Sonic Hedgehog/Shh, N-Terminus 組換え体(リコンビナント)タンパク質 | Recombinant Mouse Sonic Hedgehog/Shh, N-Terminus

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• CF(Carrier-Free)とは？
• Product Details
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• Citations

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CF(Carrier-Free)とは？

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Product Details

Source

E. coli-derived, Cys25-Gly198, with a C-terminal 6-His tag

Accession

Q62226

Purity

>97%, by SDS-PAGE under reducing conditions and visualized by silver stain.

Predicted Molecular Mass

20 kDa

Activity

Measured by its ability to induce alkaline phosphatase production by C3H10T1/2 mouse embryonic fibroblast cells. Nakamura, T. et al. (1997) Biochem. Biophys. Res. Commun. 237

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Additional Information

Molecule Information

Sonic Hedgehog/Shh

Aliases

Shh

Entrez Gene IDs

6469 (Human); 20423 (Mouse)

Background

Sonic Hedgehog

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) amino-terminal fragment (Shh-N), and a 25 kDa (residues 198 - 462) carboxy-terminal domain (Shh-C). The N-terminal domain retains all known signaling capabilities, while the C-terminal domain is responsible for the intramolecular processing, acting as a cholesterol transferase that covalently transfers the cholesterol molecule to the C-terminus of Shh-N. When Shh is expressed in insect or mammalian cells, a palmitoyl group is also attached to the N-terminal cysteine of Shh-N via an amide linkage. Although the binding affinity to their receptors is not changed, lipid-modified Shh-N proteins are more potent than the unmodified proteins in cell-based assays. Other hydrophobic modifications to unmodified Shh-N, including the substitution of the N-terminal cysteine residue with two hydrophobic isoleucine residues, can also increase Shh-N potency. At the cell surface, Shh-N activity is mediated by a multicomponent receptor complex involving the 12-pass transmembrane protein, Patched (Ptc) which binds Shh with high affinity and Smoothened (Smo), a signaling seven transmembrane G-protein coupled receptor. In the absence of Shh, Ptc represses Smo activity. The binding of Shh to Ptc releases the basal repression of Smo by Ptc. Shh is expressed in key embryonic tissues such as the Hensen’s node, the zone of polarizing activity in the posterior limb bud, the notochord, and the floor plate of the neural tube. 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.

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Citations

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