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Initiation of transcription by RNA polymerase II requires the activities of more than 70 polypeptides. Additionally we are shipping TBP Antibodies (144) and TBP Kits (25) and many more products for this protein.
Showing 10 out of 33 products:
Data indicate the crystal structure of a Brf2-TBP-Bdp1 complex bound to a DNA promoter.
Study could not determine a definitive cutoff value for the pathologic CAG repeat (show CELF3 Proteins) number of SCA17.
TBP attenuates Msx1 (show MSX1 Proteins)-mediated glycoprotein hormone alpha (show CGA Proteins) transcriptional repression.
this analysis of the 2.2-kb doubly spliced RNA (2.2DS-RNA) -mediated suppression of viral RNA expression showed that 2.2DS-RNA inhibited transcription via binding to the TATA-binding protein and stress granule proteins.
Our results provide first evidence that Taspase1 processing affects TFIIA (show GTF2A1 Proteins) regulation of TFIID and suggest that Taspase1 processing of TFIIA (show GTF2A1 Proteins) is required to establish INR (show INSR Proteins)-selective core promoter activity in the presence of NC2 (show GTF2H5 Proteins).
TBP (and GATA2 (show GATA2 Proteins) and Sp1 (show PSG1 Proteins)) have key roles in inflammation and ischemia-like conditions through MAOA (show MAOA Proteins) regulation.
Deactivation of TBP contributes to SCA17 pathogenesis.
HOXA2 (show HOXA2 Proteins) acts as a suppressor or TBP-antagonist to inhibit MMP-9 (show MMP9 Proteins) expression; while methylation-mediated inactivation of HOXA2 (show HOXA2 Proteins) in NPC (show NPC1 Proteins) derepresses MMP-9 (show MMP9 Proteins) production and increases invasion of NPC (show NPC1 Proteins) cells.
The data reveal synergistic effects of H3K4me3, H3K14ac and a TATA box sequence on TFIID binding in vitro. Stoichiometry analyses of affinity purified human TFIID identified the presence of a stable dimeric core.
The UL4 protein directly interacted with the host TBP and the carboxy-terminal domain of RNA polymerase II in infected cells.
the TAF10-containing canonical TFIID and SAGA complexes are dispensable for early paraxial mesoderm development, arguing against the generic role in transcription proposed for these fully assembled holo-complexes
Our study establishes glial dysfunction as an important component of SCA17 pathogenesis and suggests targeting glial inflammation as a potential therapeutic approach for SCA17 treatment.
This evidence demonstrates that TBP2 (show Tbpl2 Proteins) does not replace TBP during muscle differentiation, as previously proposed, with limiting amounts of TFIID-TBP being required to promote muscle-specific (show EIF3K Proteins) gene expression
The large TBP polyQ repeat decreases the association of MyoD with TBP and DNA promoters and causes muscle degeneration in spinocerebellar ataxia 17 transgenic mice.
Thus, modulating the levels of both Huwe1 and USP10 (show USP10 Proteins) appears to fine-tune the requisite degradation of TBP during myogenesis.
This study demonistrated that denervation-induced muscle atrophy on Tbp expression in mice.
The results of this study confirmed motor deficits in the Tbp/Q71 mice and present previously unrecognized behavioral characteristics obtained from the automated home cage, indicating its use for high-throughput screening and testing.
TBP might be a marker for transmitting cellular memory to daughter cells.
we show that the differentiation of fetal liver progenitors to adult hepatocytes involves a wholesale depletion of canonical cofactor required for Sp1 activation/Mediator and TFIID complexes at both the RNA and protein level
Alcohol induces RNA polymerase III-dependent transcription through c-Jun (show JUN Proteins) by co-regulating TATA-binding protein (TBP) and Brf1 (show ZFP36L1 Proteins) expression.
TBP plays an important role in the degradation of a specific subset of maternal mRNAs during late blastulation/early gastrulation, which involves targets of the miR (show MYLIP Proteins)-430 pathway.
Results indicate that a portion of Brf1 is sandwiched between Bdp1 and TBP upstream of the U6 TATA box. Furthermore, Bdp1 traverses the DNA under the N-terminal stirrup of TBP to interact with the DNA (and very likely Brf1) downstream of the TATA sequence.
TFIID (show TAF8 Proteins) has two disctinct modes of transcription initiation, de novo initiation and reinitiation, as revealed by the inhibitory effect of TFIID (show TAF8 Proteins)-bound tin (show MSH2 Proteins) compounds on the de novo initiation, but not on the reinitiation.
Aptamers generated by both selections were able to bind specifically to TBP, but the two groups showed characteristics which were clearly different in terms of their capability to compete with TATA-DNA.
in fruit flies, different classes of RNA polymerase III promoters differentially utilize TBP and TRF1 (show TERF1 Proteins) for the initiation of transcription.
Tbp targets core histone transcription.
TBP activates TATA-dependent transcription and represses DPE-dependent transcription, whereas Mot1 and NC2 (show GTF2H5 Proteins) block TBP function and thus repress TATA-dependent transcription and activate DPE-dependent transcription.
Initiation of transcription by RNA polymerase II requires the activities of more than 70 polypeptides. The protein that coordinates these activities is transcription factor IID (TFIID), which binds to the core promoter to position the polymerase properly, serves as the scaffold for assembly of the remainder of the transcription complex, and acts as a channel for regulatory signals. TFIID is composed of the TATA-binding protein (TBP) and a group of evolutionarily conserved proteins known as TBP-associated factors or TAFs. TAFs may participate in basal transcription, serve as coactivators, function in promoter recognition or modify general transcription factors (GTFs) to facilitate complex assembly and transcription initiation. This gene encodes TBP, the TATA-binding protein. A distinctive feature of TBP is a long string of glutamines in the N-terminus. This region of the protein modulates the DNA binding activity of the C terminus, and modulation of DNA binding affects the rate of transcription complex formation and initiation of transcription. The number of CAG repeats encoding the polyglutamine tract is usually 32-39, and expansion of the number of repeats increases the length of the polyglutamine string and is associated with spinocerebellar ataxia 17, a neurodegenerative disorder classified as a polyglutamine disease. Two transcript variants encoding different isoforms have been found for this gene.
TATA sequence-binding protein
, TATA-box binding protein N-terminal domain
, TATA-box factor
, TATA-box-binding protein
, transcription initiation factor TFIID TBP subunit
, TATA-binding factor
, TATA-binding protein
, TFIID core protein
, TA-TA binding protein 1
, TATA binding protein
, TATA box binding protein
, 42kDa polypeptide
, TATA box-binding protein
, TATA-box binding protein
, transcription factor
, Transcription initiation factor TFIID TBP subunit
, TATA-box binding protein S homeolog