Ubiquitin, human recombinant

Catalog number: SBB-UP0013,10 mg

Ubiquitin is a small (8.5 kDa) regulatory protein that has been found in almost all tissues of eukaryotic organisms. The addition of ubiquitin to a substrate protein is called ubiquitination or ubiquitylation. Ubiquitination can affect proteins in many ways: it can signal for their degradation via the proteasome, alter their cellular location, affect their activity, and promote or prevent protein interactions. [1][2][3][4][5]

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Ubiquitin is a 76 amino acid post-translational modifier expressed throughout all tissues in eukaryotic organisms. The many roles of ubiquitin modification include proteasomal degradation, signal transduction, inflammatory response, and DNA damage repair. Ubiquitin modification occurs through a pyramidal cascade of an E1 activating enzyme, E2 conjugating enzymes, and an E3 ubiquitin ligases. This enzymatic cascade results in modification of a ɜ-amine of a lysine reside on a substrate protein. Substrates may either be mono or poly-ubiquitinated by M1, K6, 11, 27, 29, 33, 48 or 63 linkages. Removal of ubiquitin from a substrate protein occurs via deconjugating enzymes, of which there are nearly 100 known enzymes with various linkage specificities. This product consists of a full-length human, mature ubiquitin polypeptide (amino acids 1-76), expressed in E.coli. Typical working concentrations range from 250 to 750 µM.

For Research Use Only, Not For Use In Humans.


Product Overview
Quantity: 10 mg
Molecular Weight: 8.6 kDa
Purity: >99% by SDS-PAGE
Substrate Properties: Typical working concentrations range from 250 to 750 µM.
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

Ubiquitin, human recombinant

Figure 1. Ubiquitin, SDS-PAGE From left to right, increasing amounts of ubiquitin loaded onto a 16% SDS-PAGE gel, stained with coomassie blue.

Citations & References

1) Glickman MH, Ciechanover A (Apr 2002). "The ubiquitin-proteasome proteolytic pathway: destruction for the sake of construction". Physiological Reviews. 82 (2): 373–428.doi:10.1152/physrev.00027.2001. PMID 11917093.

2) Mukhopadhyay D, Riezman H (Jan 2007). "Proteasome-independent functions of ubiquitin in endocytosis and signaling".Science. 315 (5809): 201–5. doi:10.1126/science.1127085.PMID 17218518.

3) Schnell JD, Hicke L (Sep 2003). "Non-traditional functions of ubiquitin and ubiquitin-binding proteins". The Journal of Biological Chemistry. 278 (38): 35857–60. doi:10.1074/jbc.R300018200.PMID 12860974.

4) Huang F., Kirkpatrick D., Jiang X., Gygi S.P., Sorkin A. “Differential regulation of EGF receptor internalization and degradation by multiubiquitination within the kinase domain.” Mol. Cell 21:737-748(2006)

5) Komander D. “The emerging complexity of protein ubiquitination.”Biochem. Soc. Trans. 37:937-953(2009)