Cloning

Molecular cloning and expression analysis of heat shock protein 20 (HSP20) from the pearl oyster Pinctada martensii

Q. N. Lei, Wu, Y. Y., Liang, H. Y., Wang, Z. X., Zheng, Z., Deng, Y. W., Lei, Q. N., Wu, Y. Y., Liang, H. Y., Wang, Z. X., Zheng, Z., and Deng, Y. W., Molecular cloning and expression analysis of heat shock protein 20 (HSP20) from the pearl oyster Pinctada martensii, vol. 15, p. -, 2016.

Small heat shock proteins (HSPs) are molecular chaperones with ATP-independent properties. They are involved in a variety of physiological and stress processes. In this study, the full-length HSP 20 (HSP20) from Pinctada martensii, designated as PmHSP20, was obtained from hemocytes using rapid amplification of cDNA ends technology. The PmHSP20 cDNA was 952 bp in length, containing an open reading frame of 534 bp that encoded 177-amino acid residues, with an isoelectric point of 5.86 and molecular weight of 20.24 kDa.

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