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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 (140) and UBE2C Proteins (29) and many more products for this protein.
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Identification of UBE2C as a target of wild-type and GOF mutant p53 (show TP53 ELISA Kits) further highlights the contribution of p53 (show TP53 ELISA Kits) in regulation of spindle assembly checkpoint
The anaphase-promoting complex/cyclosome C activity in human cells is tuned by the combinatorial use of three E2 ubiquitin-conjugating enzymes, namely UBE2C, UBE2S (show UBE2S ELISA Kits), and UBE2D.
Study shows an overexpression of UbcH10 mRNA and protein in the vast majority of colorectal cancer (CRC (show CALR ELISA Kits)) patients analyzed and indicates that UbcH10 expression regulates CRC (show CALR ELISA Kits) growth.
the present study showed that miR (show MLXIP ELISA Kits)-196a promoted cell proliferation by targeting UBE2C in breast cancer. Thus, miR (show MLXIP ELISA Kits)-196a may be a potential oncogene (show RAB1A ELISA Kits) in breast cancer and a promising therapeutic target in breast cancer treatment.
UBE2C could regulate phospho-ERK1/2 (show MAPK1/3 ELISA Kits) level.
Data suggest that ubiquitin-conjugating enzyme (show Ube2t ELISA Kits) UbcH10 may be a promising target for the therapy of breast cancer.
Upregulation of miR-17/20a promotes gastric cancer cell growth by targeting UBE2C.
UbcH10 overexpression increases carcinogenesis and blocks ALLN susceptibility in colorectal cancer.
in addition to binding APC11 (show ANAPC11 ELISA Kits)'s RING, UBCH10 is corecruited via interactions with APC2
excess E2F1 (show E2F1 ELISA Kits) due to Rb inactivation recruits the complex of Cdc20 (show CDC20 ELISA Kits) and the anaphase-promoting complex/cyclosome to deregulate the expression of UBCH10
alongside their canonical function in protein degradation, Ube2C and -S also control the extrusion of the first polar body.
results identify UbcH10 as a prominent protooncogene that causes whole chromosome instability and tumor formation over a wide gradient of overexpression levels
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