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BRIP1 antibody (BRCA1 Interacting Protein C-terminal Helicase 1) (C-Term)

Details for Product anti-BRIP1 Antibody No. ABIN965700, Supplier: Login to see
Antigen
  • MGC68622
  • BRIP1
  • fancj
  • si:ch211-158l18.1
  • BACH1
  • FANCJ
  • OF
  • 3110009N10Rik
  • 8030460J03Rik
  • Bach1
  • FACJ
  • Fancj
Epitope
C-Term
16
15
12
12
11
7
3
2
2
1
1
1
Reactivity
Human
68
3
1
Host
Rabbit
52
15
1
Clonality
Polyclonal
Conjugate
This BRIP1 antibody is un-conjugated
3
3
3
2
2
2
1
1
1
1
1
1
1
1
Application
51
23
10
8
8
5
4
3
Supplier
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Immunogen Polyclonal antibody produced in rabbits immunizing with a synthetic peptide corresponding to C-terminal residues of human BRIP1 (ATP-dependent RNA helicase)
Alternative Name BRIP1 (BRIP1 Antibody Abstract)
Background BRIP1 (ATP-dependent RNA helicase Is a DNA-dependent ATPase and 5' to 3' DNA helicase which is required for the maintenance of chromosomal stability. BRIP1 acts late in the Fanconi anemia pathway, after FANCD2 ubiquitination. BRIP1 is involved in the repair of DNA doublestrand breaks by homologous recombination in a manner that depends on its association with BRCA1. BRIP1 binds directly to the BRCT domains of BRCA1. BRIP1 is ubiquitously expressed, with highest levels in testis. Defects in BRIP1 are a cause of susceptibility to breast cancer (BC). BC is an extremely common malignancy, affecting one in eight women during their lifetime. A positive family history has been identified as major contributor to risk of development of the disease, and this link is striking for early-onset breast cancer. At the cellular level it is associated with hypersensitivity to DNA-damaging agents, chromosomal instability (increased chromosome breakage), and defective DNA repair.
Synonyms: FACJ (Fanconi anemia group J protein), BRCA1 (interacting protein C-terminal helicase 1)
Pathways DNA Damage Repair
Restrictions For Research Use only
Product cited in: Cantor, Drapkin, Zhang et al.: "The BRCA1-associated protein BACH1 is a DNA helicase targeted by clinically relevant inactivating mutations." in: Proceedings of the National Academy of Sciences of the United States of America, Vol. 101, Issue 8, pp. 2357-62, 2004 (PubMed).

Yu, Chini, He et al.: "The BRCT domain is a phospho-protein binding domain." in: Science (New York, N.Y.), Vol. 302, Issue 5645, pp. 639-42, 2003 (PubMed).

Background publications Beausoleil, Jedrychowski, Schwartz et al.: "Large-scale characterization of HeLa cell nuclear phosphoproteins." in: Proceedings of the National Academy of Sciences of the United States of America, Vol. 101, Issue 33, pp. 12130-5, 2004 (PubMed).

Cantor, Bell, Ganesan et al.: "BACH1, a novel helicase-like protein, interacts directly with BRCA1 and contributes to its DNA repair function." in: Cell, Vol. 105, Issue 1, pp. 149-60, 2001 (PubMed).