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UBIQUITIN RESEARCH TOOLS

Ubiquitin (Ub), a small (76 amino acids) polypeptide, is highly conserved among all living eukaryotes. Ubiquitin is covalently attached to cellular proteins and can regulate the levels, activity and localization of these proteins. Several ubiquitin-like proteins have been identified including SUMO, NEDD8 and ISG15. All of these UBLs utilize a similar mechanism for conjugation to target proteins. Briefly, energy is required to activate ubiquitin at its carboxy terminus; activation is catalysed by E1, which binds the Ub C-terminus to a side chain cysteine of the enzyme. The second enzyme of the series, E2 (called the ubiquitin conjugating protein), receives Ub as a thioester (Ub-CO-S-E1 - Ub-CO-S-E2); E2 then transfers Ub to a target polypeptide, which is bound to the third enzyme in the sequence, called E3, or Ubiquitin ligase. Thus, the E3 primarily determines the specificity of ubiquitination. Poly-Ub chains can be formed via linkage of another Ub moiety to lysine 48 of the previous Ub protein. Other lysines may also serve as linkage sites in chain formation including lysine 63. It is important to note that not every Ub attachment results in formation of a poly-Ub tag. Attachment of a single Ub moiety to its target protein can modulate activity or localization. Ubiquitin is cleaved from substrates by deubiquitinating enzymes (also called ubiquitin hydrolases or ubiquitin isopeptidases). Isopeptidases are a family of cysteine proteases that specifically cleave ubiquitin-derived substrates of the general structure ubiquitin-X, where X = any number of leaving groups ranging from small thiols and amines to ubiquitin and other proteins. Thus, isopeptidases act to reverse the modification of proteins by ubiquitin or ubiquitin-like proteins. Modulation of cellular processes can be controlled by regulating protein ubiquitination via modulation of E3 ligase and isopeptidase activity.

Fig 1. Ubiquitin conjugation pathway. Protein modification by ubiquitin requires sequential action of three enzymes: Ubiquitin activated by a specific activating enzyme (E1) to form a Ub-E1-thiolester. Activated Ub is transferred to a carrier protein or 'conjugase' E2, and then transferred to a ligase (E3) and linked via isopeptide bond to a lysine residue on the substrate protein. After linkage of Ub to the substrate, a polyUb chain can be formed in some cases. Ubiquitinated proteins can be deubiquitinated by specific isopeptidases.

LifeSensors has the largest collection of ubiquitin research tools commercially available for studying the enzymes involved in this complex pathway. Using these tools scientists will be able to characterize enzyme function, identify substrates, discover modulators of this pathway, and make scientific breakthroughs that will deepen our understanding of the ubiquitin pathway.

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LifeSensors presented an overview of ubiquitin proteomics at the 3rd GTC Conference, Ubiquitin Research and Drug Discovery, Las Vegas, February 25-26th, 2013.
Complexity of ubiquitin pathways leads to frequent questions related to identification of ubiquitin pathway enzymes (E3s and DUBs) and their substrates. An overview of biochemical proteomics for drug discovery applications including Ubiquitin Protein Microarray Services from LifeSensors was presented by Christian Loch, Assistant Director, R&D. Visit our website to find additional information about our Ubiquitin Protein Microarrays.
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LifeSensors Inc. appointed 4A Biotech Co.Ltd as another distributor of its innovative reagents and technologies in China
Located at Guanglian Industrial Park, Beijing, 4A Biotech Co.Ltd. is a leading life science product provider in China.
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LifeSensors presents data at FASEB's Ubiquitin & Cellular Regulation meeting June 24th-29th.
Download PDFs of poster #54 "Effect of DUB inhibitor PR-619 on the microtubule network and protein aggregate formation in oligodendroglial cells: Implications for neurodegeneration" and poster #61 "Decoding the information content of ubiquitin chains: Application of linkage-specific TUBES to the ubiquitome" from our Technical Documentation page (bottom of the page).
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