In this study, Chenopodium quinoa CqSAP8 was cloned based on the sequence on the NCBI website. Bioinformatics methods were used to analyze the sequence, physicochemical property and structure of CqSAP8 protein. The expression patterns of CqSAP8 in tissues and under different abiotic stresses were determined by using qRTPCR method. The results showed that: (1) the CDS of CqSAP8 was 528 bp, encoding 175 amino acids with a relative molecular weight of 18.73 kD and an isoelectric point of 7.46. CqSAP8 was predicated to be a stable hydrophilic protein. CqSAP8 contained a A20 conserved domain in the N terminus and an AN1 conserved domain in the C terminus, which was a typical SAP protein. (2) Sequence alignment and evolutionary analysis showed that CqSAP8 was mostly closely related to BvSAP8 and SoSAP8 with a sequence similarity 89.66% and 89.47%, respectively. (3) qRTPCR analysis showed that CqSAP8 expressed in root, stem, leaf, flower and seed, and the highest expression was found in seed. The expression of CqSAP8 gene reached the maximum at 12 h under drought stress and high temperature stress, which was 13.09 and 17.47 times of that of the control, respectively, while the maximum expression under both high salt and low temperature stress was 3.91 times that of the control, indicating that CqSAP8 responded to a variety of abiotic stresses. Additionally, The expression level of CqSAP8 increased sharply at 24 h under ABA stress, suggesting that the response of CqSAP8 in the early stage of abiotic stress was independent of ABA. This study laid a foundation for further study on the function and molecular mechanism of CqSAP8 gene.