USP6 Protein, Human (Sf9)

USP6 protein is an ATP-independent isopeptidase with unique deubiquitinase activity that can cleave the C-terminus of ubiquitin and catalyze its own deubiquitination. Notably, it coordinates ARF6 plasma membrane localization and selectively affects ARF6-dependent endocytic protein trafficking. USP6 Protein, Human (Sf9) is the recombinant human-derived USP6 protein, expressed by Sf9 insect cells , with tag free.

USP6, an ATP-independent isopeptidase, possesses distinctive deubiquitinase activity, cleaving at the C-terminus of the ubiquitin moiety and catalyzing its own deubiquitination. In vitro, isoform 2 exhibits deubiquitinating activity, contrasting with isoform 3. Notably, USP6 plays a crucial role in orchestrating plasma membrane localization of ARF6 and selectively modulating ARF6-dependent endocytic protein trafficking. Its functional significance extends to tumorigenesis initiation, as it induces the production of matrix metalloproteinases through NF-kappa-B activation. USP6's multifaceted activity highlights its pivotal role in cellular processes, positioning it as a key player in protein regulation, membrane dynamics, and the intricate balance involved in tumorigenesis.

Human

Sf9 insect cells

Tag Free

P35125 (K529-Q1406)

9098

Greater than 90% as determined by reducing SDS-PAGE.

<1 EU/μg, determined by LAL method.