Recombinant Human SALL2 protein

SALL2. a member of the Spalt-like (SALL) transcription factor family, is characterized by its zinc finger domains that mediate DNA binding and protein interactions. It plays critical roles in embryonic development, cell differentiation, and tissue homeostasis. SALL2 is notably involved in regulating gene networks tied to neurogenesis, eye development, and kidney formation. Studies also link SALL2 to cancer biology, where it exhibits dual roles—acting as a tumor suppressor in some contexts (e.g., ovarian cancer) while promoting tumorigenesis in others (e.g., glioblastoma). Its expression is frequently dysregulated in malignancies, often correlating with clinical outcomes.

Recombinant SALL2 protein, produced via expression systems like *E. coli* or mammalian cells, retains the functional domains necessary for studying its molecular mechanisms. Researchers use it to investigate SALL2's interaction partners, DNA-binding specificity, and regulatory effects on downstream targets such as *p21* or *MYC*. Purification tags (e.g., His-tag) enable efficient isolation for *in vitro* assays. Notably, SALL2 recombinant proteins aid in exploring its role in oxidative stress responses and DNA repair pathways, which may inform therapeutic strategies. Mutations in *SALL2* are associated with developmental disorders, making recombinant variants valuable for modeling genetic defects. Despite progress, functional redundancy within the SALL family and context-dependent signaling pose challenges in delineating SALL2-specific pathways. Current research focuses on its epigenetic regulatory functions and potential as a biomarker or drug target.