SPA17 was first described as a rabbit sperm antigen with lectin-like properties . It is a major zona pellucida-binding protein, but its ubiquitous expression suggests a broader role in cell-cell adhesion and/or cell migration . The central portion of SPA17 contains carbohydrate-binding motifs, which likely contribute to its cell-cell adhesion functions .
SPA17 is a member of the cancer-testis antigen (CTA) family, which are proteins typically expressed in the testis but aberrantly expressed in various cancers . This unique expression pattern makes SPA17 a potential target for cancer immunotherapy. Studies have shown that SPA17 is highly expressed in endometrial and cervical cancers, among others . Its expression in these cancers is heterogeneous and not correlated with the histological subtype or grade of malignancy .
SPA17 has been proposed as a useful target for tumor-vaccine strategies and a novel marker to define tumor subsets and predict drug response . It has been found to regulate the progression of various cancers and is significantly correlated with immune-activated hallmarks, immune cell infiltrations, and immunoregulator expressions . This makes SPA17 a promising candidate for cancer immunotherapy and a potential prognostic marker .
Recombinant SPA17 is produced using recombinant DNA technology, which involves inserting the gene encoding SPA17 into a suitable expression system, such as bacteria or yeast, to produce the protein in large quantities. This recombinant protein can be used in various research applications, including studying its role in fertilization, cell adhesion, and cancer progression.