American shad (Alosa sapidissima) belongs to Clupeomorpha, Clupeiformes, Clupeidae, Alosa. As eurythermal, euryhaline anadromous and migratory fish, American shad and Chinese shad are not only very similar in appearance and habits, but also have high nutritional value and economic value. American shad is extremely sensitive to changes in the external environment, vulnerable to the impact of environmental factors change (such as sound, light, water physical and chemical factors, etc.) and the influence of manual operation such as fishing, transportation, etc. Heat stress proteins (HSPs), also known as heat shock proteins, are founded that it is widely present in different species. It is a family of non-specific cell protective protein associated with resilience, and similar to a number of housekeeping genes. And the heat stress protein, especially the heat stress protein 70 (hsp70) family, is highly conserved in evolution. It also has a variety of biological functions: As a molecular chaperone, it assists proteins in properly folding, assembling, transporting, and regulating, repairing damaged proteins, and disintegrating of denatured proteins under stress; In cell protection, it can protect mitochondria from cytokines damage, play an important role in the anti-apoptotic, anti-oxidation and immune response. Besides, it also participates in the immune response in antigen-presenting, synergistic immune function. Hsp70 cDNA was cloned, analyzed, and the expression level of hsp70 mRNA was detected in A variety of fish species, such as bluntnose black bream (Megalobrama amblycephala), grass carp (Ctenopharyngodon idellus), silver carp (Hypophthalmichthys molitrix), nile tilapia (Tilapia nilotica), roughskin sculpin (Trachidermus fasciatus), bronze gudgeon (Coreius guichenoti ), siberian sturgeon (Acipenser baerii), sword tali (Xiphophorus hellerii), bastard halibut (Paralichthys olivaceus) etc. Studies show that the expression of hsp70 gene is regulated at the transcriptional level. The experiment, by the study on the expression of hsp70 gene in American shad broodstocks tissues and differential expression before and after the transport stress, aimed at a further understanding of the American shad in HSP70 protein synthesis and expression and regulation mechanism, in order to provide a theoretical basis for resistance mechanism study of American shad. In this experiment, by means of artificial transportation stress, we take 6 tails as the transport 0 h sampling, then catch 24 tails randomly divided into 12 bags, each bag 2 tails: 6 bags for 2 h transport stress sampling, while the other 6 bags for 4 h sampling. The differences between groups were analyzed by ANOVA One-way, and the results were expressed by Mean±SE. The full-length cDNA of hsp70 of American shad was cloned by reverse transcription poly merase chainreaction (RT-PCR) and rapid amplification of cDNA ends (RACE) methods. The results revealed that the length of hsp70 cDNA is 2 545 bp, containing an open reading frame (ORF) of 1 914 bp specified a peptide of 637 amino acids. The secondary structures contained three signature sequences of HSP70 family (Fig. 2). The homology analysis indicated that hsp70 of American shad shared more than 84.0% identity with the hsp70s of other fishes such as Astyanax mexicanus , it is also shared as high as 73% and 38% identity with Drosophila auraria and Escherichia coli (Tab. 2). The tissue-specific expressions of hsp70 mRNAs were detected in American shad. A high expression was observed in the gill, muscle and head kidney，while relatively high expression was encountered in brain and heart，and a weak expression in the liver, spleen, intestine and kidney (Fig. 4). Utilizing real-time quantitative PCR studied the effects of transport stress on expression of hsp70 mRNA in parent fish of American shad. Result of showed that hsp70 mRNA content in gill and liver increased significantly after transport 2 hours and then dropped after transport 4 hours (Fig. 5 and Fig. 6), in head kidney showing an increasing trend (Fig. 7). Results showed the gene is consistent with the characteristics of hsp70. And the hsp70 mRNA in gill, liver, head kidney showed obvious response on transport stress.