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The modification of proteins with ubiquitin is an important cellular mechanism for targeting abnormal or short-lived proteins for degradation. Additionally we are shipping Ubiquitin-Like Modifier Activating Enzyme 7 Antibodies (95) and Ubiquitin-Like Modifier Activating Enzyme 7 Proteins (8) and many more products for this protein.
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RNF170, an endoplasmic reticulum (ER)-associated ubiquitin E3 ligase, interacted with pUL50 and promoted pUL50-mediated UBE1L degradation via ubiquitination.
the cellular effects of progerin expression in Hutchinson-Gilford progeria syndrome are transduced, at least in part, through reduced function of the Ran GTPase and E2 SUMOylation pathways.
UBE1L is a retinoid target that triggers PML/RARalpha degradation and apoptosis in acute promyelocytic leukemia
RA treatment of APL and other RA-responsive leukemic cells induced expression of UBE1L and ISG15 as well as intracellular ISG15 conjugates. A physical association was found between UBE1L and ISG15 in vivo.
Ube1L was required for transfer of ISG15 to UbcH8 and for binding of Ube1L to UbcH8
UBE1L-ISG15 preferentially inhibits cyclin D1 in lung cancer
Inhibitor-sensitive tyrosine kinase controls the population heterogeneity of basal STAT1 activity in Ube1l deficient fibroblasts.
Bone marrow transplantation experiment revealed a 50% reduction in repopulation potential of Ube1L-deficient cells at 3weeks posttransplantation, but no differences at 6 and 12weeks.
UBE1L and protein ISGylation are not critical for IFN-alpha/beta signaling via JAK/STAT activation.
Ube1l is not a tumor suppressor gene in K-ras(LA2) lung cancer mouse model.
Both UbE1L(-/-) and ISG15(-/-) mice display increased susceptibility to influenza B virus infection, including non-mouse-adapted strains.
The importance of UbE1L was confirmed by demonstrating that mice lacking this ISG15 E1 enzyme were highly susceptible to Sindbis virus infection.
ISG15, UBE1l and UBCH8 genes are significantly upregulated in the artificially inseminated pregnant cows.
The modification of proteins with ubiquitin is an important cellular mechanism for targeting abnormal or short-lived proteins for degradation. Ubiquitination involves at least three classes of enzymes: ubiquitin-activating enzymes, or E1s, ubiquitin-conjugating enzymes, or E2s, and ubiquitin-protein ligases, or E3s. This gene encodes a member of the E1 ubiquitin-activating enzyme family. The encoded enzyme is a retinoid target that triggers promyelocytic leukemia (PML)/retinoic acid receptor alpha (RARalpha) degradation and apoptosis in acute promyelocytic leukemia, where it is involved in the conjugation of the ubiquitin-like interferon-stimulated gene 15 protein.
UBA1, ubiquitin-activating enzyme E1 homolog B
, UBA7, ubiquitin-activating enzyme E1
, ubiquitin-activating enzyme 7
, ubiquitin-activating enzyme E1 homolog
, ubiquitin-activating enzyme E1-related protein
, ubiquitin-activating enzyme-2
, ubiquitin-like modifier-activating enzyme 7
, ubiquitin-activating enzyme E1 (A1S9T and BN75 temperature sensitivity complementing)
, ubiquitin-conjugating enzyme E2R 2
, ubiquitin conjugating enzyme E2
, ubiquitin-like modifier activating enzyme 7
, ubiquitin-like modifier-activating enzyme 7-like