Recombinant Mouse Sonic Hedgehog/Shh, N-Terminus Protein, CF Summary
Details of Functionality |
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 0.6-3 µg/mL. |
Source |
E. coli-derived mouse Sonic Hedgehog/Shh protein Cys25-Gly198, with a C-terminal 6-His tag |
Accession # |
|
N-terminal Sequence |
Cys25 |
Protein/Peptide Type |
Recombinant Proteins |
Gene |
Shh |
Purity |
>97%, by SDS-PAGE under reducing conditions and visualized by silver stain |
Endotoxin Note |
<0.10 EU per 1 μg of the protein by the LAL method. |
Applications/Dilutions
Dilutions |
|
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. |
Publications |
Read Publications using 461-SH/CF in the following applications:
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Packaging, Storage & Formulations
Storage |
Use a manual defrost freezer and avoid repeated freeze-thaw cycles.- 12 months from date of receipt, -20 to -70 °C as supplied.
- 1 month, 2 to 8 °C under sterile conditions after reconstitution.
- 3 months, -20 to -70 °C under sterile conditions after reconstitution.
|
Buffer |
Lyophilized from a 0.2 μm filtered solution in PBS with Trehalose. |
Purity |
>97%, by SDS-PAGE under reducing conditions and visualized by silver stain |
Reconstitution Instructions |
Reconstitute at 100 μg/mL in sterile PBS. |
Notes
This product is produced by and ships from R&D Systems, Inc., a Bio-Techne brand.
Alternate Names for Recombinant Mouse Sonic Hedgehog/Shh, N-Terminus Protein, CF
Background
Sonic Hedgehog (Shh) 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. Shh 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). Mouse Shh encodes a 437 amino acid (aa) precursor 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). Shh-C, which is responsible for the intramolecular processing of Shh, is rapidly degraded following Shh proteolysis (5). Shh-N 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 Shh as well as its assembly into various sized multimers (6-9). Lipid modification and multimerization greatly increase Shh-N receptor binding affinity and signaling potency (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 Shh functionality and are required for the development of protein gradients important in tissue morphogenesis (9, 13). Canonical signaling of Shh is mediated by a multicomponent receptor complex that includes Patched (PTCH1, PTCH2) and Smoothened (SMO) (14). The binding of Shh 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.
- Echelard, Y. et al. (1993) Cell 75:1417.
- 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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