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Ubiquitin/Ubl Isopeptidases

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DUBs are a class of isopeptidases that cleave ubiquitin from target proteins, including other ubiquitins. Other classes of isopeptidases perform the same function for ubiquitin-like proteins fused to their target proteins. Both conjugation and deconjugation of ubiquitin or ubiquitin-like proteins (UBLs) contribute to the maintenance of cellular homeostasis, the disruption of which can lead to disease. Accordingly, DUBs and UBL isopeptidases have been found to be overexpressed or dysregulated in a number of pathophysiologies [Nicholson et al, 2007]. Inhibition (or, in some cases, activation) of DUBs represents a novel, underexploited form of therapeutic intervention, and efforts are underway to discover or design inhibitors and activators of these enzymes that can be developed as medicines [Berlin, Tenarife meeting abstracts, 2008, Keystone meeting, 2009].

LifeSensors has the largest collection of deubiquitylases (DUBs) commercially available. These enzymes can be utilized for high throughput screening or determining which enzymes recognize a given ubiquitylated substrate.

 

Our DUBs are in liquid format, in 25 µg size. Please inquiry for bulk quantities, or for access to non-listed DUBs.

 

USP FAMILY OF DUBS
UCH FAMILY OF DUBS
OTU FAMILY OF DUBS
JAMM FAMILY OF DUBS
MJD FAMILY OF DUBS
VIRAL-BACTERIAL DUBS
DENEDDYLASES
DESUMOYLASES

 

USP FAMILY OF DUBS

The USP class is the largest and most diverse class of DUBs present in the human genome. The catalytic domain of a USP consists of a Cys box and a His box which may be separated by 300-800 amino acids. USPs typically cleave ubiquitin conjugates from mono or polyubiquitinylated protein substrates. Aberrant regulation of USPs has been implicated in neoplastic disease.

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UCH FAMILY OF DUBS

Biochemical and structural studies have suggested that the UCH class of DUBs preferentially cleave relatively small protein substrates from ubiquitin. The primary functions of UCH enzymes include the processing of newly synthesized ubiquitin and the recycling of ubiquitin inappropriately conjugated to intracellular nucleophiles.

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OTU FAMILY OF DUBS

The OTU family was discovered by a bioinformatics approach using the otu gene that is expressed in the Drosophilia melanogaster ovary as a starting point. The structure of one of the OTU family members, OTUB2 revealed that in contrast to other DUBs the catalytic triad of OTUB2 differs in that it is stabilized by a alternative hydrogen bonding network.

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JAMM FAMILY OF DUBS

JAMM-DUB specifically disassembles K63-linked ubiquitin chains

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MJD FAMILY OF DUBS

The MJD class is characterized by a Josephin domain. Whilst sequence similarity between the best known example of the MJDs, Ataxin 3 and other classes of DUBs is low, structural studies show that the spatial arrangement of the catalytic triad is preserved.

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VIRAL-BACTERIAL DUBS

A number of viral and bacterial pathogens express Ub/Ubl-isopeptidases that may be required for evasion of the host cell immune response.

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DENEDDYLASES

DEN1 (SENP8, NEDP1) is a deNEDDylase that deconjugates NEDD8 conjugates. A recent study demonstrated that DEN1 deNEDDylated the tumor suppressor breast cancer-associated protein BCA3. Full length DEN1 cleaves NEDD8-PLA2 with high efficiency.

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DESUMOYLASES

Mammalian deSUMOylases (SENPs) are cysteine proteases that process pro-small ubiquitin-related modifier (SUMOs) and cleave isopeptide bonds between SUMO and proteins. The Saccharomyces cerevisiae SUMO ortholog Smt3 is cleaved by the SENP homologs Ulp1 and Ulp2.

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