Recombinant mouse Sonic Hedgehog protein

Specifications

Form

Lyophilized

Additional notes

Purity is greater than 97% as determined by reducing and non-reducing SDS-PAGE and analytical HPLC.

General info

Function

Sonic hedgehog protein. The C-terminal part of the sonic hedgehog protein precursor displays an autoproteolysis and a cholesterol transferase activity (PubMed : 7736596, PubMed : 7891723, PubMed : 8824192). Both activities result in the cleavage of the full-length protein into two parts (ShhN and ShhC) followed by the covalent attachment of a cholesterol moiety to the C-terminal of the newly generated ShhN (PubMed : 8824192). Both activities occur in the reticulum endoplasmic (PubMed : 21357747). Once cleaved, ShhC is degraded in the endoplasmic reticulum (PubMed : 21357747).. Sonic hedgehog protein N-product. The dually lipidated sonic hedgehog protein N-product (ShhNp) is a morphogen which is essential for a variety of patterning events during development. Induces ventral cell fate in the neural tube and somites (PubMed : 11430830, PubMed : 24863049). Involved in the patterning of the anterior-posterior axis of the developing limb bud (PubMed : 15315762). Essential for axon guidance (PubMed : 12679031). Binds to the patched (PTCH1) receptor, which functions in association with smoothened (SMO), to activate the transcription of target genes (By similarity). In the absence of SHH, PTCH1 represses the constitutive signaling activity of SMO (By similarity).

Sequence similarities

Belongs to the hedgehog family.

Post-translational modifications

Sonic hedgehog protein. The C-terminal domain displays an autoproteolysis activity and a cholesterol transferase activity (PubMed:7736596, PubMed:7891723, PubMed:8824192). Both activities result in the cleavage of the full-length protein and covalent attachment of a cholesterol moiety to the C-terminal of the newly generated N-terminal fragment (ShhN) (PubMed:7736596, PubMed:7891723, PubMed:8824192). Cholesterylation is required for the sonic hedgehog protein N-product targeting to lipid rafts and multimerization (PubMed:24522195, PubMed:8824192). ShhN is the active species in both local and long-range signaling, whereas the C-product (ShhC) is degraded in the reticulum endoplasmic (PubMed:21357747).. Sonic hedgehog protein N-product. N-palmitoylation by HHAT of ShhN is required for sonic hedgehog protein N-product multimerization and full activity (PubMed:11486055, PubMed:15075292). It is a prerequisite for the membrane-proximal positioning and the subsequent shedding of this N-terminal peptide (PubMed:24522195).. Sonic hedgehog protein N-product. The lipidated N- and C-terminal peptides of ShhNp can be cleaved (shedding) (PubMed:24522195). The N-terminal palmitoylated peptide is cleaved at the Cardin-Weintraub (CW) motif site (PubMed:24522195). The cleavage reduced the interactions with heparan sulfate (PubMed:23118222). The cleavage is enhanced by SCUBE2.