|Catalog Number||Size||Price (USD)||Shopping Cart|
|PR15000||25 ug||$255.00||Buy Now | Add to Cart|
|PR15000CF||25 ug||$255.00||Buy Now | Add to Cart|
Hedgehog (Hh) proteins are widely distributed throughout the animal kingdom and play important regulatory roles in various development processes. The three known mammalian Hh proteins, Sonic (Shh), Desert (Dhh) and Indian (Ihh) are structurally related and share a high degree of amino acid sequence identity (e.g. Shh and Ihh are 93 % identical). Although, Hh proteins have unique expression patterns and distinct biological roles within their respective regions of secretion, they signal through the same Patched (Ptc)/Smoothened (Smo) receptor complex, activate the same intracellular signaling pathway, and can substitute for each other in experimental systems. The mature biologically active form of Hh molecules is produced by autocatalytic cleavage of their precursor proteins and corresponds to approximately the N-terminal half of the precursor molecule. Recombinant human Shh is a 20.6 kDa protein consisting of 174 amino acid residues, which correspond to the active N-terminal portion of the Shh precursor.
Figure: in vitro relative cell proliferation assay in renal cell carcinoma cell lines in RenCa (Panel A) and ACNH cells (Panel B) treated with dimethyl sulfoxide. Only RenCa cells showed that Cy blocked cell proliferation enhanced by r-Shh treatment. ACNH cells did not show any inhibiting effect of Cy on cell proliferation. Cell proliferation of V was set as 1.0. The treatments were performed for 48 hours. Each point represents triplicate averages±standard deviation or ON. Asterisks show significant cell proliferations compared with V. V, vehicle-treated control; S, recombinant sonic hedgehog (r-Shh) protein (1 µg/mL); Cy, cyclopamine (5 µM). Korean J Urol. 2013 Aug;54(8):547-554. http://dx.doi.org/10.4111/kju.2013.54.8.547
A DNA sequence encoding amino acid residues Cys 25 - Gly 198 of mouse Shh (Echelard, Y. et al., 1993, Cell 75:1417 - 1430) was fused to a 6X histidine tag at the carboxy-terminus. The fusion protein was expressed in E. coli.