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Updated: Feb 28, 2026

Pull-down of Calmodulin-binding Proteins
Published on: January 23, 2012
Characterization and function of a novel calmodulin-like protein from crayfish Procambarus clarkii
Baojian Zhu1, Yingying Yu1, Jin Gao1
1College of Life Sciences, Anhui Agricultural University, Hefei 230036, China.
Abstract:
Calmodulin plays an important role in calcium-dependent signal transduction pathways. In this experiment, a novel calmodulin-like gene (Pc-CaM-L) was identified in the crayfish Procambarus clarkii; it encodes a polypeptide of 145 amino acids. Quantitative real-time PCR analysis revealed that Pc-CaM-L was expressed in all examined tissues, including hepatopancreas, hemocytes, heart, gill, intestine and muscle; the highest Pc-CaM-L expression level was detected in the hepatopancreas. Sodium dodecyl sulfate polyacrylamide gel electrophoresis and western blot analysis demonstrated that a recombinant Pc-CaM-L protein was successfully expressed in Escherichia coli. The calcium-binding activity of the purified Pc-CaM-L protein was confirmed by gel mobility shift assay. The expression of Pc-CaM-L was significantly upregulated in gut, gill and hemocytes after lipopolysaccharide or polyinosinic:polycytidylic acid induction. These results suggest that Pc-CaM-L plays a role in the immune response of P. clarkii.
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