Animal ID:
RB0053-0054
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Host:
Rabbit
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Reactivity:
human
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Buffers:
Purified rabbit polyclonal antibody supplied in PBS with 0.09% (W/V) sodium azide. This antibody is purified through a protein G column and eluted out with both high and low pH buffers and neutralized immediately after elution then followed by dialysis against PBS.
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Storage:
Maintain refrigerated at 2-8ºC for up to 6 months. For long term storage store at -20ºC. Avoid repeated freeze-thaw cycles.
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Application:
Tested by peptide-specific ELISA (1:1,000).
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Immunogen:
KLH conjugated synthetic peptide comprised of amino acids 108 - 124 [CSKLRNLLHDNELSDLK] of the human BRCA1 associated RING domain 1 (BARD1) protein.
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Accession number:
NM_000465
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Descrption:
BRCA1 associated RING domain 1 (BARD1) interacts with the N-terminal region of breast cancer 1 early onset protein (BRCA1). It enhances BRCA1¿s E3 ubiquitin ligase activity through direct interaction. In addition to its ability to bind BRCA1 in vivo and in vitro, BARD1 shares homology with the 2 most conserved regions of BRCA1: (i) the N-terminal RING motif and (ii) 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. The BARD1 protein also contains 3 tandem ankyrin repeats. BRCA1 / BARD1 are associated with the RNA polymerase II holoenzyme and 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. BARD1 also induces BRCA1 intranuclear foci formation by increasing RING-dependent BRCA1 nuclear import and inhibiting BRCA1 nuclear export. Germline mutations of BARD1 have been detected in hereditary breast and breast/ovarian cancers negative for BRCA1 and BRCA2 alterations.
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Alternative Name(s):
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References:
- Xia Y, Pao GM, Chen HW, Verma IM, Hunter T: Enhancement of BRCA1 E3 ubiquitin ligase activity through direct interaction with the BARD1 protein. J. Biol. Chem. 278(7): 5255-5263 (2003).
- Chiba N, Parvin JD: The BRCA1 and BARD1 association with the RNA polymerase II holoenzyme. Cancer Res. 62(15): 4222-4228 (2002).
- Irminger-Finger I, Leung WC: BRCA1-dependent and independent functions of BARD1. Int. J. Biochem. Cell Biol. 34(6): 582-587 (2002). Review.
- Chen A, Kleiman FE, Manley JL, Ouchi T, Pan ZQ: Autoubiquitination of the BRCA1*BARD1 RING ubiquitin ligase. J. Biol. Chem. 277(24): 22085-22092 (2002).
- Irminger-Finger I, Leung WC, Li J, Dubois-Dauphin M, Harb J, Feki A, Jefford CE, Soriano JV, Jaconi M, Montesano R, Krause KH: Identification of BARD1 as mediator between proapoptotic stress and p53-dependent apoptosis. Mol. Cell. 8(6): 1255-1266 (2001).
- Thai TH, Du F, Tsan JT, Jin Y, Phung A, Spillman MA, Massa HF, Muller CY, Ashfaq R, Mathis JM, Miller DS, Trask BJ, Baer R, Bowcock AM: Mutations in the BRCA1-associated RING domain (BARD1) gene in primary breast, ovarian and uterine cancers. Hum. Mol. Genet. 7(2): 195-202 (1998).
- Wu LC, Wang ZW, Tsan JT, Spillman MA, Phung A, Xu XL, Yang MC, Hwang LY, Bowcock AM, Baer R: Identification of a RING protein that can interact in vivo with the BRCA1 gene product. Nat. Genet. 14(4): 430-440 (1996).
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For Research Use Only. Not for Diagnostic or Therapeutic Use.
Purchase does not include or carry any right to resell or transfer this product either as a stand-alone product or as a component of another product. Any use of this product other than the permitted use without the express written authorization of Orbigen, Inc. is strictly prohibited
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