UBE2J2 Protein, Human (GST)

The UBE2J2 protein plays a crucial role in cellular processes by catalyzing the covalent attachment of ubiquitin to other proteins. Its function is involved in the selective degradation of misfolded membrane proteins extending into the endoplasmic reticulum (ERAD), as suggested by the similarity of related processes. UBE2J2 Protein, Human (GST) is the recombinant human-derived UBE2J2 protein, expressed by E. coli , with N-GST labeled tag. The total length of UBE2J2 Protein, Human (GST) is 101 a.a., with molecular weight of 30 & 36 kDa, respectively.

UBE2J2, or ubiquitin-conjugating enzyme E2 J2, is a protein that plays a central role in the covalent attachment of ubiquitin to other proteins, a process critical for the regulation of protein stability and degradation. UBE2J2 is suggested to function in the selective degradation of misfolded membrane proteins from the endoplasmic reticulum (ERAD), indicating its involvement in cellular quality control mechanisms. Additionally, in cooperation with the GATOR2 complex, UBE2J2 catalyzes 'Lys-6'-linked ubiquitination of NPRL2, suggesting its participation in the regulation of cellular processes through ubiquitin modification. It has to highlight UBE2J2's dual role in ERAD and the ubiquitination of specific targets, illustrating its versatility in participating in diverse cellular pathways.

Human

E. coli

N-GST

Q8N2K1 (E124-R224)

118424  [NCBI]

EKGPTLGSIETSDFTKRQLAVQSLAFNLKDKVFCELFPEVVEEIKQKQKAQDELSSRPQTLPLPDVVPDGETHLVQNGIQLLNGHAPGAVPNLAGLQQANR

30&36 kDa

Greater than 95% as determined by reducing SDS-PAGE.

<1 EU/μg, determined by LAL method.