Human Shh cDNA encodes a 462 amino acid (aa) residue (45 kDa) precursor protein with a 23 aa signal
peptide. An autocatalytic cleavage reaction yields a 19 kDa (residues 24 197) aminoterminal fragment
(ShhN), and a 25 kDa (residues 198 462) carboxyterminal domain (Shh C). The Nterminal domain retains all known signaling capabilities, while the Cterminal domain is responsible for the intramolecular processing, acting as a cholesterol transferase that covalently transfers the cholesterol molecule to the Cterminus of Shh N. When Shh is expressed in insect or mammalian cells, a palmitoyl group is also attached to the Nterminal cysteine of Shh N via an amide linkage. Although the binding affinity to their receptors is not changed, lipidmodified ShhN proteins are more potent than the unmodified proteins in cellbased assays. Other hydrophobic modifications to unmodified ShhN, including the substitution of the Nterminal cysteine residue with two hydrophobic isoleucine residues, can also increase ShhN potency. Shh is involved in regulating the patterning of the developing central nervous system, somite, and limb. Shh plays an important role in the development of particular tissues such as whisker, hair, foregut, tooth and bone. Studies suggest that Shh is involved in regulating stem cell fates of neural and hematopoeitic lineages, and that aberrant Shh signaling is implicated in basal cell carcinomas and other diseases.
- Product Reviews
- Product Publications
If you've used this product in a publication, let us know. Email email@example.com, with the publication details and you could be eligible for an Amazon gift card.
- Related Products