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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 UBE2C Antibodies (139) and UBE2C Proteins (24) and many more products for this protein.
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UBE2C is involved in the anti-proliferative and pro-apoptotic functions of ECRG4 (show C2orf40 ELISA Kits) in esophageal squamous cell carcinoma.
loss of BRCA1 function results in an increase in UBE2C expression and chemical resistance to doxorubicin in breast cancer cells.
FoxM1 (show FOXM1 ELISA Kits) promotes glioma progression by enhancing UBE2C transcription
SAG/RBX2 (show RNF7 ELISA Kits) E3 ligase complexes with UBCH10 and UBE2S ubiquitin-conjugating enzymes to ubiquitylate beta-TrCP1 (show BTRC ELISA Kits) via K11-linkage for degradation.
UBE2C and HOXA1 RNA and protein are differentially expressed in conventional and Spitz nevi and melanoma.
High UBE2C expression is associated with esophageal squamous cell carcinoma.
Urinary UBE2C cell-free RNA may be a valuable diagnostic marker for bladder cancer.
A role was identified for UBE2C as a marker of the androgen signaling pathway in prostate cancer.
Data suggest that the activity of AURKA (show AURKA ELISA Kits) might be regulated by UBE2C through regulating the activity of anaphasepromoting complex. UBE2C may be a new marker in the diagnosis of gastric cancer and may be a potential therapeutic target for the treatment of gastric adenocarcinoma.
High UBCH10 expression is associated with bortezomib-resistance in multiple myeloma.
alongside their canonical function in protein degradation, Ube2C and -S also control the extrusion of the first polar body.
UbcH10 overexpression increases carcinogenesis and blocks ALLN susceptibility in colorectal cancer.
results identify UbcH10 as a prominent protooncogene that causes whole chromosome instability and tumor formation over a wide gradient of overexpression levels
These results indicated that ubiquitination of certain factors by UBE2S and UBE2C plays a role in the escape from metaphase II arrest in porcine oocytes.
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 the destruction of mitotic cyclins and for cell cycle progression. Multiple transcript variants encoding different isoforms have been found for this gene.
ubiquitin-conjugating enzyme E2C
, ubiquitin carrier protein C
, ubiquitin-protein ligase C
, cyclin-selective ubiquitin carrier protein
, mitotic-specific ubiquitin-conjugating enzyme
, ubiquitin-conjugating enzyme E2 C