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Validated All-in-One™ qPCR Primer for BARD1(NM_000465.3) Search again
Product ID:
HQP015946
(click here to view gene annotation page)
Powered by BiozSpecies:
Human
Symbol:
Alias:
-
Gene Description:
BRCA1 associated RING domain 1
Target Gene Accession:
NM_000465.3(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.
Validated result:
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| A | B |
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Each All-in-One™ qPCR Primer is experimentally validated to yield a single dissociation curve peak and to generate a single amplification of the correct size for the targeted gene. A cDNA Pool, containing reverse transcript products of 8 different human tissue total RNA(Liver, Testis,Muscle,Thyroid,Brain,Spleen,Stomach,Small Intestine)),was used as the qPCR validation template. qPCR was performed using 0.2 µM primer with 2XAll-in-One™ qPCR Mix (Catalog#: QP001,QP002,QP004,QP005). Reactions were incubated for 10min. at 95°C, followed by 40 cycles of 95°C for 10 sec.; 60°C, 20 sec. and 72°C, 15sec. using Bio-Rad iQ5™ Instrument. At the end of the last cycle, temperature was increased from 72 to 95°C to produce a melting curve. Panel A: Validated Result for Amplification Curve; Panel B: Validated Result for Melting Curve. |
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Summary
This gene encodes a protein which interacts with the N-terminal region of BRCA1. In addition to its ability to bind BRCA1 in vivo and in vitro, it shares homology with the 2 most conserved regions of BRCA1: the N-terminal RING motif and the C-terminal BRCT domain. The RING motif is a cysteine-rich sequence found in a variety of proteins that regulate cell growth, including the products of tumor suppressor genes and dominant protooncogenes.
Gene References into function
- BARD1 acts in p53-Dependent Apoptosis
- Germline mutations of BARD1 have been detected in hereditary breast and breast/ovarian cancers negative for BRCA1 and BRCA2 alterations.
- BARD1 induces BRCA1 intranuclear foci formation by increasing RING-dependent BRCA1 nuclear import and inhibiting BRCA1 nuclear export
- Autoubiquitination of the BRCA1*BARD1 RING ubiquitin ligase.
- It is structurally homologous to BRCA1 (it shares the conserved RING finger and BRCT domains); may be involved in tumor suppression because BARD1-BRCA1 complexes in ubiquination of RNA Pol II and BARD1 interacts with CstF-50 (inhibiting mRNA processing).
- BRCA1 and BARD1 are associated with the RNA polymerase II holoenzyme.
- enhancement of BRCA1 E3 ubiquitin ligase activity through direct interaction with the BARD1 protein
- Purified RINGs, including BARD1, self-assemble into supramolecular structures in vitro that resemble those they form in cells. Self-assembly controls and amplifies E3 ubiquitin conjugation activity of BARD1:BRCA1.
- BRCA1/BARD1 catalyses the formation of multiple polyubiquitin chains on itself and potentiates the E3 ubiquitin ligase activity of the BRCA1/BARD1 complex >20-fold
- Forms a heterodimer with BRCA1 and the resulting complex functions as an E3 ubiquitin ligase that catalyzes the synthesis of polyubiquitin chains.
- Data show that expression of truncated mouse or human BARD1 peptides capable of interacting with Brca1 results in a homologous-repair deficiency.
- BRCA1-BARD1 mediates novel polyubiquitin chains that may be distinctly edited by 26 S proteasome from conventional Lys-48-linked polyubiquitin chains.
- BRCA1/BARD1 heterodimer formation is important for optimal nuclear targeting of BARD1 and its role in DNA repair and cell survival.
- cooperates with BRCA1 to increase ubiquitin conjugation in cells
- BRCA1-BARD1 complexes act as an adaptor to mediate phosphorylation of p53, influencing G(1)/S cell cycle progression after DNA damage.
- BRCA1-BARD1 catalyzes the polyubiquitination of nucleolar phosphoprotein nucleophosmin/B23
- differential gene expression of Bard1, a tumor suppressor gene, plays a significant role in the proliferation of breast cancer
- Our findings identify a novel apoptosis inhibitory function of BARD1 and suggest that nuclear retention of BRCA1-BARD1 complexes contributes to both DNA repair and cell survival.
- results suggest a possible role for BARD1 in hereditary susceptibility to breast cancer
- BARD1 regulation of the cell cycle is a nuclear event and may be linked to its induced expression during mitosis.
- BRCA1 interacts with BARD1 to generate significant ubiquitin ligase activity which catalyzes nontraditional Lys-6-linked polyubiquitin chains in breast csancer.
- BARD1, by binding to the kinase and its substrate, catalyses p53 phosphorylation.
- BARD1 phosphorylation plays a role in the cellular response to DNA damage
- BRCA1 and BARD1 can ubiquitinate phosphorylated RNA polymerase II
- Missense mutations in the BARD1 gene may contribute to the cancer phenotype in breast and ovarian cancer.
- genetic and epigenetic changes might lead to elevated cytoplasmic expression of BARD1 and that cytoplasmic BARD1 might be a poor prognostic factor for breast and ovarian cancers
- Neither Cys557Ser nor Val507Met mutations in BARD1 have an effect on familial breast cancer susceptibility.
- BARD1 Cys557Ser is an ancient variant that confers risk of single and multiple primary breast cancers, and this risk extends to carriers of the BRCA2 999del5 mutation.
- The Cys557Ser mutation within the BARD1 gene is associated with an increased risk of breast cancer.
- The ubiquitin-proteasome degradation pathway plays a significant role in the coordinated protein stability of BRCA1 and its partner BARD1 in ovarian granulosa cells.
- ERalpha associated with the ninth intron of the endogenous BARD 1 gene in MCF-7 cells.
- BARD1 mutations may predispose to breast cancer in Poland
- we were unable to identify either qualitatively or quantitatively tumor-specific expression patterns of the identified BARD1 splicing variants.
- the BARD1 BRCT structure provides insights into the mechanisms by which the cancer-associated missense mutations C645R, V695L, and S761N may adversely affect the structure and function of BARD1.
- Expression of BARD1 and its isoforms is temporally and spatially regulated by human chorionic gonadotropin and by hypoxia, both factors known to regulate the invasive phase and proliferation of cytotrophoblasts.
- BARD1 may regulate the transcriptional activities of p53 as tumor suppressors
- BARD1 variants are not associated with breast cancer risk in Australian familial breast cancer.
- BARD1 isoform expression is required for cancer cell proliferation, which is compatible with the notion that BARD1 isoforms act as cancer maintenance genes in gynecological cancers.
- We propose that BARD1 reduces BRCA1 transcriptional activity, and that this at least partly involves BRCA1/BARD1 E3 ubiquitin ligase activity, which is disrupted by the C61G mutation.
- crystallographic analysis of the BARD1 ankyrin repeat domain and its functional consequences
- characterize the BARD1 structural biochemistry responsible for CstF-50 binding
- Results suggest that BAP1 and BRCA1/BARD1 coordinately regulate ubiquitination during the DNA damage response and the cell cycle.
- BARD1 has BRCA1-dependent and BRCA1-independent functions in mitosis. BARD1, but not BRCA1, localizes to the midbody at telophase and cytokinesis, where it colocalizes with Aurora B.