di-ubiquitin activity based probe explorer panel

a panel of 7 deubiquitylating enzymes (DUB) activity-based probes based on K6, 11, 27, 29, 33, 48, and 63 linked diUb (10 μg each)

productsheet

Additional information

Weight 0.005 kg
Applications

,

target

source

shipping

purity

molecular weight

storage

Powder at −20°C; solution at −80°C. Please avoid multiple freeze/thaw cycles.

sample preparation

For detailed sample preparation see product sheet.sired.

regulatory statement

aliquot size

Clear
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450.00

Description

UbiQ-L04 contains seven deubiquitylating enzymes (DUB) activity-based probes based on K6, 11, 27, 29, 33, 48, and 63 linked diUb (10 μg each).
These irreversible and specific inhibitors of DUBs can be used for activity-based protein profiling experiments and structural studies.
Please note that the native distance between the proximal and distal Ubiquitin is preserved as much as possible in these new diUb probes, giving rise to less artefact binding compared to the native diUb cleavage profile of DUBs.
For details see product sheets.

Additional information

Weight 0.005 kg
Applications

,

target

source

shipping

purity

molecular weight

storage

Powder at −20°C; solution at −80°C. Please avoid multiple freeze/thaw cycles.

sample preparation

For detailed sample preparation see product sheet.sired.

regulatory statement

aliquot size

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