UBE2V2 Protein, Human (sf9, His, strep)

UBE2V2 protein lacks independent ubiquitin ligase activity and forms a functional heterodimer with UBE2N. Together, they catalyze nonclassical polyubiquitin chain synthesis ("Lys-63"), distinct from proteasome-driven degradation. UBE2V2 Protein, Human (sf9, His, strep) is the recombinant human-derived UBE2V2 protein, expressed by Sf9 insect cells, with N-His and N-Strep labeled tag.

The UBE2V2 protein lacks ubiquitin ligase activity when acting alone, but forms a functional heterodimer with UBE2N to catalyze the synthesis of non-canonical poly-ubiquitin chains linked through 'Lys-63'. Notably, this type of poly-ubiquitination does not result in protein degradation by the proteasome. UBE2V2 plays a pivotal role in mediating the transcriptional activation of target genes, exerting influence over cell cycle progression, and contributing to cellular differentiation. Furthermore, it is involved in the error-free DNA repair pathway, enhancing cell survival following DNA damage. UBE2V2 primarily functions as a heterodimer with UBE2N and demonstrates binding affinity for CHFR, suggesting its involvement in various cellular processes and molecular interactions.

Human

Sf9 insect cells

N-His;N-Strep

Q15819 (M1-N145)

7336

Full Length

MAVSTGVKVPRNFRLLEELEEGQKGVGDGTVSWGLEDDEDMTLTRWTGMIIGPPRTNYENRIYSLKVECGPKYPEAPPSVRFVTKINMNGINNSSGMVDARSIPVLAKWQNSYSIKVVLQELRRLMMSKENMKLPQPPEGQTYNN

Approximately 16.4 kDa,based on SDS-PAGE under reducing conditions.

≥ 90%, as determined by reducing SDS-PAGE.

<1 EU/μg, determined by LAL method.