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SAFB regulated the activity of NF-kappaB (show NFKB1 Proteins) signaling in CRC (show CALR Proteins) by targeting TAK1 (show MAP3K7 Proteins) This novel mechanism provides a comprehensive understanding of both SAFB and the NF-kappaB (show NFKB1 Proteins) signaling pathway in the progression of CRC (show CALR Proteins) and indicates that the SAFB-TAK1 (show MAP3K7 Proteins)-NF-kappaB (show NFKB1 Proteins) axis is a potential target for early therapeutic intervention in CRC (show CALR Proteins) progression
Depletion of SAFB1 reduced FUS's localization to chromatin-bound fraction and splicing activity, suggesting SAFB1 could tether FUS (show FUS Proteins) to chromatin compartment thorough N-terminal DNA-binding motif. Moreover, FUS (show FUS Proteins) interacts with another nuclear matrix-associated (show SMARCA5 Proteins) 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 (show MCAM Proteins) (NCAM1 (show NCAM1 Proteins)) and ASTN2 (show ASTN2 Proteins) was influenced by SAFB1.
Single depletion of either SAFB1 or SAFB2 (show SAFB2 Proteins) leads to an increase in expression of the other SAFB protein.
reveals an unexpected role of SUMO-1 (show SUMO1 Proteins) and SAFB in the stimulatory coupling of promoter binding, transcription initiation and RNA processing
SAFB1 formed a complex with the histone methyltransferase EZH2 (show EZH2 Proteins).
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 (show SAFB2 Proteins) are crucial repressors for ERalpha (show ESR1 Proteins) dynamics in association with the nuclear matrix and that their synergistic regulation of ERalpha (show ESR1 Proteins) mobility is sufficient for inhibiting ERalpha (show ESR1 Proteins) function.
transcriptional repressor SAFB1 is modified by both SUMO1 (show SUMO1 Proteins) and SUMO2 (show SUMO2 Proteins)/3, and this modification is necessary for its full repressive activity.
despite a high degree of sequence similarity, SAFB1(-/-) and SAFB2 (show SAFB2 Proteins)(-/-) 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 represses ERalpha (show ESR1 Proteins) activity via indirect association with histone deacetylation and interaction with the basal transcription machinery
SAFB1 plays a critical role in development, growth regulation, and reproduction.
SAFB1 interacts in pull-down assays not only with PPARgamma (show PPARG Proteins) but also with all nuclear receptors tested
SAFB1 loss causes lack of contact inhibition, increased foci formation, and increased oncogene (show RAB1A Proteins)-induced anchorage-independent growth.
Our data show that SAFB1 heterozygosity does not influence Wnt-1 (show WNT1 Proteins) induced tumorigenesis
These results indicate a major role for SAFB1 in the activation of Srebp-1c (show SREBF1 Proteins) through its interaction with RBMX (show RBMX Proteins).
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