UBE1 Background Information The ubiquitin activating enzyme E1 (UBE1) catalyzes the first step in ubiquitin conjugation to mark cellular proteins for degradation. Specifically, UBE1 functions to adenylate the C-terminal glycine residue of ubiquitin, a reaction that is ATP-dependent and is proceeded by the formation of a thiolester bond with a cysteine residue of UBE1. The UBE1-activated ubiquitin is then transferred to a ubiquitin conjugated enzyme, which donates the ubiquitin residue to target substrates. The UBE1 gene is an example of an X-Y homologous gene, which is X-linked with a distinct Y-linked gene in many mammals. However, no UBE1 homolog is detectable on the human Y chromosome. UBE1 is thought to escape X inactivation in humans.
UBE1 (2G2)
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UBE1 (2G2): sc-53555. Western blot analysis of UBE1 expression in HeLa nuclear extract (A) and Hep G2 (B) and Jurkat (C) whole cell lysates.
UBE1 (2G2): sc-53555. Immunofluorescence staining of methanol-fixed HeLa cells showing nuclear localization.
UBE1 (2G2): sc-53555. Immunoperoxidase staining of formalin fixed, paraffin-embedded human testis tissue showing nuclear and cytoplasmic staining of cells in seminiferus ducts and Leydig cells (low and high magnification). Kindly provided by The Swedish Human Protein Atlas (HPA) program.
UBE1 (2G2): sc-53555. Western blot analysis of UBE1 expression in HL-60 whole cell lysate.
UBE1 (2G2): sc-53555. Western blot analysis of UBE1 expression in non-transfected: sc-117752 (A) and human UBE1 transfected: sc-171710 (B) 293T whole cell lysates and HeLa nuclear extract (C).
