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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 (85) 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 Proteins)-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 Proteins) activity by Usp28 is a safeguard mechanism for maintaining physiological levels of proto-oncogenic Fbw7 (show FBXW7 Proteins) substrates, which is equivalently disrupted by loss or overexpression of Usp28.
identified Usp28 as a c-MYC (show MYC Proteins) target gene highly expressed in colorectal cancers, which indicates that USP28 and c-MYC (show MYC Proteins) form a positive feedback loop that maintains high c-MYC (show MYC Proteins) protein levels in tumors
USP28 has a chain preference activity for Lys (show LYZ Proteins)(11), Lys (show LYZ Proteins)(48), and Lys (show LYZ Proteins)(63) diubiquitin (show UBD Proteins) 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 Proteins) 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