||Recombinant Human Ubiquitin Bexpressed inE.coliwas cloned from human cDNA. The protein consists of the human ubiquitin (residues 1-76, swissprot accession P62988) and of 6 c-terminal additional histidines. MW= 9.4 kDa.
||Ubiquitin is a small, highly-conserved regulatory protein that is ubiquitously expressed in eukaryotes. Ubiquitination (or ubiquitylation) refers to the post-translational modification of a protein by the covalent attachment (via an isopeptide bond) of one or more ubiquitin monomers. The most prominent function of ubiquitin is labeling proteins for proteasomal degradation. Besides this function, ubiquitination also controls the stability, function, and intracellular localization of a wide variety of proteins. The ubiquitylation (or ubiquitination) cascade is started by the E1 enzyme.
||>95% by SDS-PAGE. The protein was observed as a single band migrating at a molecular weight <10 kDa.
||Freeze-dried from pure water.
||Solution at conc. up to 2mM of protein in 50mM Phosphate buffer, pH 7, 0.02% NaN3, 10% D2O, in NMR tube (high quality) sealed under inert atmosphere. Total sample volume 550ul. The concentration is calculated from the absorbance at 280nm (e280 = 1490 M-1 cm-1).
||15N, 13C, 2H in any combination. Selective labeling of some aminoacids is available on request.
||Under the above described conditions, to avoid precipitation or protein dimerization, the product can be concentrated to a maximum concentration of 2mM.
||The protein is stable at 4 ºC for months and at 25 ºC for at least two weeks. Avoid repeated freeze/defrost cycles./defrost cycles.