|Other Names||Ubiquitin-like modifier-activating enzyme 7, Ubiquitin-activating enzyme 7, D8, Ubiquitin-activating enzyme E1 homolog, UBA7, UBE1L, UBE2|
|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||Activates ubiquitin by first adenylating with ATP its C- terminal glycine residue and thereafter linking this residue to the side chain of a cysteine residue in E1, yielding a ubiquitin- E1 thioester and free AMP. Catalyzes the ISGylation of influenza A virus NS1 protein.|
|Tissue Location||Expressed in a variety of normal and tumor cell types, but is reduced in lung cancer cell lines|
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Provided below are standard protocols that you may find useful for product applications.
The modification of proteins with ubiquitin is animportant cellular mechanism for targeting abnormal or short-livedproteins for degradation. Ubiquitination involves at least threeclasses of enzymes: ubiquitin-activating enzymes, or E1s,ubiquitin-conjugating enzymes, or E2s, and ubiquitin-proteinligases, or E3s. This gene encodes a member of the E1ubiquitin-activating enzyme family. The encoded enzyme is aretinoid target that triggers promyelocytic leukemia (PML)/retinoicacid receptor alpha (RARalpha) degradation and apoptosis in acutepromyelocytic leukemia, where it is involved in the conjugation ofthe ubiquitin-like interferon-stimulated gene 15 protein. [providedby RefSeq].
Fransen, K., et al. Hum. Mol. Genet. 19(17):3482-3488(2010)Morgan, A.R., et al. Hum. Immunol. 71(6):602-609(2010)Feng, Q., et al. Mol. Cancer Ther. 7(12):3780-3788(2008)Durfee, L.A., et al. J. Biol. Chem. 283(35):23895-23902(2008)Takeuchi, T., et al. J. Biochem. 138(6):711-719(2005)
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