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Recombinant Mouse Sonic Hedgehog/Shh (C25II) N-Terminus, CF

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Recombinant Mouse Sonic Hedgehog/Shh (C25Il), N-Terminus (Catalog # 464-SH/CF) induces alkaline phosphatase production by the C3H10T1/2 mouse embryonic fibroblast cell line. The activity is more than 30-fold greater ...read more
Recombinant Mouse Sonic Hedgehog/Shh (C25II), N-Terminus (Catalog # 464-SH/CF) has a molecular weight (MW) of 20.7 kDa as analyzed by SEC-MALS, suggesting that this protein is a monomer.  MW may differ from predicted ...read more
1 μg/lane of Recombinant Mouse Sonic Hedgehog/Shh (C25Il), N-Terminus was resolved with SDS-PAGE under reducing (R) conditions and visualized by silver staining, showing a single band at 22 kDa.
Dopaminergic neurons were generated from human pluripotent stem cells in media that included Bovine Fibronectin Protein (1030-FN) to support cell attachment and spreading, the ITS and N-2 Plus Media Supplements (AR013 ...read more
Dopaminergic neurons were generated from human pluripotent stem cells in media that included Bovine Fibronectin Protein (1030-FN) to support cell attachment and spreading, the ITS and N-2 Plus Media Supplements (AR013 ...read more

Product Details

Summary
Reactivity MuSpecies Glossary
Applications Bioactivity
Format
Carrier-Free

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Recombinant Mouse Sonic Hedgehog/Shh (C25II) N-Terminus, 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 0.05-0.25 µg/mL.
Source
E. coli-derived mouse Sonic Hedgehog/Shh protein
Cys25-Gly198 (Cys25Ile-Ile), with an N-terminal Met
Accession #
N-terminal Sequence
Met
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
  • Bioactivity
Theoretical MW
19.8 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
464-SH/CF in the following applications:

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 NaH2PO4, NaCl and DTT.
Purity
>97%, by SDS-PAGE under reducing conditions and visualized by silver stain.
Reconstitution Instructions
Reconstitute at 100-200 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 (C25II) N-Terminus, CF

  • 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

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).
  1. Briscoe, J. and P.P. Therond (2013) Mol. Cell. Biol. 14:416.
  2. Aviles, E.C. et al. (2013) Front. Cell. Neurosci. 7:86.
  3. Xie, J. et al. (2013) OncoTargets Ther. 6:1425.
  4. Echelard, Y. et al. (1993) Cell 75:1417.
  5. Zeng, X. et al. (2001) Nature 411:716.
  6. Feng, J. et al. (2004) Development 131:4357.
  7. Goetz, J.A. et al. (2006) J. Biol. Chem. 281:4087.
  8. Pepinsky, R.B. et al. (1998) J. Biol. Chem. 273:14037.
  9. Chen, M.-H. et al. (2004) Genes Dev. 18:641.
  10. Etheridge, L.A. et al. (2010) Development 137:133.
  11. Jakobs, P. et al. (2014) J. Cell Sci. 127:1726.
  12. Dierker, T. et al. (2009) J. Biol. Chem. 284:8013.
  13. Lewis, P.M. et al. (2001) Cell 105:599.
  14. Carpenter, D. et al. (1998) Proc. Natl. Acad. Sci. USA 95:13630.
  15. Filmus, J. and M. Capurro (2014) Matrix Biol. 35:248.
  16. Chuang, P.-T. and A.P. McMahon (1999) Nature 397:617.

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Publications for Sonic Hedgehog/Shh (464-SH/CF)(62)

We have publications tested in 6 confirmed species: Human, Mouse, Chicken, Primate - Callitrix jacchus (Common Marmoset), Primate - Rhesus macaque, Zebrafish.

We have publications tested in 5 applications: Bioassay, Cell Culture, Differentiation, In Vivo, Tissue Culture.


