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SHH Antibody (Center) Blocking peptide

Synthetic peptide

Product Information
Primary Accession Q15465
Clone Names 90625210
Peptide ID 90625210
Additional Information
Gene ID 6469
Other Names Sonic hedgehog protein, SHH, HHG-1, Sonic hedgehog protein N-product, Sonic hedgehog protein C-product, SHH
Format Synthetic peptide was lyophilized with 100% acetonitrile and is supplied as a powder. Reconstitute with 0.1 ml DI water for a final concentration of 1 mg/ml.
StorageMaintain refrigerated at 2-8°C for up to 6 months. For long term storage store at -20°C.
PrecautionsThis product is for research use only. Not for use in diagnostic or therapeutic procedures.
Protein Information
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 N-product: Cell membrane {ECO:0000250|UniProtKB:Q62226}; Lipid-anchor {ECO:0000250|UniProtKB:Q62226}. Note=The dual-lipidated sonic hedgehog protein N-product (ShhNp) is firmly tethered to the cell membrane where it forms multimers (PubMed:24522195). Further solubilization and release from the cell surface seem to be achieved through different mechanisms, including the interaction with DISP1 and SCUBE2, movement by lipoprotein particles, transport by cellular extensions called cytonemes or by the proteolytic removal of both terminal lipidated peptides (PubMed:26875496, PubMed:24522195).
Research Areas
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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.


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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Cat# BP12343c
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