|Other Names||NEDD8-conjugating enzyme UBE2F, 632-, NEDD8 carrier protein UBE2F, NEDD8 protein ligase UBE2F, NEDD8-conjugating enzyme 2, Ubiquitin-conjugating enzyme E2 F, UBE2F, NCE2|
|Target/Specificity||The synthetic peptide sequence used to generate the antibody AP1070b was selected from the C-term region of human NCE2. A 10 to 100 fold molar excess to antibody is recommended. Precise conditions should be optimized for a particular assay.|
|Format||The synthetic peptide was lyophilized with 100% acetonitrile and is supplied as a powder. Reconstitute with 0.1 ml deionized 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||Accepts the ubiquitin-like protein NEDD8 from the UBA3- NAE1 E1 complex and catalyzes its covalent attachment to other proteins. The specific interaction with the E3 ubiquitin ligase RBX2, but not RBX1, suggests that the RBX2-UBE2F complex neddylates specific target proteins, such as CUL5.|
|Tissue Location||Widely expressed (at protein level).|
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Provided below are standard protocols that you may find useful for product applications.
Ubiquitin is covalently attached to target proteins by a multienzymatic system consisting of E1 (ubiquitin-activating), E2 (ubiquitin-conjugating), and E3 (ubiquitin-ligating) enzymes. NEDD8, a ubiquitin-like protein, is conjugated to proteins in a manner analogous to ubiquitinylation. beta-amyloid precursor protein-binding protein-1 (APPBP1) can bind to NEDD8 in rabbit reticulocyte lysates. However, since APPBP1 shows similarity to only the N-terminal domain of an E1 enzyme, it must interact with a protein showing similarity to the C-terminal region of E1s. By searching sequence databases, a cDNAs encoding UBA3 was identified as the human homolog of yeast Uba3. The predicted 442-amino acid UBA3 protein shares 43% sequence identity with yeast Uba3. In vitro, UBA3 formed a complex with APPBP1 and a thioester linkage with NEDD8. APPBP1/UBA3 complex may function as an E1-like enzyme for the activation of NEDD8.
Strausberg, R.L., et al., Proc. Natl. Acad. Sci. U.S.A. 99(26):16899-16903 (2002).
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