recommended for detection of UBE2J2 of mouse, rat and human origin by WB, IP, IF, IHC(P) and ELISA; also reactive with additional species, including canine
UBE2J2 Background Information Ubiquitination is an important molecular mechanism by which abnormal or short-lived proteins are targeted for degradation by the concerted efforts of at least three classes of enzymes: ubiquitin-activating enzymes (E1s), ubiquitin-conjugating enzymes (E2s) and ubiquitin-protein ligases (E3s). UBE2J2 (Ubiquitin-conjugating enzyme E2 J2), also known as NCUBE2 (Non-canonical ubiquitin-conjugating enzyme 2), is a 259 amino acid single pass type IV membrane protein that that belongs to the E2 ubiquitin-conjugating enzyme family and is involved in protein degradation. Localized to the membrane of the endoplasmic reticulum (ER), UBE2J2 catalyzes the attachment of ubiquitin to misfolded membrane proteins, thereby targeting them for proteasomal destruction. This ATP-dependent reaction yields AMP, a diphosphate and a ubiquitin-tagged protein and may be a method of quality control within the ER. Two isoforms of UBE2J2 exist due to alternative splicing events.
UBE2J2 (L-24)
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UBE2J2 (L-24): sc-134139. Immunoperoxidase staining of formalin-fixed, paraffin-embedded human intestine tissue showing cytoplasmic localization.
UBE2J2 (L-24): sc-134139. Western blot analysis of UBE2J2 expression in Hep G2 whole cell lysate.