Use your antibodies-online credentials, if available.
No Products on your Comparison List.
Your basket is empty.
Find out more
Show all species
Show all synonyms
Select your species and application
anti-Human BARD1 Antibodies:
anti-Mouse (Murine) BARD1 Antibodies:
anti-Rat (Rattus) BARD1 Antibodies:
Go to our pre-filtered search.
Human Polyclonal BARD1 Primary Antibody for IP, PLA - ABIN151785
Hu, Ghosh, Amleh, Yue, Lu, Katz, Li: Modulation of aromatase expression by BRCA1: a possible link to tissue-specific tumor suppression. in Oncogene 2005
Show all 13 Pubmed References
Human Polyclonal BARD1 Primary Antibody for IHC, IHC (p) - ABIN4283035
Jerjees, Alabdullah, Green, Alshareeda, Macmillan, Ellis, Rakha: Prognostic and biological significance of proliferation and HER2 expression in the luminal class of breast cancer. in Breast cancer research and treatment 2014
Show all 2 Pubmed References
Human Polyclonal BARD1 Primary Antibody for IF (p), IHC (p) - ABIN706496
Liu, Ao, Jia, Bai, Xu, Hu, Jiang, Chen, Wu: FOXK2 transcription factor suppresses ER?-positive breast cancer cell growth through down-regulating the stability of ER? via mechanism involving BRCA1/BARD1. in Scientific reports 2015
BARD1delta binds more efficiently than BARD1 to telomere binding proteins and causes their depletion from telomeres, leading to telomere and chromosomal instability and tumor cell cycle arrest.
BRCA1-BARD1 mutants with weakened RAD51 (show RAD51 Antibodies) interactions show compromised DNA joint formation and impaired mediation of homologous recombination and DNA repair in cells; results identify a late role of BRCA1-BARD1 in homologous recombination, an attribute of the tumour suppressor complex that could be targeted in cancer therapy
variants in BARD1 were associated with moderate risks of breast cancer.
NPM1 (show NPM1 Antibodies) downregulation by P-STAT5 (show STAT5A Antibodies) is mediated by impairing the BRCA1-BARD1 ubiquitin ligase, which controls the stability of NPM1 (show NPM1 Antibodies). In turn, decreased NPM1 (show NPM1 Antibodies) levels led to suppression of p53 (show TP53 Antibodies) expression, resulting in enhanced cell survival.
In MCF-7 cells BARD1 variants do vary considerably their cellular distribution and in their ability to influence apoptotic response to cisplatin.
substitutions that create a structurally intact BRCA1/BARD1 heterodimer that is inactive in vitro with all E2 enzymes. Other substitutions in BRCA1 or BARD1 RING domains result in hyperactivity, revealing that both proteins have evolved attenuated activity. Loss of attenuation results in decreased product specificity, providing a rationale for why nature has tuned BRCA1 activity.
Findings suggest that the study of AtROW1 in plant may provide a model for elucidating the functional mechanism of BARD1 in mammals.
BRCA1-BARD1 ligase activity and subsequent SMARCAD1 (show SMARCAD1 Antibodies)-dependent chromatin remodeling are critical regulators of DNA repair in cancer cells.
Results suggest that BRCA1-associated RING domain protein 1 (BARD1) rs7585356 G>A polymorphism may be associated with nephroblastoma risk.
BARD1 rs6435862 T>G and rs3768716 A>G single nucleotide polymorphisms contribute to increased susceptibility to neuroblastoma (show ARHGEF16 Antibodies), especially for children at age >/=12 months in a Southern Chinese population.
Suggest BARD1 as a driver of proliferation and of pulmonary fibrosis pathogenesis.
identification of BARD1 as mediator between proapoptotic stress and p53 (show TP53 Antibodies)-dependent apoptosis
the developmental functions of Brca1 (show BRCA1 Antibodies) and Bard1 are mediated by the Brca1 (show BRCA1 Antibodies)/Bard1 heterodimer.
Data show that expression of truncated mouse or human BARD1 peptides capable of interacting with Brca1 results in a homologous-repair deficiency.
the ankyrin (show ANK Antibodies) and BRCT motifs of BARD1 are each essential for both chromosome stability and homology-directed DNA repair.
The remarkable similarities between the mammary carcinomas of Bard1-, Brca1 (show BRCA1 Antibodies)-, and Bard1/Brca1 (show BRCA1 Antibodies)-mutant mice indicate that the tumor suppressor activities of both genes are mediated through the BRCA1 (show BRCA1 Antibodies)/BARD1 heterodimer.
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. This protein also contains 3 tandem ankyrin repeats. The BARD1/BRCA1 interaction is disrupted by tumorigenic amino acid substitutions in BRCA1, implying that the formation of a stable complex between these proteins may be an essential aspect of BRCA1 tumor suppression. This protein may be the target of oncogenic mutations in breast or ovarian cancer.
BRCA1 associated RING domain 1
, BRCA1-associated RING domain protein 1-like
, BRCA1 associated RING domain 1 isoform alfa
, BRCA1 associated RING domain 1 isoform beta
, BRCA1 associated RING domain 1 isoform delta
, BRCA1 associated RING domain 1 isoform epsilon
, BRCA1 associated RING domain 1 isoform eta
, BRCA1 associated RING domain 1 isoform gamma
, BRCA1 associated RING domain 1 isoform phi
, BRCA1-associated RING domain gene 1
, BRCA1-associated RING domain protein 1