Cystatin C

Molecular cloning and gene expression analysis of cystatin C-like proteins in spinyhead croaker Collichthys lucidus

W. Song, Jiang, K. J., Zhang, F. Y., Zhao, M., Ma, L. B., Song, W., Jiang, K. J., Zhang, F. Y., Zhao, M., Ma, L. B., Song, W., Jiang, K. J., Zhang, F. Y., Zhao, M., and Ma, L. B., Molecular cloning and gene expression analysis of cystatin C-like proteins in spinyhead croaker Collichthys lucidus, vol. 15, p. -, 2016.

Cystatins are natural tight-binding reversible inhibitors of cysteine proteases. In this study, a cDNA library was constructed from Collichthys lucidus using the SMART technique. A complete cDNA sequence with high identity to the conserved sequence of the cystatin C gene was cloned from the library using EST analysis and rapid amplification of cDNA ends (RACE), then subjected to further investigation. The full-length cDNA of cystatin C from C.

Effect of codon optimization on expression levels of human cystatin C in Pichia pastoris

Y. M. Li, Li, D. J., Xu, X. J., Cui, M., Zhen, H. H., and Wang, Q., Effect of codon optimization on expression levels of human cystatin C in Pichia pastoris, vol. 13, pp. 4990-5000, 2014.

Human cystatin C (CysC) is a cysteine proteinase inhibitor with many potential applications. To facilitate further studies of the functions and applications of CysC, we improved the heterologous expression of CysC using a basic codon optimization method. In this study, we cloned the high-GC content wild-type sequence of the CysC gene and also designed a slightly AT-biased sequence, with codons optimized for expression in the Pichia pastoris GS115 strain.

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