Recombinant Human Sonic Hedgehog/Shh, N-Terminus Protein

Newer Version Available: 8908-SH-005
A New rh Shh is Available! C-term cholesterol, N-term fatty acid-modified; 250-fold activity!
Formulations:
Catalog # Availability Size / Price Qty
1314-SH-025
Recombinant Human Sonic Hedgehog/Shh, N-Terminus Protein Bioactivity
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Product Details
Citations (9)
FAQs
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Recombinant Human Sonic Hedgehog/Shh, N-Terminus Protein Summary

Purity
>97%, by SDS-PAGE with silver staining, under reducing conditions
Endotoxin Level
<0.10 EU per 1 μg of the protein by the LAL method.
Activity
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 <5 µg/mL.
Source
E. coli-derived human Sonic Hedgehog/Shh protein
Cys24-Gly197, with a C-terminal 6-His tag
Accession #
N-terminal Sequence
Analysis
Cys24
Predicted Molecular Mass
20 kDa
SDS-PAGE
22 kDa, reducing conditions

Product Datasheets

Carrier Free

What does CF mean?

CF stands for Carrier Free (CF). We typically add Bovine Serum Albumin (BSA) as a carrier protein to our recombinant proteins. Adding a carrier protein enhances protein stability, increases shelf-life, and allows the recombinant protein to be stored at a more dilute concentration. The carrier free version does not contain BSA.

What formulation is right for me?

In general, we advise purchasing the recombinant protein with BSA for use in cell or tissue culture, or as an ELISA standard. In contrast, the carrier free protein is recommended for applications, in which the presence of BSA could interfere.

1314-SH

Formulation Lyophilized from a 0.2 μm filtered solution in NaH2PO4, NaCl and DTT with BSA as a carrier protein.
Reconstitution Reconstitute at 100 μg/mL in sterile PBS containing at least 0.1% human or bovine serum albumin.
Shipping The product is shipped at ambient temperature. Upon receipt, store it immediately at the temperature recommended below.
Stability & 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.

1314-SH/CF

Formulation Lyophilized from a 0.2 μm filtered solution in NaH2PO4, NaCl and DTT.
Reconstitution Reconstitute at 100 μg/mL in PBS.
Shipping The product is shipped at ambient temperature. Upon receipt, store it immediately at the temperature recommended below.
Stability & 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.

Data Images

Bioactivity Recombinant Human Sonic Hedgehog/Shh, N-Terminus Protein Bioactivity View Larger

Recombinant Human Sonic Hedgehog/Shh, N-Terminus (Catalog # 1314-SH) induces alkaline phosphatase production by the C3H10T1/2 mouse embryonic fibroblast cell line. The ED50 for this effect is 5 μg/mL.

SDS-PAGE Recombinant Human Sonic Hedgehog/Shh, N-Terminus Protein SDS-PAGE View Larger

1 μg/lane of Recombinant Human Sonic Hedgehog/Shh, N-Terminus was resolved with SDS-PAGE under reducing (R) conditions and visualized by silver staining, showing a single band at 22 kDa.

Reconstitution Calculator

Reconstitution Calculator

The reconstitution calculator allows you to quickly calculate the volume of a reagent to reconstitute your vial. Simply enter the mass of reagent and the target concentration and the calculator will determine the rest.

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Background: Sonic Hedgehog/Shh

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). Human Shh encodes a 462 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).

References
  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. Marigo, V. et al. (1995) Genomics 28:44.
  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.
Entrez Gene IDs
6469 (Human); 20423 (Mouse)
Alternate Names
HHG1; HHG-1; HLP3; HPE3; MCOPCB5sonic hedgehog (Drosophila) homolog; Shh; SMMCIsonic hedgehog homolog (Drosophila); sonic hedgehog homolog; sonic hedgehog protein; Sonic Hedgehog; TPT; TPTPS

Citations for Recombinant Human Sonic Hedgehog/Shh, N-Terminus Protein

R&D Systems personnel manually curate a database that contains references using R&D Systems products. The data collected includes not only links to publications in PubMed, but also provides information about sample types, species, and experimental conditions.

