K11 diUb-VME

a potent, irreversible and specific inhibitor of deubiquitylating enzymes (DUBs) based on K11 linked diUb

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Weight 0.05 kg
aliquot size

Applications

, , , ,

target

source

shipping

purity

molecular weight

storage

Powder at −20°C, solution at −80°C.

sample preparation

For detailed sample preparation see product sheet.

regulatory statement

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300.00

Description

UbiQ-082 (K11 linked diUbiquitin VME) is a potent, irreversible and specific inhibitor of deubiquitylating enzymes (DUBs) based on K11 linked diUb.
This DUB activity based probe can be used for activity profiling experiments and structural studies. Lys11 has been replaced by a diaminobutyric acid(vinylamide) residue as reactive mimic of the native isopeptidic linked Lys(Gly) residue.
Please note the native distance between the proximal and distal Ubiquitin is preserved as much as possible in our diUbiquitin probe.

Additional information

Weight 0.05 kg
aliquot size

Applications

, , , ,

target

source

shipping

purity

molecular weight

storage

Powder at −20°C, solution at −80°C.

sample preparation

For detailed sample preparation see product sheet.

regulatory statement

Misaghi, S., et al. Structure of the Ubiquitin Hydrolase UCH-L3 Complexed with a Suicide Substrate. J. Biol. Chem. 280, 1512-1520 (2005).
http://www.ncbi.nlm.nih.gov/pubmed/15531586

de Jong, A., et al. Ubiquitin-based probes prepared by total synthesis to profile the activity of deubiquitinating enzymes. ChemBiochem 13, 2251-2258 (2012).
http://www.ncbi.nlm.nih.gov/pubmed/23011887

Altun, M., et al. Activity-based chemical proteomics accelerates inhibitor development for deubiquitylating enzymes. Chem. Biol. 18, 1401-1412 (2011).
http://www.ncbi.nlm.nih.gov/pubmed/22118674

Mulder, M.P., et al. A native chemical ligation handle that enables the synthesis of advanced activity-based probes: diubiquitin as a case study. ChemBiochem 15, 946-949 (2014).
http://www.ncbi.nlm.nih.gov/pubmed/24623714

Haj-Yahya, N., et al. Dehydroalanine-based diubiquitin activity probes. Org. Lett. 16, 540-543 (2014).
http://www.ncbi.nlm.nih.gov/pubmed/24364494

Li, G., et al. Activity-based diubiquitin probes for elucidating the linkage specificity of deubiquitinating enzymes. Chem. Commun. 20, 216-218 (2014).
http://www.ncbi.nlm.nih.gov/pubmed/24225431

Iphöfer, A., et al. Profiling ubiquitin linkage specificities of deubiquitinating enzymes with branched ubiquitin isopeptide probes. Chembiochem 13, 1416-1420 (2012).
http://www.ncbi.nlm.nih.gov/pubmed/22689415

McGouran, J.F., et al. Deubiquitinating enzyme specificity for ubiquitin chain topology profiled by di-ubiquitin activity probes. Chem. Biol. 20, 1447-1455 (2013).
http://www.ncbi.nlm.nih.gov/pubmed/24290882