The ubiquitin activating enzyme E1 (UBE1) catalyzes the first step in ubiquitin conjugation to mark cellular proteins for degradation. UBE1 activates ubiquitin by first adenylating (with ATP) its carboxy-terminal glycine residue and thereafter linking this residue to the side chain of a cysteine residue in E1, yielding a ubiquitin-E1 thioester and a free AMP. UBE1 is an example of an X-Y homologous gene, which is X-linked with a distinct Y-linked gene in many mammals. UBE1L (Ubiquitin-activating enzyme E1 homolog), also known as UBA7 (Ubiquitin-like modifier-activating enzyme 7) or UBE2, is a 1011 amino acid homolog of UBE1. Like UBE1, UBE1L functions in the activation of ubiquitin through ATP-dependent adenylation. UBE1L is expressed in tumor cells and is a retinoid target that, through conjugation with ISG15 (Interferon-induced 15 kDa protein), triggers degradation and apoptosis in acute promyelocytic leukemia.

Ubiquitin-like modifier-activating enzyme 7; Ubiquitin-activating enzyme 7; D8; Ubiquitin-activating enzyme E1 homolog; UBA7; UBE1L; UBE2

p41226

Human,Mouse,Rat

WB,IHC

WB 1:500-1:1000
IHC 1:50-1:200

~ 112 kDa

Rabbit

This antibody detects endogenous levels of UBE1L protein.

Synthetic peptide, corresponding to amino acids C-terminus of Human UBE1L.

Polyclonal

Rabbit IgG

The antibody was affinity-purified from rabbit antiserum by affinity-chromatography using epitope-specific immunogen and the purity is > 95% (by SDS-PAGE).

PBS with 0.02% sodium azide, 50% glycerol, pH7.2

1mg/ml

Store at 4℃ short term,and store at -20℃ long term. Avoid freeze-thaw cycles.