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Validated All-in-One™ qPCR Primer for BRD4(NM_058243.3) Search again
Product ID:
HQP171596
(click here to view gene annotation page)
Powered by BiozSpecies:
Human
Symbol:
Alias:
CAP, FSHRG4, HUNK1, HUNKI, MCAP
Gene Description:
bromodomain containing 4
Target Gene Accession:
NM_058243.3(click here to view gene page)
Estimated Delivery:
Approximately 1-3 weeks, but may vary. Please email sales@genecopoeia.com or call 301-762-0888 to confirm ETA.
Important Note:
By default, qPCR primer pairs are designed to measure the expression level of the splice variant (accession number) you selected for this gene WITHOUT consideration of other possible variants of this gene. If this gene has multiple variants, and you would like to measure the expression levels of one particular variant, multiple variants, or all variants, please contact us for a custom service project at inquiry@genecopoeia.com.
Summary
The protein encoded by this gene is homologous to the murine protein MCAP, which associates with chromosomes during mitosis, and to the human RING3 protein, a serine/threonine kinase.
Gene References into function
- brd4 binds to replication factor C and inhibits progression to S phase
- E2 protein interacts with Brd4 and tethers the viral DNA to the host mitotic chromosomes.
- Data identif a Rap GTPase-activating protein, signal-induced proliferation-associated protein 1 (SPA-1), as a factor that interacts with Brd4.
- Brd4 has recently been proposed to mediate the association between bovine papilomavirus1 E2 and mitotic chromosomes.
- Wild type Brd4 inhibits G(1) to S progression and we also found that the Brd4-NUT fusion augments the inhibition of progression to S phase compared with wild type Brd4.
- establish a broader role for Brd4 in the papillomavirus life cycle than as the chromosome tether for papillomavirus E2 during mitosis
- Brd4 is a component of human papillomavirus-assembled transcriptional silencing complex with a novel function as a cellular cofactor modulating viral gene expression.
- there are distinct functional roles for the two bromodomain proteins RING3/Brd2 and Brd4 in LANA binding
- The major papillomavirus E2-binding protein was identified by mass spectrometry and western blotting as the long isoform of Brd4.[Brd4]
- We show the X-ray crystal structure of the carboxy-terminal domain of Brd4 in complex with HPV-16 E2, and with this information have developed a Brd4-Tat fusion protein that is efficiently taken up by different transformed cells harboring HPV plasmids.
- evidence for a Brd4-independent mechanism of E2-mediated repression and suggests that different cellular factors must be involved in E2-mediated transcriptional activation and repression functions.
- Tax may compete and functionally substitute for Brd4 in P-TEFb regulation.Tax and Brd4 compete for binding to P-TEFb through direct interaction with cyclin T1
- Overexpression of the BRD4 P-TEFb-interacting domain disrupts the interaction between the HIV transactivator Tat and positive transcription elongation factor b and suppresses the ability of Tat to transactivate the HIV promoter
- BRD-NUT fusion proteins contribute to carcinogenesis by associating with chromatin and interfering with epithelial differentiation.
- while the P-TEFb level remains constant, the Brd4-P-TEFb interaction increases dramatically in cells progressing from late mitosis to early G(1).
- The two bromodomains of Brd4 are mainly monomeric in solution; therefore Brd4 should have its own mechanism to reinforce its association with chromatin both in mitotic retention and related cellular processes.
- The authors provide evidence that Brd4 regulates P-TEFb kinase activity by inducing a negative pathway via phosphorylation of CDK9 at threonine 29 (T29) in the HIV transcription initiation complex, inhibiting CDK9 kinase activity.
- Brd4 as a novel coactivator of NF-kappaB through specifically binding to acetylated lysine-310 of RelA.
- Bovine papillomavirus type 1 (BPV-1) E2 binds cellular chromatin in complex with Brd4 in both mitotic and interphase cells.