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In complex with CUL3, involved in ubiquitination and proteasomal degradation of several substrates (By similarity). Zusätzlich bieten wir Ihnen SPOP-B Kits (28) und SPOP-B Proteine (12) und viele weitere Produktgruppen zu diesem Protein an.
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Expression of the F133V mutation and wild-type SPOP was at much lower levels compared to that of F102C and Y87N mutations; however, at present, it is unknown if this also affects the biological activity of the SPOP protein.
PD-L1 protein abundance is regulated by cyclin D-CDK4 and the cullin 3-SPOP E3 ligase via proteasome-mediated degradation
methylation status of SPOP promoter can be used as a novel epigenetic biomarker and a therapeutic target in colorectal cancer.
these data highlight SPOP as an important regulator of luminal epithelial cell proliferation and c-MYC expression in prostate physiology, identify c-MYC as a novel bona fide SPOP substrate, and help explain the frequent inactivation of SPOP in human prostate adenocarcinoma.
Results elucidate the tumor-suppressor role of SPOP in prostate cancer in which it acts as a negative regulator of BET protein stability and also provide a molecular mechanism for resistance to BET inhibitors in individuals with prostate cancer bearing SPOP mutations.
SPOP mutation in endometrial cancer increased degradation of BRD2 (zeige BRD2 Antikörper), BRD3 (zeige BRD3 Antikörper) and BRD4 (zeige BRD4 Antikörper) proteins. SPOP mutation in prostate cancer increased expression of BRD2 (zeige BRD2 Antikörper), BRD3 (zeige BRD3 Antikörper) and BRD4 (zeige BRD4 Antikörper) proteins.
Prostate cancer-derived SPOP mutants failed to interact with Cdc20 (zeige CDC20 Antikörper) to promote its degradation. As a result, SPOP-deficient prostate cancer cells with elevated Cdc20 (zeige CDC20 Antikörper) expression became resistant to a pharmacological Cdc20 (zeige CDC20 Antikörper) inhibitor.
While wild-type SPOP localizes to liquid nuclear speckles, self-association-deficient SPOP mutants have a diffuse distribution in the nucleus. SPOP oligomerizes through its BTB and BACK domains.
SPOP mutation activates both PI3K (zeige PIK3CA Antikörper)/mTOR (zeige FRAP1 Antikörper) and androgen receptor (zeige AR Antikörper) signaling, effectively uncoupling the normal negative feedback between these two pathways.
SPOP-containing complex regulates SETD2 (zeige SETD2 Antikörper) stability and H3K36me3-coupled alternative splicing.
loss of Spop, but not Spopl (zeige SPOPL Antikörper), disrupts chondrocyte hypertrophy and osteoblast differentiation in the mouse, suggesting the requirement for Spop-mediated protein degradation in mouse skeletal development; overexpressed Spop targets both Gli3FL (zeige GLI3 Antikörper) and Gli3R for ubiquitination and degradation and Spop is an important positive regulator of Ihh (zeige IHH Antikörper) signaling and skeletal development
Results demonstrate a negative role of Spop in the level and activity of Gli3 (zeige GLI3 Antikörper), Shh (zeige SHH Antikörper) signaling and ventral spinal cord patterning.
Speckle-type pox virus and zinc finger (POZ) protein (SPOP) regulates endometrial stromal cell decidualization in mice and that hormones regulate the expression of SPOP. This study suggests that ubiquitination may be involved in embryonic implantation.
These results implicate SPOP as a novel participant in DNA double strand break repair and suggest that SPOP mutation drives prostate tumorigenesis in part through genomic instability.
miR-145 has a role in post-transcriptional regulation of SPOP expression in selected tissues.
Dzip1 (zeige DZIP1 Antikörper)-dependent stabilization of Spop/HIB is evolutionarily conserved and essential for proper regulation of Gli (zeige GLI1 Antikörper)/Ci proteins in the Hh pathway.
similar S/T-rich motifs are present in Gli proteins as well as in numerous HIB-interacting proteins and mediate Gli degradation by SPOP
MacroH2A1.2 binds the nuclear protein Spop.
Interaction of endogenous PDX-1 (zeige PDX1 Antikörper) and PCIF1 in MIN6 insulinoma (zeige RPS15 Antikörper) cells, is demonstarted.
This gene encodes a protein that may modulate the transcriptional repression activities of death-associated protein 6 (DAXX), which interacts with histone deacetylase, core histones, and other histone-associated proteins. In mouse, the encoded protein binds to the putative leucine zipper domain of macroH2A1.2, a variant H2A histone that is enriched on inactivated X chromosomes. The BTB/POZ domain of this protein has been shown in other proteins to mediate transcriptional repression and to interact with components of histone deacetylase co-repressor complexes. Alternative splicing of this gene results in multiple transcript variants encoding the same protein.
HIB homolog 1
, roadkill homolog 1
, PDX-1 C-terminal-interacting factor 1
, speckle-type POZ protein B