Recombinant Human Shh proteins induce alkaline phosphatase production by mesenchymal stem cells. High Activity Shh (green), purified from HEK293 cells and containing the correct post-translational modifications ...read more
1 μg/lane of Recombinant Human Sonic Hedgehog/Shh Protein was resolved with SDS-PAGE under reducing (R) and non-reducing (NR) conditions and visualized by silver staining, showing 18-24 kDa bands.
LC/ESI-MS analysis of Recombinant Human (rh)SHH Protein, High Activity shows major peaks at 20119.3, 20145.2, and 20171.6 Da, suggesting that recombinant human SHH molecules are dual-modified with cholesterol at ...read more
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. 237:465. The ED50 for this effect is typically 6-36 ng/mL.
Source
Human embryonic kidney cell, HEK293-derived human Sonic Hedgehog/Shh protein Cys24-Gly197
Cholesterol-modified at the C-terminal and fatty acid-modified at the N-terminal
Protein/Peptide Type
Recombinant Proteins
Gene
SHH
Purity
>90%, by SDS-PAGE visualized with Silver Staining and quantitative densitometry by Coomassie® Blue Staining.
Endotoxin Note
<0.10 EU per 1 μg of the protein by the LAL method.
Applications/Dilutions
Dilutions
Bioactivity
Theoretical MW
20 kDa. Disclaimer note: The observed molecular weight of the protein may vary from the listed predicted molecular weight due to post translational modifications, post translation cleavages, relative charges, and other experimental factors.
SDS-PAGE
18-24 kDa, reducing conditions
Publications
Read Publications using 8908-SH in the following applications:
Use a manual defrost freezer and avoid repeated freeze-thaw cycles.
6 months from date of receipt, -20 to -70 °C as supplied.
3 months, -20 to -70 °C under sterile conditions after opening.
Buffer
Supplied as a 0.2 μm filtered solution in MES, NaCl and CHAPS with BSA as a carrier protein.
Purity
>90%, by SDS-PAGE visualized with Silver Staining and quantitative densitometry by Coomassie® Blue Staining.
Notes
This product is produced by and ships from R&D Systems, Inc., a Bio-Techne brand.
Alternate Names for Recombinant Human Sonic Hedgehog/Shh Protein, High Activity
HHG1
HHG-1
HLP3
HPE3
MCOPCB5
MCOPCB5sonic hedgehog (Drosophila) homolog
Shh
ShhNC
SMMCI
SMMCIsonic hedgehog homolog (Drosophila)
sonic hedgehog homolog
sonic hedgehog protein
Sonic Hedgehog
TPT
TPTPS
Background
The Sonic Hedgehog (Shh) protein is expressed in embryonic tissues that are critical for the patterning of the developing central nervous system, somite, and limb. It is also involved in whisker, hair, foregut, tooth, and bone development. The Shh protein regulates neural and hematopoietic stem cell fate and is important for thymocyte differentiation and proliferation as well as T cell determination. In adult tissue, Shh is associated with cancer development and tissue remodeling following injury (1-3). Human Shh encodes a 462 amino acid (aa) precursor Shh protein that is autocatalytically processed to yield a non-glycosylated 19 kDa N-terminal fragment (Shh-N) and a glycosylated 25 kDa C-terminal protein (Shh-C) (4). The Shh-C protein, which is responsible for the intramolecular processing of Shh, is rapidly degraded following Shh proteolysis (5). The Shh-N protein is highly conserved, sharing >98% aa identity between mouse, human, rat, canine, porcine, and chicken Shh-N. Shh-N can be palmitoylated at its N-terminal cysteine and modified by cholesterol addition at its C-terminus (6). These modifications contribute to the membrane tethering of the Shh protein as well as its assembly into various sized multimers (6-9). Lipid modification and multimerization greatly increase the receptor binding affinity and signaling potency of the Shh-N protein (5, 6, 8, 9). Monomeric and multimeric Shh can be released from the plasma membrane by the cooperative action of DISP1, SCUBE2, and TACE/ADAM17 (10-12). Modifications also extend the effective range of functionality of the Shh protein and are required for the development of Shh protein gradients important in tissue morphogenesis (9, 13). Canonical signaling by the Shh protein is mediated by a multicomponent receptor complex that includes Patched (PTCH1, PTCH2) and Smoothened (SMO) (14). Binding of the Shh protein to PTCH releases the basal repression of SMO by PTCH. Shh activity can also be regulated through interactions with heparin, glypicans, and membrane-associated Hip (hedgehog interacting protein) (13, 15, 16).
Briscoe, J. and P.P. Therond (2013) Mol. Cell. Biol. 14:416.
Aviles, E.C. et al. (2013) Front. Cell. Neurosci. 7:86.
Xie, J. et al. (2013) OncoTargets Ther. 6:1425.
Marigo, V. et al. (1995) Genomics 28:44.
Zeng, X. et al. (2001) Nature 411:716.
Feng, J. et al. (2004) Development 131:4357.
Goetz, J.A. et al. (2006) J. Biol. Chem. 281:4087.
Pepinsky, R.B. et al. (1998) J. Biol. Chem. 273:14037.
Chen, M.-H. et al. (2004) Genes Dev. 18:641.
Etheridge, L.A. et al. (2010) Development 137:133.
Jakobs, P. et al. (2014) J. Cell Sci. 127:1726.
Dierker, T. et al. (2009) J. Biol. Chem. 284:8013.
Lewis, P.M. et al. (2001) Cell 105:599.
Carpenter, D. et al. (1998) Proc. Natl. Acad. Sci. USA 95:13630.
Filmus, J. and M. Capurro (2014) Matrix Biol. 35:248.
Chuang, P.-T. and A.P. McMahon (1999) Nature 397:617.
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