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Hydrolase that can remove conjugated ubiquitin from proteins and therefore plays an important regulatory role at the level of protein turnover by preventing degradation. Additionally we are shipping USP8 Antibodies (86) and USP8 Kits (9) and many more products for this protein.
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Ubpy loss of function results in the accumulation of autophagosomes due to a blockade of the autophagy flux.
Results show that in addition to the scaffolding function in complex formation, BRUCE has an E3 ligase function to promote BRIT1 (show MCPH1 Proteins) deubiquitination by USP8 leading to accumulation of BRIT1 (show MCPH1 Proteins) at DNA double-strand break.
No somatic mutations were observed in USP8 in a cohort of GH-secreting pituitary adenomas.
Studies indicate that ubiquitin specific protease 8 protein (USP8) mutations contribute to adrenocorticotropic hormone (ACTH) overproduction in Cushing's disease (CD).
The presence of USP8 mutations may predict favorable responses to the somatostatin (show SST Proteins) analog pasireotide in corticotroph adenomas of Cushing's disease.
The identification of USP8 mutations as contributors to the pathogenesis of ACTH (show POMC Proteins)-secreting pituitary adenomas represents an exciting advance in our understanding of Cushing's disease and its potential treatment into the of precision medicine.
these findings implicate a novel role for K6-linked Ub conjugates and USP8-mediated deubiquitination in the regulation of PARK2 (show PARK2 Proteins) in mitochondrial quality control
In surgically resected primary USP8-mutated tumor cells, USP8 knockdown or blocking EGFR (show EGFR Proteins) effectively attenuates ACTH (show POMC Proteins) secretion. Inhibition of USP8 or EGFR (show EGFR Proteins) is promising for treating USP8-mutated corticotrophin adenoma.
USP8 is frequently mutated in adenomas causing Cushing's disease, especially in those from female adult patients diagnosed at a younger age.
BRUCE acts as a scaffold, bridging the ubiquitin-specific peptidase 8 (USP8) and BRIT1 (show MCPH1 Proteins) in a complex to coordinate USP8-catalyzed deubiquitination of BRIT1 (show MCPH1 Proteins).
the membrane receptor MET, described herein for the first time in spermatids, is a USP8/UBPy-target substrate is delivered to the acrosome.
in neuronal cells USP8 could be involved in endosomal trafficking, retrograde transport and synaptic plasticity. In disorders leading to neurodegeneration USP8 is upregulated and could influence the neuron-oligodendrocyte interactions.
The spatio-temporal expression of mUBPy suggests that the enzyme may be involved in neuroregulatory processes during embryogenesis.
a role for the USP8.STAM (show STAM Proteins) complex as a protective mechanism regulating early endosomal sorting of EGFR (show EGFR Proteins) between pathways destined for lysosomal degradation and recycling.
USP8 was able to interact with spermatid endosomal-sorting complex required for transport-0 and microtubule structures; USP8 can directly link, via its MIT domain, the labeled vesicles/developing acrosome to microtubules.
in wobbler testis expression of mouse ubiquitin-specific processing protease (mUBPy)is up-regulated, while a differential sorting of the protein characterizes wobbler spermatids where acrosome formation is impaired
Data indicate a novel mechanism where diacylglycerol kinase delta and protein kinase (show CDK7 Proteins) Calpha (show PRKACA Proteins) modulate the levels of ubiquitinated epidermal growth factor (show EGF Proteins) receptors through Akt (show AKT1 Proteins) and ubiquitin-specific protease 8.
deubiquitinating enzyme specifically expressed in testis, associates with the acrosome and centrosome in mouse germ cells
Results indicate that Nrdp1 (show RNF41 Proteins) is a specific target for the USP8 deubiquitinating enzyme and are consistent with a model where USP8 augments Nrdp1 (show RNF41 Proteins) activity by mediating its stabilization.
We conclude that UBPY negatively regulates the rate of EGFR (show EGFR Proteins) down-regulation by deubiquitinating EGFR (show EGFR Proteins) on endosomes.
Hydrolase that can remove conjugated ubiquitin from proteins and therefore plays an important regulatory role at the level of protein turnover by preventing degradation. Converts both 'Lys-48' an 'Lys-63'-linked ubiquitin chains. Catalytic activity is enhanced in the M phase. Involved in cell proliferation. Required to enter into S phase in response to serum stimulation. May regulate T-cell anergy mediated by RNF128 via the formation of a complex containing RNF128 and OTUB1. Probably regulates the stability of STAM2 and RASGRF1. Regulates endosomal ubiquitin dynamics, cargo sorting, membrane traffic at early endosomes, and maintenance of ESCRT-0 stability. The level of protein ubiquitination on endosomes is essential for maintaining the morphology of the organelle. Deubiquitinates EPS15 and controles tyrosine kinase stability. Removes conjugated ubiquitin from EGFR thus regulating EGFR degradation and downstream MAPK signaling. Involved in acrosome biogenesis through interaction with the spermatid ESCRT-0 complex and microtubules. Deubiquitinates BIRC6/bruce and KIF23/MKLP1.
ubiquitin carboxyl-terminal hydrolase 8
, ubiquitin-specific-processing protease 8
, ubiquitin specific peptidase 8
, ubiquitin carboxyl-terminal hydrolase 8-like
, deubiquitinating enzyme 8
, ubiquitin isopeptidase Y
, ubiquitin specific protease 8
, ubiquitin thioesterase 8
, ubiquitin thiolesterase 8
, putative deubiquitinating enzyme