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SPOP 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. Additionally we are shipping Speckle-Type POZ Protein Antibodies (59) and Speckle-Type POZ Protein Proteins (11) and many more products for this protein.
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Dzip1-dependent stabilization of Spop/HIB is evolutionarily conserved and essential for proper regulation of Gli (show GLI1 ELISA Kits)/Ci proteins in the Hh pathway.
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 (show CD274 ELISA Kits) protein abundance is regulated by cyclin D-CDK4 (show CDK4 ELISA Kits) 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 (show MYC ELISA Kits) expression in prostate physiology, identify c-MYC (show MYC ELISA Kits) 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 (show BRD2 ELISA Kits), BRD3 (show BRD3 ELISA Kits) and BRD4 (show BRD4 ELISA Kits) proteins. SPOP mutation in prostate cancer increased expression of BRD2 (show BRD2 ELISA Kits), BRD3 (show BRD3 ELISA Kits) and BRD4 (show BRD4 ELISA Kits) proteins.
Prostate cancer-derived SPOP mutants failed to interact with Cdc20 (show CDC20 ELISA Kits) to promote its degradation. As a result, SPOP-deficient prostate cancer cells with elevated Cdc20 (show CDC20 ELISA Kits) expression became resistant to a pharmacological Cdc20 (show CDC20 ELISA Kits) 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 (show PIK3CA ELISA Kits)/mTOR (show FRAP1 ELISA Kits) and androgen receptor (show AR ELISA Kits) signaling, effectively uncoupling the normal negative feedback between these two pathways.
SPOP-containing complex regulates SETD2 stability and H3K36me3-coupled alternative splicing.
loss of Spop, but not Spopl, 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 (show GLI3 ELISA Kits) and Gli3R for ubiquitination and degradation and Spop is an important positive regulator of Ihh (show IHH ELISA Kits) signaling and skeletal development
Results demonstrate a negative role of Spop in the level and activity of Gli3 (show GLI3 ELISA Kits), Shh (show SHH ELISA Kits) 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 (show MLXIP ELISA Kits)-145 has a role in post-transcriptional regulation of SPOP expression in selected tissues.
similar S/T-rich motifs are present in Gli (show GLI1 ELISA Kits) proteins as well as in numerous HIB-interacting proteins and mediate Gli (show GLI1 ELISA Kits) degradation by SPOP
MacroH2A1.2 binds the nuclear protein (show HEMGN ELISA Kits) Spop.
Interaction of endogenous PDX-1 (show PDX1 ELISA Kits) and PCIF1 in MIN6 insulinoma (show RPS15 ELISA Kits) 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.
speckle-type POZ protein
, Speckle-type POZ protein
, speckle-type POZ protein-like
, HIB homolog 1
, speckle-type POZ protein B
, roadkill homolog 1
, PDX-1 C-terminal-interacting factor 1