Filter By Application
Bioassay
(55)
Cell Culture
(4)
Differentiation
(2)
In Vivo
(1)
Tissue Culture
(1)
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Human
(37)
Mouse
(21)
Chicken
(1)
Primate - Callitrix jacchus (Common Marmoset)
(1)
Primate - Rhesus macaque
(1)
Zebrafish
(2)
All Species
Showing Publications 1 - 10 of 62. Show All 62 Publications.
Publications using 464-SH/CF Applications Species
Y Fan, J Hackland, A Baggiolini, LY Hung, H Zhao, P Zumbo, P Oberst, AP Minotti, E Hergenrede, S Najjar, Z Huang, NM Cruz, A Zhong, M Sidharta, T Zhou, E de Stanchi, D Betel, RM White, M Gershon, KG Margolis, L Studer hPSC-derived sacral neural crest enables rescue in a severe model of Hirschsprung&#039;s disease Cell Stem Cell, 2023;30(3):264-282.e9. 2023 [PMID: 36868194] (Bioassay, Human) Bioassay Human
Y Fan, J Hackland, A Baggiolini, LY Hung, H Zhao, P Zumbo, P Oberst, AP Minotti, E Hergenrede, S Najjar, Z Huang, NM Cruz, A Zhong, M Sidharta, T Zhou, E de Stanchi, D Betel, RM White, M Gershon, KG Margolis, L Studer hPSC-derived sacral neural crest enables rescue in a severe model of Hirschsprung&#039;s disease Cell Stem Cell, 2023-03-02;30(3):264-282.e9. 2023-03-02 [PMID: 36868194] (Bioassay, Human) Bioassay Human
MJ Corenblum, A McRobbie-J, E Carruth, K Bernard, M Luo, LJ Mandarino, S Peterson, D Billheimer, T Maley, ED Eggers, L Madhavan Parallel Neurodegenerative Phenotypes in Sporadic Parkinson&#039;s Disease Fibroblasts and Midbrain Dopamine Neurons bioRxiv : the preprint server for biology, 2023-02-12;0(0):. 2023-02-12 [PMID: 36798207] (Bioassay, Human) Bioassay Human
PR Wu, SY Chiang, R Midence, WC Kao, CL Lai, IC Cheng, SJ Chou, CC Chen, CY Huang, RH Chen Wdr4 promotes cerebellar development and locomotion through Arhgap17-mediated Rac1 activation Cell Death & Disease, 2023-01-21;14(1):52. 2023-01-21 [PMID: 36681682] (Bioassay, Mouse) Bioassay Mouse
S Wu, NC Hernandez, DW Sirkis, I Thomas-Wri, R Wade-Marti, R Schekman Unconventional secretion of alpha-synuclein mediated by palmitoylated DNAJC5 oligomers Elife, 2023-01-10;12(0):. 2023-01-10 [PMID: 36626307] (Bioassay, Mouse) Bioassay Mouse
A Iannielli, M Luoni, SG Giannelli, R Ferese, G Ordazzo, M Fossati, A Raimondi, F Opazo, O Corti, JHM Prehn, S Gambardell, R Melki, V Broccoli Modeling native and seeded Synuclein aggregation and related cellular dysfunctions in dopaminergic neurons derived by a new set of isogenic iPSC lines with SNCA multiplications Cell Death & Disease, 2022-10-19;13(10):881. 2022-10-19 [PMID: 36261424] (Bioassay, Human) Bioassay Human
N Moriarty, CW Gantner, CPJ Hunt, CM Ermine, S Frausin, S Viventi, DA Ovchinniko, D Kirik, CL Parish, LH Thompson A combined cell and gene therapy approach for homotopic reconstruction of midbrain dopamine pathways using human pluripotent stem cells Cell Stem Cell, 2022-02-17;29(3):434-448.e5. 2022-02-17 [PMID: 35180398] (Bioassay, Human) Bioassay Human
C Tang, X Wu, Q Ren, M Yao, S Xu, Z Yan Hedgehog signaling is controlled by Rac1 activity Theranostics, 2022-01-01;12(3):1303-1320. 2022-01-01 [PMID: 35154488] (Bioassay, Mouse) Bioassay Mouse
AM Earley, LF Burbulla, D Krainc, R Awatramani Identification of ASCL1 as a determinant for human iPSC-derived dopaminergic neurons Scientific Reports, 2021-11-15;11(1):22257. 2021-11-15 [PMID: 34782629] (Bioassay, Human) Bioassay Human
de Rus Jacquet A, Tancredi J, Lemire A, DeSantis M, Li W, O'Shea E The LRRK2 G2019S mutation alters astrocyte-to-neuron communication via extracellular vesicles and induces neuron atrophy in a human iPSC-derived model of Parkinson&#039;s disease. Elife, 2021-09-30;10(0):. 2021-09-30 [PMID: 34590578] (Bioassay, Human) Bioassay Human
Show All 62 Publications.

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Bioinformatics

Gene Symbol Shh
Uniprot