PURPOSE: The similarity in collagen fiber diameter between the camel cornea (CC) and the human cornea, along with its relatively large size, positions the CC as a promising candidate for tissue engineering applications. This study aimed to evaluate the effectiveness of various decellularization methods on the CC, followed by assessing protein content similarities between the CC and the human cornea, highlighting its potential for human-related tissue engineering research. METHODS: Camel corneas were extracted from freshly isolated camel eyeballs and subjected to multiple decellularization protocols, including sodium dodecyl sulfate (SDS)-based and formic acid (FA)-based methods. The decellularized camel corneas (dCCs) were then analyzed for histological properties, cell viability, collagen fiber integrity, ultrastructural characteristics, and susceptibility to bacterial contamination. Additionally, the amino acid (AA) composition of CC proteins was compared to that of the human cornea. RESULTS: Histological analyses confirmed successful decellularization of the CC using both SDS- and FA-based protocols. Cell viability significantly increased when cells were cultured on dCC scaffolds, with the highest improvement observed in the 0.5% SDS-Tris-treated group. OrgA and 0.5% SDS-Tris protocols preserved collagen fibers most effectively among the treatment groups. Ultrastructural assessments revealed consistent results across all groups. However, susceptibility to bacterial contamination was noted in the FA-treated group after one week of refrigerated storage. Lastly, the AA composition of CC proteins demonstrated a notable resemblance to the human cornea. CONCLUSION: This study demonstrates that the CC can be effectively decellularized using SDS- and FA-based methods while maintaining tissue morphology, ultrastructure, and collagen fiber integrity. Despite FA's efficacy in decellularization, its potential for causing bacterial contamination warrants caution in its application. The high degree of similarity in AA composition between CC and the human cornea further underscores the potential of CC as a scaffold for human-related tissue engineering studies.