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SHH Antibody (Center) Blocking peptide
Synthetic peptide
- SPECIFICATION
- CITATIONS
- PROTOCOLS
- BACKGROUND
| Primary Accession | Q15465 |
|---|---|
| Clone Names | 90625210 |
| Gene ID | 6469 |
|---|---|
| Other Names | Sonic hedgehog protein, SHH, HHG-1, Sonic hedgehog protein N-product, Sonic hedgehog protein C-product, SHH |
| Format | Peptides are lyophilized in a solid powder format. Peptides can be reconstituted in solution using the appropriate buffer as needed. |
| Storage | Maintain refrigerated at 2-8°C for up to 6 months. For long term storage store at -20°C. |
| Precautions | This product is for research use only. Not for use in diagnostic or therapeutic procedures. |
| Name | SHH (HGNC:10848) |
|---|---|
| Function | [Sonic hedgehog protein]: The C-terminal part of the sonic hedgehog protein precursor displays an autoproteolysis and a cholesterol transferase activity (By similarity). 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 (By similarity). Both activities occur in the reticulum endoplasmic (By similarity). Once cleaved, ShhC is degraded in the endoplasmic reticulum (By similarity). |
| Cellular Location | [Sonic hedgehog protein]: Endoplasmic reticulum membrane. Golgi apparatus membrane. Secreted Note=Co-localizes with HHAT in the ER and Golgi membrane |
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Provided below are standard protocols that you may find useful for product applications.
Background
This gene encodes a protein that is instrumental inpatterning the early embryo. It has been implicated as the keyinductive signal in patterning of the ventral neural tube, theanterior-posterior limb axis, and the ventral somites. Of threehuman proteins showing sequence and functional similarity to thesonic hedgehog protein of Drosophila, this protein is the mostsimilar. The protein is made as a precursor that isautocatalytically cleaved; the N-terminal portion is soluble andcontains the signalling activity while the C-terminal portion isinvolved in precursor processing. More importantly, the C-terminalproduct covalently attaches a cholesterol moiety to the N-terminalproduct, restricting the N-terminal product to the cell surface andpreventing it from freely diffusing throughout the developingembryo. Defects in this protein or in its signalling pathway are acause of holoprosencephaly (HPE), a disorder in which thedeveloping forebrain fails to correctly separate into right andleft hemispheres. HPE is manifested by facial deformities. It isalso thought that mutations in this gene or in its signallingpathway may be responsible for VACTERL syndrome, which ischaracterized by vertebral defects, anal atresia, tracheoesophagealfistula with esophageal atresia, radial and renal dysplasia,cardiac anomalies, and limb abnormalities. Additionally, mutationsin a long range enhancer located approximately 1 megabase upstreamof this gene disrupt limb patterning and can result in preaxialpolydactyly.
References
Maloverjan, A., et al. J. Biol. Chem. 285(39):30079-30090(2010)Li, F., et al. Arterioscler. Thromb. Vasc. Biol. 30(9):1787-1794(2010)Lesiak, A., et al. Pol. Merkur. Lekarski 29(170):141-143(2010)Choi, S.S., et al. Hepatology 52(1):278-290(2010)Jugessur, A., et al. PLoS ONE 5 (7), E11493 (2010) :
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