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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-Conjugating Enzyme E2A Antibodies (57) and Ubiquitin-Conjugating Enzyme E2A Kits (19) and many more products for this protein.
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RAD6 is upregulated in response to chemotherapy and significantly correlated with expression of ovarian cancer (OC) stem cell signaling genes ALDH1A1 (show ALDH1A1 Proteins) and SOX2 (show SOX2 Proteins) and poor prognosis of OC patients.
RAD6 promotes proteasome activity and nuclear translocation by enhancing the degradation of PSMF1 (show PSMF1 Proteins) and the lamin B receptor (show LBR Proteins).
Data show that the ubiquitin-conjugating enzyme E2 RAD6A/B-MDM2 ubiquitin ligase machinery regulates anti-silencing function 1A protein (ASF1A) degradation.
Results showed KCMF1 C-terminus binds directly to RAD6, whereas N-terminal domains interact with UBR4 and point mutations found in X-linked intellectual disability (XLID) patients specifically lose the interaction with KCMF1 and UBR4.
This study investigates clinical and molecular data of two unrelated, affected males with chromosome Xq24 deletions encompassing UBE2A.
RAD6 physically interacts with heterochromatin protein 1alpha and ubiquitinates HP1alpha (show CBX5 Proteins) at residue K154, thereby promoting heterochromatin protein 1alpha degradation through the autophagy pathway
HHR6 and hRad18 can monoubiquitinate FANCD2 at lysine 561 in vitro. This activity may represent a novel stress response pathway.
RNF168 (show RNF168 Proteins), in complex with RAD6A or RAD6B (show UBE2B Proteins), is activated in the DNA-damage-induced protein ubiquitination cascade.
RAD6A is a regulator of Parkin (show PARK2 Proteins)-dependent mitophagy plays a critical role in maintaining neuronal function.
UBE2A specifically interacts with CDK9 (show CDK9 Proteins), but not CDK2 (show CDK2 Proteins) and is phosphorylated by CDK9 (show CDK9 Proteins) in vitro.
results indicate a causal role of UBE2A in learning and mGLUR (show GRM8 Proteins)-dependent long-term depression
Disruption of pre-TCR expression accelerates lymphomagenesis in E2A (show TCF3 Proteins)-deficient mice.
signaling through Notch (show NOTCH1 Proteins) modulates the turnover of E2A (show TCF3 Proteins) proteins
absence of mHR6A in oocytes prevents development beyond the embryonic two-cell stage
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 E2 ubiquitin-conjugating enzyme family. This enzyme is required for post-replicative DNA damage repair. Multiple alternatively spliced transcript variants have been found for this gene and they encode distinct isoforms.
ubiquitin-conjugating enzyme E2 A
, ubiquitin-conjugating enzyme E2A (RAD6 homolog)
, ubiquitin-conjugating enzyme E2A
, RAD6 homolog A
, ubiquitin carrier protein A
, ubiquitin-protein ligase A
, ubiquitin-conjugating enzyme E2A, RAD6 homolog
, ubiquitin-conjugating enzyme HR6A