protein

USP11 Protein, Human (Sf9)

HY-P702063

20 μg;50 μg

350;790 USD

USP11 Protein, Human (Sf9)

proteins

Sf9 insect cells

20 μg;50 μg

350;790 USD

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. The total length of USP11 Protein, Human (Sf9) is 962 a.a., .

Human

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.

USP11; Ubiquitin carboxyl-terminal hydrolase 11; Deubiquitinating enzyme 11; Ubiquitin thioesterase 11; Ubiquitin-specific-processing protease 11

Greater than 85% as determined by reducing SDS-PAGE.

Supplied as a 0.22 μm filtered solution of 50 mM Tris-HCl, pH7.5, 200 mM NaCl, 20% glycerol.

Shipping with dry ice