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U6510

Sigma-Aldrich

Ubiquitin-Specific Protease 5 human

recombinant, expressed in Sf9 cells, ≥51% (SDS-PAGE)

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UNSPSC Code:
12352204
NACRES:
NA.54

recombinant

expressed in Sf9 cells

Quality Level

form

buffered aqueous glycerol solution

mol wt

96 kDa

concentration

≥0.20 mg/mL protein (Bradford)
≥51% (SDS-PAGE)

NCBI accession no.

shipped in

dry ice

storage temp.

−70°C

General description

Human USP5 (Ubiquitin-Specific Protease 5) or Isopeptidase T (isoT), amino acids 2-858 (end) with an N-terminal FLAG-tag, expressed in a baculovirus-infected Sf9 cell expression system.

Application

Useful for the study of enzyme kinetics, screening inhibitors, and selectivity profiling.

Biochem/physiol Actions

The tumor suppressor gene P53 was shown to be a target of ubiquitin-specific protease 5.

Physical form

Solution in 40 mM Tris-HCl, 110 mM NaCl, 2.2 mM KCl, 80 ng/μl Flag peptide, 3 mM DTT, and 20% Glycerol at pH 8.0.

WGK

WGK 1

Flash Point(F)

Not applicable

Flash Point(C)

Not applicable

Regulatory Information

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Francisca E Reyes-Turcu et al.
The Journal of biological chemistry, 283(28), 19581-19592 (2008-05-17)
The conjugation of polyubiquitin to target proteins acts as a signal that regulates target stability, localization, and function. Several ubiquitin binding domains have been described, and while much is known about ubiquitin binding to the isolated domains, little is known
Saurabh Dayal et al.
The Journal of biological chemistry, 284(8), 5030-5041 (2008-12-23)
Both p53 and its repressor Mdm2 are subject to ubiquitination and proteasomal degradation. We show that knockdown of the deubiquitinating enzyme USP5 (isopeptidase T) results in an increase in the level and transcriptional activity of p53. Suppression of USP5 stabilizes

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