|Other Names||Serine/threonine-protein kinase ULK3, Unc-51-like kinase 3, ULK3|
|Target/Specificity||The synthetic peptide sequence used to generate the antibody AP13473b was selected from the C-term region of ULK3. A 10 to 100 fold molar excess to antibody is recommended. Precise conditions should be optimized for a particular assay.|
|Format||Synthetic peptide was lyophilized with 100% acetonitrile and is supplied as a powder. Reconstitute with 0.1 ml DI water for a final concentration of 1 mg/ml.|
|Storage||Maintain refrigerated at 2-8°C for up to 6 months. For long term storage store at -20°C.|
|Precautions||This product is for research use only. Not for use in diagnostic or therapeutic procedures.|
|Function||Serine/threonine protein kinase that acts as a regulator of Sonic hedgehog (SHH) signaling and autophagy. Acts as a negative regulator of SHH signaling in the absence of SHH ligand: interacts with SUFU, thereby inactivating the protein kinase activity and preventing phosphorylation of GLI proteins (GLI1, GLI2 and/or GLI3). Positively regulates SHH signaling in the presence of SHH: dissociates from SUFU, autophosphorylates and mediates phosphorylation of GLI2, activating it and promoting its nuclear translocation. Phosphorylates in vitro GLI2, as well as GLI1 and GLI3, although less efficiently. Also acts as a regulator of autophagy: following cellular senescence, able to induce autophagy.|
|Cellular Location||Cytoplasm. Note=Localizes to pre-autophagosomal structure during cellular senescence|
|Tissue Location||Widely expressed. Highest levels observed in fetal brain. In adult tissues, high levels in brain, liver and kidney, moderate levels in testis and adrenal gland and low levels in heart, lung, stomach, thymus, prostate and placenta. In the brain, highest expression in the hippocampus, high levels also detected in the cerebellum, olfactory bulb and optic nerve. In the central nervous system, lowest levels in the spinal cord|
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Serine/threonine protein kinase which enhances GLI1 and GLI2 transcriptional activity and consequently positively regulates GLI-dependent SHH signaling. May exert this function by promoting GLI1 nuclear localization. Phosphorylates in vitro GLI2, as well as GLI1 and GLI3, although less efficiently.
Maloverjan, A., et al. J. Biol. Chem. 285(39):30079-30090(2010)Takeuchi, F., et al. Circulation 121(21):2302-2309(2010)Maloverjan, A., et al. Exp. Cell Res. 316(4):627-637(2010)Levy, D., et al. Nat. Genet. 41(6):677-687(2009)Kim, D.H., et al. Blood 113(11):2517-2525(2009)
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