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The ubiquitin-dependent protein degradation pathway is essential for proteolysis of intracellular proteins and peptides. Additionally we are shipping USP28 Antibodies (77) and USP28 Proteins (5) and many more products for this protein.
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These results showed that USP28 is overexpressed in human glioblastomas and it contributes to glioma tumorigenicity.
Data indicte that deubiquitinating enzyme USP28 was targeted by microRNA miR (show MLXIP ELISA Kits)-4295.
findings provide a first insight into understanding how the enzymatic activity of Usp28 is regulated by its non-catalytic UBR and endogenous ligands.
Dual regulation of Fbw7 (show FBXW7 ELISA Kits) activity by Usp28 is a safeguard mechanism for maintaining physiological levels of proto-oncogenic Fbw7 (show FBXW7 ELISA Kits) substrates, which is equivalently disrupted by loss or overexpression of Usp28.
identified Usp28 as a c-MYC (show MYC ELISA Kits) target gene highly expressed in colorectal cancers, which indicates that USP28 and c-MYC (show MYC ELISA Kits) form a positive feedback loop that maintains high c-MYC (show MYC ELISA Kits) protein levels in tumors
USP28 has a chain preference activity for Lys (show LYZ ELISA Kits)(11), Lys (show LYZ ELISA Kits)(48), and Lys (show LYZ ELISA Kits)(63) diubiquitin (show UBD ELISA Kits) linkages
Usp28 expression was indentified as a independent predictors of survival (P = 0.001) and potentially valuable in prognostic evaluation of bladder cancer
Study reveals a critical mechanism underlying the epigenetic regulation by USP28.
USP28 is not a critical factor in double-strand break metabolism and is unlikely to be an attractive target for therapeutic intervention aimed at chemotherapy sensitization.
USP28 gene expression is down regulated by oxidative stress through the mediation of reactive oxygen species
In mice, an unusually direct antagonism between an E3 ligase and a deubiquitinase, Fbw7 (show FBXW7 ELISA Kits) and Usp28, modulate intestinal homeostasis and cancer.
The ubiquitin-dependent protein degradation pathway is essential for proteolysis of intracellular proteins and peptides. Enzymes that remove ubiquitin from ubiquitin-conjugated peptides, like USP28, affect the fate and degradation of intracellular proteins and are essential for maintenance of cell-free ubiquitin pools (Valero et al., 2001).
ubiquitin specific peptidase 28
, ubiquitin carboxyl-terminal hydrolase 28-like
, ubiquitin specific protease 28
, ubiquitin carboxyl-terminal hydrolase 28
, deubiquitinating enzyme 28
, ubiquitin carboxyl-terminal hydrolase 28 variant 1
, ubiquitin thioesterase 28
, ubiquitin thiolesterase 28
, ubiquitin-specific-processing protease 28