Catalog number: SBB-UP0061, 25 μg
This K6 linked tetra-ubiquitin was recombinantly expressed in E. coli, enzymatically conjugated, and purified via liquid chromatography.
The array of cellular processes initiated and regulated by ubiquitin has been partially explained by the structural diversity of differently linked ubiquitin chains. In a ubiquitin chain, ubiquitin moieties can be conjugated through one of their lysine residues (K6, K11, K27, K29, K33, K48 and K63) or the N-terminal methionine residue (M1), offering countless possibilities to assemble a specific polymer. Ubiquitin molecules can also be modified by other post-translational modifications, including acetylation and phosphorylation, adding another layer of ubiquitin signal regulation and diversification. K6 linked ubiquitin linkages are found at increased levels in response to UV radiation, indirectly associated with DNA repair, and have been identified on mitochondrial outer membrane (MOM) proteins. This K6 linked tetra-ubiquitin was recombinantly expressed in E. coli, enzymatically conjugated, and purified via liquid chromatography.
For Research Use Only, Not For Use In Humans.
|Molecular Weight:||34 kDa|
|Purity:||>95% by SDS-PAGE|
|Storage Buffer:||50 mM HEPES pH 7.5|
|Storage||Store at −80°C after product arrival. Avoid multiple freeze / thaws. It is recommended to make multiple aliquots after the first thaw.|
Figures & Data
K6-Linked Tetra-Ubiquitin, human recombinant
Figure 1. K6-Linked Tetra-Ubiquitin, SDS-PAGE From left to right, increasing amounts of tetra-ubiquitin loaded onto a 10-20% SDS-PAGE gel, stained with coomassie brillant blue. Purity is > 95%.
Certificates of Analysis (COA)
Citations & References
1) Dikic, I., Wakatsuki, S., & Walters, K. J. (2009). Ubiquitin-binding domains — from structures to functions. Nature Reviews Molecular Cell Biology, 10(10), 659–671. https://doi.org/10.1038/nrm2767
2) Akutsu, M., Dikic, I., & Bremm, A. (2016). Ubiquitin chain diversity at a glance. Journal of Cell Science, 129(5), 875–880. https://doi.org/10.1242/jcs.183954