USP11 Protein, Human (sf9)

The USP11 protein is a multifunctional protease that selectively removes ubiquitin from target proteins and polyubiquitin chains, thereby hindering their proteasomal degradation. It shows a preference for “Lys-6” and “Lys-63” linked ubiquitin chains and less activity towards other linkages. USP11 Protein, Human (sf9) is the recombinant human-derived USP11 protein, expressed by sf9 insect cells , with tag free.

USP11 protein functions as a protease with the capability to remove conjugated ubiquitin from target proteins and polyubiquitin chains, inhibiting their degradation by the proteasome. Exhibiting a preference for 'Lys-6' and 'Lys-63'-linked ubiquitin chains, USP11 shows lower activity towards 'Lys-11' and 'Lys-33'-linked chains, and minimal activity with 'Lys-27', 'Lys-29', and 'Lys-48'-linked chains in vitro. Beyond its proteolytic role, USP11 is integral to the regulation of pathways leading to NF-kappa-B activation and plays a crucial role in DNA repair following double-stranded DNA breaks. Additionally, it acts as a chromatin regulator through association with the Polycomb group (PcG) multiprotein PRC1-like complex, potentially by deubiquitinating components of this complex. USP11's involvement in cell proliferation is highlighted by its ability to deubiquitinate phosphorylated E2F1, further emphasizing its multifaceted role in cellular processes.

The fundamental role of USP11 is specific removal of ubiquitin from substrates. USP11 catalyses the ubiquitin from the substrate Ub-Rho110 to release fluorophores. Rho110 will release 535 nM emission light under the excitation condition of 485 nM. The signal of which can be quickly and reliably captured using a microplate reader.

Human

Sf9 insect cells

Tag Free

P51784 (A2-N963)

/

Partial

AVAPRLFGGLCFRFRDQNPEVAVEGRLPISHSCVGCRRERTAMATVAANPAAAAAAVAAAAAVTEDREPQHEELPGLDSQWRQIENGESGRERPLRAGESWFLVEKHWYKQWEAYVQGGDQDSSTFPGCINNATLFQDEINWRLKEGLVEGEDYVLLPAAAWHYLVSWYGLEHGQPPIERKVIELPNIQKVEVYPVELLLVRHNDLGKSHTVQFSHTDSIGLVLRTARERFLVEPQEDTRLWAKNSEGSLDRLYDTHITVLDAALETGQLIIMETRKKDGTWPSAQLHVMNNNMSEEDEDFKGQPGICGLTNLGNTCFMNSALQCLSNVPQLTEYFLNNCYLEELNFRNPLGMKGEIAEAYADLVKQAWSGHHRSIVPHVFKNKVGHFASQFLGYQQHDSQELLSFLLDGLHEDLNRVKKKEYVELCDAAGRPDQEVAQEAWQNHKRRNDSVIVDTFHGLFKSTLVCPDCGNVSVTFDPFCYLSVPLPISHKRVLEVFFIPMDPRRKPEQHRLVVPKKGKISDLCVALSKHTGISPERMMVADVFSHRFYKLYQLEEPLSSILDRDDIFVYEVSGRIEAIEGSREDIVVPVYLRERTPARDYNNSYYGLMLFGHPLLVSVPRDRFTWEGLYNVLMYRLSRYVTKPNSDDEDDGDEKEDDEEDKDDVPGPSTGGSLRDPEPEQAGPSSGVTNRCPFLLDNCLGTSQWPPRRRRKQLFTLQTVNSNGTSDRTTSPEEVHAQPYIAIDWEPEMKKRYYDEVEAEGYVKHDCVGYVMKKAPVRLQECIELFTTVETLEKENPWYCPSCKQHQLATKKLDLWMLPEILIIHLKRFSYTKFSREKLDTLVEFPIRDLDFSEFVIQPQNESNPELYKYDLIAVSNHYGGMRDGHYTTFACNKDSGQWHYFDDNSVSPVNENQIESKAAYVLFYQRQDVARRLLSPAGSSGAPASPACSSPPSSEFMDVN

≥ 85%, as determined by reducing SDS-PAGE.

Solution

Supplied as a 0.22 μm filtered solution of 50 mM Tris-HCl, pH 7.5, 200 mM NaCl, 20% glycerol or 50 mM Tris-HCl, pH 7.5, 150 mM NaCl, 5% glycerol, 2 mM DTT.
Note: For SPR assay, please replace the buffer. Primary amine components (e.g., Tris, imidazole) can affect protein-coupled chips.

<1 EU/μg, determined by LAL method.

Please use rapid thawing with running water to thaw the protein.

Stored at -80°C for 1 year from date of receipt. It is stable at -20°C for 3 months after opening. It is recommended to freeze aliquots at -80°C for extended storage. Avoid repeated freeze-thaw cycles.

Shipping with dry ice.