Heat shock proteins (Hsps) play an essential role in cell defense against cell damages by several environmental and physiological stresses. We cloned and sequenced full-length heat shock protein 60-kDa (Hsp60) from the Arctic copepod Calanus glacialis cDNA. The complete nucleotide sequence of Calanus glacialis Hsp60 ( CgHsp60) gene contained 2,092 bp in length. The open reading frame (ORF) was 1,743 bp flanked by a 5`-UTR of 90 bp and a long 3`-UTR of 259 bp, and encoded a putative protein of 581 amino acids with a calculated molecular weight of 62 kDa. It showed high similarity to those of Culicoides variipennis(73%), Aedes aegypti (72%), and Tribolium castaneum (71%) at the amino acid sequence level. In phylogenetic analysis, it clustered with other arthropods sequences. We also confirmed that the recombinant protein of C. glacialis Hsp60 by the SDS-PAGE and immunoblotting analysis after expression of recombinant gene construct in Escherichia coli.