|Other Names||E3 UFM1-protein ligase 1, 632-, LZAP-binding protein, UFL1, KIAA0776, NLBP|
|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||E3 protein ligase that mediates ufmylation, the covalent attachment of the ubiquitin-like modifier UFM1 to substrate proteins, a post-translational modification on lysine residues of proteins that may play a crucial role in a number of cellular processes. Mediates DDRGK1 ufmylation and may regulate the proteasomal degradation of DDRGK1 and CDK5RAP3 thereby modulating NF-kappa-B signaling (PubMed:20018847, PubMed:20164180, PubMed:20228063, PubMed:25219498). May also through TRIP4 ufmylation play a role in nuclear receptors-mediated transcription (PubMed:25219498). May play a role in the unfolded protein response, mediating the ufmylation of multiple proteins in response to endoplasmic reticulum stress (PubMed:23152784).|
|Cellular Location||Endoplasmic reticulum. Cytoplasm, cytosol|
|Tissue Location||Ubiquitously expressed, with a high expression in liver (at protein level). Low expression in several invasive hepatocellular carcinomas, such Hep-G2, Hep 3B2.1-7, HLE and PLC|
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Provided below are standard protocols that you may find useful for product applications.
Kwon, J., et al. J. Biol. Chem. 285(16):12232-12240(2010)Ewing, R.M., et al. Mol. Syst. Biol. 3, 89 (2007) :Olsen, J.V., et al. Cell 127(3):635-648(2006)Beausoleil, S.A., et al. Proc. Natl. Acad. Sci. U.S.A. 101(33):12130-12135(2004)Beausoleil, S.A., et al. Proc. Natl. Acad. Sci. U.S.A. 101(33):12130-12135(2004) Mungall, A.J., et al. Nature 425(6960):805-811(2003)
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