9 Citations: Showing 1 - 9
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  1. Comparative Analysis of Spontaneous and Stimulus-Evoked Calcium Transients in Proliferating and Differentiating Human Midbrain-Derived Stem Cells
    Authors: T Johansen, C Krabbe, SI Schmidt, AM Serrano, M Meyer
    Stem Cells Int, 2017;2017(0):9605432.
    Species: Human
    Sample Types: Whole Cells
    Applications: Bioassay
  2. Ex vivo analysis of the contribution of FGF10(+) cells to airway smooth muscle cell formation during early lung development
    Authors: E El Agha, V Kheirollah, A Moiseenko, W Seeger, S Bellusci
    Dev. Dyn., 2017;0(0):.
    Species: Mouse
    Sample Types: Whole Cells
    Applications: Bioassay
  3. Inhibition of the Hedgehog pathway induces autophagy in pancreatic ductal adenocarcinoma cells.
    Authors: Xu Y, An Y, Wang X, Zha W, Li X
    Oncol Rep, 2014;31(2):707-12.
    Species: Human
    Sample Types: Whole Cells
    Applications: Bioassay
  4. The hedgehog system in ovarian follicles of cattle selected for twin ovulations and births: evidence of a link between the IGF and hedgehog systems.
    Authors: Aad, Pauline, Echternkamp, Sherrill, Sypherd, David D, Schreiber, Nicole B, Spicer, Leon J
    Biol Reprod, 2012;87(4):79.
    Species: Bovine
    Sample Types: Whole Cells
    Applications: Bioassay
  5. Derivation of cerebellar neurons from human pluripotent stem cells.
    Authors: Erceg S, Lukovic D, Moreno-Manzano V, Stojkovic M, Bhattacharya S
    Curr Protoc Stem Cell Biol, 2012;20(0):1H.51.
    Species: Human
    Sample Types: Whole Cells
    Applications: Bioassay
  6. Vitronectin promotes oligodendrocyte differentiation during neurogenesis of human embryonic stem cells.
    Authors: Gil JE, Woo DH, Shim JH, Kim SE, You HJ, Park SH, Paek SH, Kim SK, Kim JH
    FEBS Lett., 2009;583(3):561-7.
    Species: Human
    Sample Types: Whole Cells
    Applications: Bioassay
  7. Human ES cell-derived neural rosettes reveal a functionally distinct early neural stem cell stage.
    Authors: Elkabetz Y, Panagiotakos G, Al Shamy G, Socci ND, Tabar V, Studer L
    Genes Dev., 2008;22(2):152-65.
    Species: Human
    Sample Types: Whole Cells
    Applications: Bioassay
  8. Reduced pepsin A processing of sonic hedgehog in parietal cells precedes gastric atrophy and transformation.
    Authors: Zavros Y, Waghray M, Tessier A, Bai L, Todisco A, L Gumucio D, Samuelson LC, Dlugosz A, Merchant JL
    J. Biol. Chem., 2007;282(46):33265-74.
    Species: N/A
    Sample Types: N/A
    Applications: SDS-page
  9. An early role for WNT signaling in specifying neural patterns of Cdx and Hox gene expression and motor neuron subtype identity.
    Authors: Nordstrom U, Maier E, Jessell TM, Edlund T
    PLoS Biol., 2006;4(8):e252.
    Species: Chicken
    Sample Types: Whole Tissue
    Applications: Bioassay

FAQs

  1. What is the difference between Recombinant Human Sonic Hedgehog Catalog # 1845-SH and Catalog # 1314-SH?

    • Recombinant Human Sonic Hedgehog, Catalog # 1845-SH, possesses a N-terminal mutation that increases its potency in bioassay tests. The amino acid sequence is Cys24-Gly197 (Cys24Ile-Ile), accession number NP_000184. The Cys24Ile-Ile mutation was created to match a publication that describes enhanced activity with these modifications: "http://www.ncbi.nlm.nih.gov/pubmed/11284692". Catalog # 1314-SH does not possess this mutation.

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