Desert Hedgehog proteins are synthesized as 45 kDa precursors that undergo autocatalytic cleavage. This process results in the formation of a 19 kDa N-terminal fragment, which remains membrane-associated due to modifications with cholesterol and palmitate . These modifications are essential for the protein’s signaling activity and its ability to interact with other cell surface receptors.
The primary function of Desert Hedgehog is to bind to receptors such as Patched (Ptch1), Patched 2 (Ptch2), and Hedgehog-interacting protein (Hip). This binding inhibits the ability of Patched to repress Smoothened (Smo) signaling, thereby activating the Hedgehog signaling pathway . This pathway is critical for the regulation of gene expression involved in cell growth, differentiation, and tissue patterning.
The recombinant form of Desert Hedgehog (C23II) is produced using E. coli expression systems. The protein is purified to a high degree of purity, typically greater than 95%, as determined by SDS-PAGE and visualized with silver staining and quantitative densitometry . The recombinant protein is biologically active and is measured by its ability to induce alkaline phosphatase production in MC3T3-E1 mouse preosteoblast cells .
Recombinant Mouse Desert Hedgehog (C23II) is used in various research applications, including studies on cell signaling, developmental biology, and tissue engineering. The protein is lyophilized from a 0.2 μm filtered solution in PBS and DTT, and it is recommended to reconstitute it at 500 μg/mL in sterile PBS . For optimal stability, the reconstituted protein should be stored at -20°C to -70°C under sterile conditions and should avoid repeated freeze-thaw cycles .