Desert Hedgehog is a secreted protein that undergoes autocatalytic cleavage, resulting in two distinct domains: the N-terminal signaling domain and the C-terminal domain. The N-terminal domain is responsible for the protein’s signaling activity, while the C-terminal domain is involved in precursor processing. The N-terminal domain is further modified by the addition of cholesterol and a fatty acid acyl chain, which anchor it to the cell membrane .
The primary function of DHH is to bind to Patched receptors (PTCH1 and PTCH2) on the cell surface. This binding relieves the repression of Smoothened (SMO) signaling, leading to the activation of downstream signaling pathways that regulate gene expression. DHH signaling is essential for various developmental processes, including male gonadal differentiation and perineurial development .
Recombinant human Desert Hedgehog (rhDHH) is produced using recombinant DNA technology, typically in Escherichia coli (E. coli) expression systems. The recombinant protein is a non-glycosylated polypeptide chain containing 177 amino acids, with a molecular mass of approximately 20 kDa . The production of rhDHH involves chromatographic techniques to ensure high purity and biological activity.
Recombinant human Desert Hedgehog is widely used in laboratory research to study its role in developmental biology and disease. It is particularly valuable for investigating the mechanisms of Hedgehog signaling and its implications in various conditions, such as partial gonadal dysgenesis and minifascicular polyneuropathy . Additionally, rhDHH is used in cell culture and tissue culture experiments to explore its effects on cell differentiation and tissue patterning.
Recombinant human Desert Hedgehog is typically lyophilized and stored at temperatures below -70°C to maintain its stability. Upon reconstitution, the protein remains stable for up to one week at 4°C or up to three months at -20°C. To enhance stability and prevent degradation, a carrier protein such as Bovine Serum Albumin (BSA) is often added .