USP5, Active, Recombinant, Human, FLAG-Tag (Ubiquitin Carboxyl-terminal Hydrolase 5, Ubiquitin Thiolesterase 5, Ubiquitin-specific Processing Protease 5, Deubiquitinating Enzyme 5, Isopeptidase T, ISOT)

Catalog No : USB-137397
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Product name USP5, Active, Recombinant, Human, FLAG-Tag (Ubiquitin Carboxyl-terminal Hydrolase 5, Ubiquitin Thiolesterase 5, Ubiquitin-specific Processing Protease 5, Deubiquitinating Enzyme 5, Isopeptidase T, ISOT)
Catalog No USB-137397
Supplier’s Catalog No 137397
Supplier US Biologicals
Source antigen Recombinant, Sf9 insect cells
Reactivity
Cross reactivity
Applications
Molecular weight 96
Storage -70°C
Other names
Grade Purified
Purity Purified (~55%)
Form Supplied as a liquid in 45mM Tris-HCl, pH 8.0, 124mM sodium chloride, 2.4mM potassium chloride, 10% glycerol, 3mM DTT, 90ug/ml FLAG peptide.
Reactivity life 6 months
Note For reserch purpose only
Purity Purified (~55%)
Description USP5 cleaves linear and branched multiubiquitin polymers with a marked preference for branched polymers. It’s involved in unanchored 'Lys-48'-linked polyubiquitin disassembly. It binds linear and 'Lys-63'-linked polyubiquitin with a lower affinity. Knock-down of USP5 causes the accumulation of p53/TP53 and an increase in p53/TP53 transcriptional activity because the unanchored polyubiquitin that accumulates is able to compete with ubiquitinated p53/TP53 but not with MDM2 for proteasomal recognition. Source: Recombinant corresponding to aa2-858 from human USP5, fused to FLAG-tag at N-terminal, expressedin Sf9 insect cells via a baculovirus expression system. Molecular Weight: ~96kD Applications: Suitable for for the study of enzyme kinetics, screening inhibitors, and selectivity profiling. Other applications not tested. Recommended Dilution: Optimal dilutions to be determined by the researcher. Storage and Stability: Aliquot to avoid repeated freezing and thawing and store at -70°C. Aliquots are stable for 6 months. For maximum recovery of product, centrifuge the original vial after thawing and prior to removing the cap.