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SAFB regulated the activity of NF-kappaB signaling in CRC by targeting TAK1 This novel mechanism provides a comprehensive understanding of both SAFB and the NF-kappaB signaling pathway in the progression of CRC and indicates that the SAFB-TAK1-NF-kappaB axis is a potential target for early therapeutic intervention in CRC progression
Depletion of SAFB1 reduced FUS's localization to chromatin-bound fraction and splicing activity, suggesting SAFB1 could tether FUS to chromatin compartment thorough N-terminal DNA-binding motif. Moreover, FUS interacts with another nuclear matrix-associated protein, Matrin3.
Data suggest that ERH interacts directly in nucleus with C-terminal Arg-Gly-rich region of SAFB1/SAFB2 and this multimer co-localizes in insoluble nuclear fraction; binding of ERH reverses inhibition exerted by SAFB1/SAFB2 on SRPK1. (ERH = enhancer of rudimentary homolog protein; SAFB = scaffold attachment factor B; SRPK1 = splicing kinase SR protein kinase-1)
The expression of coding and non-coding genes with SAFB1 cross-link sites was altered by SAFB1 knockdown. The isoform-specific expression of neural cell adhesion molecule (NCAM1) and ASTN2 was influenced by SAFB1.
Single depletion of either SAFB1 or SAFB2 leads to an increase in expression of the other SAFB protein.
reveals an unexpected role of SUMO-1 and SAFB in the stimulatory coupling of promoter binding, transcription initiation and RNA processing
SAFB1 formed a complex with the histone methyltransferase EZH2.
Data indicate that scaffold attachment factor SAFB1 is transiently recruited to DNA breaks in a poly(ADP-ribose)-polymerase 1- and poly(ADP-ribose)-dependent manner.
Results indicate that SAFB1 and SAFB2 are crucial repressors for ERalpha dynamics in association with the nuclear matrix and that their synergistic regulation of ERalpha mobility is sufficient for inhibiting ERalpha function.
transcriptional repressor SAFB1 is modified by both SUMO1 and SUMO2/3, and this modification is necessary for its full repressive activity.
Data show that binding of p53 to SAFB1 had a significant functional outcome, since SAFB1 was shown to suppress p53-mediated reporter gene expression.
This study shows that low SAFB protein levels predict poor prognosis of breast cancer patients, suggesting critical functions of SAFB1 and SAFB2 in breast cancer cells.
Study confirms the primary role of SAFB1/SAFB2 as corepressors and also uncovers a previously unknown role for SAFB1 in the regulation of immune genes and in estrogen-mediated repression of genes.
HSP27 is a nuclear speckle component in unstressed cells in tissue culture. It is also associated with the nucleolar compartment.
REVIEW: possibility that SAFB1 and SAFB2 are novel breast tumor suppressor genes, and how they might function in this role, are discussed
HSP27 expression may have useful diagnostic use for the prognosis of mouth squamous cell carcinoma.
SAFB1 represses ERalpha activity via indirect association with histone deacetylation and interaction with the basal transcription machinery
SAFB1 was shown to interact directly with the nuclear receptor corepressor N-CoR.
SAFB1 interacts in pull-down assays not only with PPARgamma but also with all nuclear receptors tested
PP2A-mediated dephosphorylation of HSP27 and tau correlated with PP2A-induced preservation of endothelial cell cytoskeleton
despite a high degree of sequence similarity, SAFB1(-/-) and SAFB2(-/-) mice do not totally phenocopy each other
Mice lacking SAFB1 exhibit developmental abnormalities in their lungs, high incidence of perinatal lethality, and adults develop different types of tumors. Mouse embryonic fibroblasts from Safb1-null animals are immortalized in culture.
SAFB1 plays a critical role in development, growth regulation, and reproduction.
SAFB1 loss causes lack of contact inhibition, increased foci formation, and increased oncogene-induced anchorage-independent growth.
Our data show that SAFB1 heterozygosity does not influence Wnt-1 induced tumorigenesis
These results indicate a major role for SAFB1 in the activation of Srebp-1c through its interaction with RBMX.
This gene encodes a DNA-binding protein which has high specificity for scaffold or matrix attachment region DNA elements (S/MAR DNA). This protein is thought to be involved in attaching the base of chromatin loops to the nuclear matrix but there is conflicting evidence as to whether this protein is a component of chromatin or a nuclear matrix protein. Scaffold attachment factors are a specific subset of nuclear matrix proteins (NMP) that specifically bind to S/MAR. The encoded protein is thought to serve as a molecular base to assemble a 'transcriptosome complex' in the vicinity of actively transcribed genes. It is involved in the regulation of heat shock protein 27 transcription, can act as an estrogen receptor co-repressor and is a candidate for breast tumorigenesis. This gene is arranged head-to-head with a similar gene whose product has the same functions. Multiple transcript variants encoding different isoforms have been found for this gene.
HSP27 ERE-TATA-binding protein
, HSP27 estrogen response element-TATA box-binding protein
, Hsp27 ERE-TATA binding protein
, glutathione S-transferase fusion protein
, heat-shock protein (HSP27) estrogen response element and TATA box-binding protein
, scaffold attachment factor B1
, scaffold attachment factor B2
, scaffold attachment factor B
, scaffold attachment factor b
, Scaffold attachment factor B