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Mouse Anti-BARD1 Recombinant Antibody (CBYY-0196) (CBMAB-0197-YY)

This product is mouse antibody that recognizes BARD1. The antibody CBYY-0196 can be used for immunoassay techniques such as: DB, IP, WB
See all BARD1 antibodies
Published Data

Summary

Host Animal
Mouse
Specificity
Human, Mouse, Rat
Clone
CBYY-0196
Antibody Isotype
IgG1, κ
Application
ELISA, WB, IF, IP, IHC-P

Basic Information

Immunogen
Amino acids 1-300 mapping at the N-terminus of BARD1 of human origin.
Specificity
Human, Mouse, Rat
Antibody Isotype
IgG1, κ
Clonality
Monoclonal
Application Notes
The COA includes recommended starting dilutions, optimal dilutions should be determined by the end user.
ApplicationNote
WB1:100-1:1,000
IP1-2 µg per 100-500 µg of total protein (1 ml of cell lysate)
IF(ICC)1:50-1:500
IHC-P1:50-1:500
ELISA1:100-1:1,000

Formulations & Storage [For reference only, actual COA shall prevail!]

Format
Liquid
Buffer
PBS, 0.1% gelatin
Preservative
< 0.1% sodium azide
Concentration
0.2 mg/ml
Storage
Store at +4°C short term (1-2 weeks). Aliquot and store at -20°C long term. Avoid repeated freeze/thaw cycles.

Target

Full Name
BRCA1 Associated RING Domain 1
Introduction
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. Multiple alternatively spliced transcript variants encoding different isoforMouse have been found for this gene. [provided by RefSeq, Sep 2013]
Entrez Gene ID
UniProt ID
Alternative Names
BRCA1 Associated RING Domain 1; RING-Type E3 Ubiquitin Transferase BARD1; EC 2.3.2.27; BARD-1;
Function
E3 ubiquitin-protein ligase. The BRCA1-BARD1 heterodimer specifically mediates the formation of 'Lys-6'-linked polyubiquitin chains and coordinates a diverse range of cellular pathways such as DNA damage repair, ubiquitination and transcriptional regulation to maintain genomic stability. Plays a central role in the control of the cell cycle in response to DNA damage. Acts by mediating ubiquitin E3 ligase activity that is required for its tumor suppressor function. Also forms a heterodimer with CSTF1/CSTF-50 to modulate mRNA processing and RNAP II stability by inhibiting pre-mRNA 3' cleavage.
Biological Process
Cell cycle arrest Source: UniProtKB
Cellular response to DNA damage stimulus Source: UniProtKB
DNA double-strand break processing Source: Reactome
DNA replication Source: Reactome
Double-strand break repair Source: Reactome
Double-strand break repair via nonhomologous end joining Source: Reactome
Negative regulation of apoptotic process Source: UniProtKB
Negative regulation of mRNA 3'-end processing Source: UniProtKB
Negative regulation of protein export from nucleus Source: UniProtKB
Positive regulation of apoptotic process Source: UniProtKB
Positive regulation of protein catabolic process Source: UniProtKB
Protein deubiquitination Source: Reactome
Protein K6-linked ubiquitination Source: UniProtKB
Protein ubiquitination Source: UniProtKB
Regulation of phosphorylation Source: UniProtKB
Regulation of signal transduction by p53 class mediator Source: Reactome
Tissue homeostasis Source: UniProtKB
Cellular Location
Nucleus. During S phase of the cell cycle, colocalizes with BRCA1 into discrete subnuclear foci. Can translocate to the cytoplasm. Localizes at sites of DNA damage at double-strand breaks (DSBs); recruitment to DNA damage sites is mediated by the BRCA1-A complex.
PTM
Processed during apoptosis. The homodimer is more susceptible to proteolytic cleavage than the BARD1/BRCA1 heterodimer.

Sakai, Y., Hanafusa, H., Shimizu, T., Pastuhov, S. I., Hisamoto, N., & Matsumoto, K. (2021). BRCA1–BARD1 regulates axon regeneration in concert with the Gqα–DAG signaling network. Journal of Neuroscience, 41(13), 2842-2853.

Becker, J. R., Clifford, G., Bonnet, C., Groth, A., Wilson, M. D., & Chapman, J. R. (2021). BARD1 reads H2A lysine 15 ubiquitination to direct homologous recombination. Nature, 1-5.

Tarsounas, M., & Sung, P. (2020). The antitumorigenic roles of BRCA1–BARD1 in DNA repair and replication. Nature Reviews Molecular Cell Biology, 21(5), 284-299.

Watters, A. K., Seltzer, E. S., MacKenzie, D., Young, M., Muratori, J., Hussein, R., ... & Zhang, D. (2020). The Effects of Genetic and Epigenetic Alterations of BARD1 on the Development of Non-Breast and Non-Gynecological Cancers. Genes, 11(7), 829.

Otsuka, K., Yoshino, Y., Qi, H., & Chiba, N. (2020). The Function of BARD1 in Centrosome Regulation in Cooperation with BRCA1/OLA1/RACK1. Genes, 11(8), 842.

Śniadecki, M., Brzeziński, M., Darecka, K., Klasa-Mazurkiewicz, D., Poniewierza, P., Krzeszowiec, M., ... & Wydra, D. (2020). Bard1 and breast cancer: The possibility of creating screening tests and new preventive and therapeutic pathways for predisposed women. Genes, 11(11), 1251.

Alenezi, W. M., Fierheller, C. T., Recio, N., & Tonin, P. N. (2020). Literature review of BARD1 as a cancer predisposing gene with a focus on breast and ovarian cancers. Genes, 11(8), 856.

Nakamura, K., Saredi, G., Becker, J. R., Foster, B. M., Nguyen, N. V., Beyer, T. E., ... & Groth, A. (2019). H4K20me0 recognition by BRCA1–BARD1 directs homologous recombination to sister chromatids. Nature cell biology, 21(3), 311-318.

Cimmino, F., Formicola, D., & Capasso, M. (2017). Dualistic role of BARD1 in cancer. Genes, 8(12), 375.

Liao, Y., Yuan, S., Chen, X., Zhu, P., Li, J., Qin, L., & Liao, W. (2017). Up-regulation of BRCA1-associated RING domain 1 promotes hepatocellular carcinoma progression by targeting Akt signaling. Scientific reports, 7(1), 1-11.

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For research use only. Not intended for any clinical use.

Custom Antibody Labeling

We also offer labeled antibodies developed using our catalog antibody products and nonfluorescent conjugates (HRP, AP, Biotin, etc.) or fluorescent conjugates (Alexa Fluor, FITC, TRITC, Rhodamine, Texas Red, R-PE, APC, Qdot Probes, Pacific Dyes, etc.).

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