTR) and an open reading frame of 2169 bp encoding 722 amino acids. The identity analysis of the amino acid sequence of HSP90 revealed that ChHSP90 is hi
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Authors
Dingkun Fu, Jinhui Chen, Yang Zhang, Ziniu Yu,