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Octa-dimethyl-ubiquitin: (CH3)2-MQIFVK*TLTGK*TITLEVEPSDTIENV K*AK*IQDK*EGIPPDQQRLIFAGK*QLEDGR TLSDYNIQK*ESTLHLVLRLRGG-OH where K* = (ε-dimethyl)lysyl.
Reductive methylation of the seven internal lysine ε-amino groups as well as the α-amino group to give, in this case, the octa-dimethyl derivative renders ubiquitin unable to form multi-ubiquitin chains via lysine linkages. However, the ability of this methylated ubiquitin to form an active C-terminal thioester is preserved and it may be transferred by ubiquitin-activating and conjugating enzymes (E1 and E2s) to lysine residues within substrate proteins to yield monoubiquitinylated products.
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SDS-PAGE Analysis: Lane 1: MW Marker, Lane 2: 0.5 μg, Lane 3: 1.0 μg, Lane 4: 2.0 μg, Lane 5: 5.0 μg of Purified Ubiquitin (methylated) (bovine), (native) (Prod. No. BML-UW8555).
Mass spectrum analysis by electrospray ionization mass spectrometry, (see image) indicates the octa-dimethylated ubiquitin molecular weight at 8790 Da (± 1.6 Da), doubly charged species present at 6671.7 Da. This is fully consistent with the anticipated molecular weight, given that for parent ubiquitin a molecular weight of 8565.4 Da (± 1.6 Da) is observed under identical conditions. There is no un-derivatized ubiquitin present. The signal observed at 8675.3 Da is attributable to a minor contaminant in the starting ubiquitin and is not due to the presence of octa-monomethylated ubiquitin. All other minor signals observed are at background level and are not indicative of protein artifacts.
| Regulatory Status |
RUO – Research Use Only |
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