|Other Names||Ubiquitin-fold modifier 1, UFM1, C13orf20|
|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||Ubiquitin-like modifier which can be covalently attached via an isopeptide bond to substrate proteins as a monomer or a lysine-linked polymer. The so-called ufmylation, requires the UFM1-activating E1 enzyme UBA5, the UFM1-conjugating E2 enzyme UFC1, and the UFM1-ligase E3 enzyme UFL1 (PubMed:15071506, PubMed:20018847). This post-translational modification on lysine residues of proteins may play a crucial role in a number of cellular processes. TRIP4 ufmylation may for instance play a role in nuclear receptors-mediated transcription (PubMed:25219498). Other substrates may include DDRGK1 with which it may play a role in the cellular response to endoplasmic reticulum stress (Probable).|
|Cellular Location||Nucleus. Cytoplasm|
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Provided below are standard protocols that you may find useful for product applications.
UFM1 is a ubiquitin-like protein that is conjugated totarget proteins by E1-like activating enzyme UBA5 (UBE1DC1; MIM610552) and E2-like conjugating enzyme UFC1 (MIM 610554) in amanner analogous to ubiquitylation (see UBE2M; MIM 603173).
Tatsumi, K., et al. J. Biol. Chem. 285(8):5417-5427(2010)Ewing, R.M., et al. Mol. Syst. Biol. 3, 89 (2007) :Sasakawa, H., et al. Biochem. Biophys. Res. Commun. 343(1):21-26(2006)Komatsu, M., et al. EMBO J. 23(9):1977-1986(2004)Dunham, A., et al. Nature 428(6982):522-528(2004)
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